ID   MXRA5_HUMAN             Reviewed;        2828 AA.
AC   Q9NR99; Q6P1M7; Q9Y3Y8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Matrix-remodeling-associated protein 5;
DE   AltName: Full=Adhesion protein with leucine-rich repeats and immunoglobulin domains related to perlecan;
DE            Short=Adlican;
DE   Flags: Precursor;
GN   Name=MXRA5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-824; VAL-1128; ASP-1394;
RP   SER-2000 AND VAL-2531.
RC   TISSUE=Placenta;
RA   Crowl R.M., Luk D.;
RT   "Identification of the gene encoding adlican, a novel protein expressed in
RT   human arthritic tissues.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=15609104; DOI=10.1007/s10522-004-3188-1;
RA   Chondrogianni N., Simoes D.C.M., Franceschi C., Gonos E.S.;
RT   "Cloning of differentially expressed genes in skin fibroblasts from
RT   centenarians.";
RL   Biogerontology 5:401-409(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-739.
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2245-2828.
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-702.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [7]
RP   FUNCTION, INDUCTION BY TGFB1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=27599751; DOI=10.1111/jcmm.12953;
RA   Poveda J., Sanz A.B., Fernandez-Fernandez B., Carrasco S., Ruiz-Ortega M.,
RA   Cannata-Ortiz P., Ortiz A., Sanchez-Nino M.D.;
RT   "MXRA5 is a TGF-beta1-regulated human protein with anti-inflammatory and
RT   anti-fibrotic properties.";
RL   J. Cell. Mol. Med. 21:154-164(2017).
RN   [8]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-702.
RX   PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA   Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA   Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA   Larson G., Salanti A., Clausen T.M.;
RT   "An affinity chromatography and glycoproteomics workflow to profile the
RT   chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT   the placenta and in cancer.";
RL   Glycobiology 30:989-1002(2020).
RN   [9]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-702.
RX   PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA   Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA   Pandey A.;
RT   "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL   J. Proteins Proteom. 13:187-203(2022).
RN   [10]
RP   VARIANTS LNCR ASP-98; HIS-481; CYS-611; ASN-862; PHE-1028; ALA-1491;
RP   HIS-2300; TRP-2349; ARG-2678; ALA-2716 AND GLY-2763.
RX   PubMed=22696596; DOI=10.1093/carcin/bgs210;
RA   Xiong D., Li G., Li K., Xu Q., Pan Z., Ding F., Vedell P., Liu P., Cui P.,
RA   Hua X., Jiang H., Yin Y., Zhu Z., Li X., Zhang B., Ma D., Wang Y., You M.;
RT   "Exome sequencing identifies MXRA5 as a novel cancer gene frequently
RT   mutated in non-small cell lung carcinoma from Chinese patients.";
RL   Carcinogenesis 33:1797-1805(2012).
RN   [11]
RP   VARIANTS HIS-1163 AND TRP-2663.
RX   PubMed=23092983; DOI=10.1038/tp.2012.102;
RA   Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA   Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA   Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA   Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA   Brice A., Depienne C.;
RT   "Analysis of the chromosome X exome in patients with autism spectrum
RT   disorders identified novel candidate genes, including TMLHE.";
RL   Transl. Psychiatry 2:E179-E179(2012).
RN   [12]
RP   VARIANT ASP-2426.
RX   PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA   Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA   Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT   "Homozygous missense mutation in the LMAN2L gene segregates with
RT   intellectual disability in a large consanguineous Pakistani family.";
RL   J. Med. Genet. 53:138-144(2016).
CC   -!- FUNCTION: In kidney, has anti-inflammatory and anti-fibrotic properties
CC       by limiting the induction of chemokines, fibronectin and collagen
CC       expression in response to TGB1 and pro-inflammatory stimuli.
CC       {ECO:0000269|PubMed:27599751}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:27599751}.
CC   -!- TISSUE SPECIFICITY: Detected in placenta (at protein level)
CC       (PubMed:32337544). Detected in cerebrospinal fluid and fibroblasts (at
CC       protein level) (PubMed:25326458, PubMed:36213313). Highly expressed in
CC       kidney, also detected on liver and spleen (PubMed:27599751). Expressed
CC       by proximal tubular cells of the kidney (at protein level)
CC       (PubMed:27599751). Expression highly increases during chronic kidney
CC       disease and autosomal dominant polycystic kidney disease, where is
CC       detected in cysts (PubMed:27599751). {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:27599751, ECO:0000269|PubMed:32337544,
CC       ECO:0000269|PubMed:36213313}.
CC   -!- DEVELOPMENTAL STAGE: Over-expressed in centenarians. Expression is
CC       reduced from young to old but increased from old to centenarians.
CC       {ECO:0000269|PubMed:15609104}.
CC   -!- INDUCTION: Expression is induced by TGFB1, in kidney tubular cells.
CC       This induction is inhibited by the vitamin D receptor activator
CC       paricalcitol (at protein level). {ECO:0000269|PubMed:27599751}.
CC   -!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting
CC       tissues of the lung. The most common form of lung cancer is non-small
CC       cell lung cancer (NSCLC) that can be divided into 3 major histologic
CC       subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung
CC       cancer. NSCLC is often diagnosed at an advanced stage and has a poor
CC       prognosis. {ECO:0000269|PubMed:22696596}. Note=Disease susceptibility
CC       may be associated with variants affecting the gene represented in this
CC       entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAH64986.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAH80586.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF245505; AAF86402.1; -; mRNA.
DR   EMBL; AC004616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011846; AAH11846.1; ALT_SEQ; mRNA.
DR   EMBL; BC064986; AAH64986.1; ALT_SEQ; mRNA.
DR   EMBL; BC080586; AAH80586.1; ALT_SEQ; mRNA.
DR   EMBL; AL049946; CAB43220.1; -; mRNA.
DR   CCDS; CCDS14124.1; -.
DR   PIR; T08678; T08678.
DR   RefSeq; NP_056234.2; NM_015419.3.
DR   BioGRID; 117392; 9.
DR   IntAct; Q9NR99; 4.
DR   STRING; 9606.ENSP00000217939; -.
DR   GlyConnect; 1495; 24 N-Linked glycans (7 sites).
DR   GlyCosmos; Q9NR99; 24 sites, 27 glycans.
DR   GlyGen; Q9NR99; 32 sites, 23 N-linked glycans (7 sites), 5 O-linked glycans (20 sites).
DR   iPTMnet; Q9NR99; -.
DR   PhosphoSitePlus; Q9NR99; -.
DR   BioMuta; MXRA5; -.
DR   DMDM; 317373412; -.
DR   EPD; Q9NR99; -.
DR   jPOST; Q9NR99; -.
DR   MassIVE; Q9NR99; -.
DR   PaxDb; 9606-ENSP00000217939; -.
DR   PeptideAtlas; Q9NR99; -.
DR   ProteomicsDB; 82314; -.
DR   Pumba; Q9NR99; -.
DR   Antibodypedia; 362; 89 antibodies from 22 providers.
DR   DNASU; 25878; -.
DR   Ensembl; ENST00000217939.7; ENSP00000217939.5; ENSG00000101825.8.
DR   GeneID; 25878; -.
DR   KEGG; hsa:25878; -.
DR   MANE-Select; ENST00000217939.7; ENSP00000217939.5; NM_015419.4; NP_056234.2.
DR   UCSC; uc004crg.6; human.
DR   AGR; HGNC:7539; -.
DR   CTD; 25878; -.
DR   DisGeNET; 25878; -.
DR   GeneCards; MXRA5; -.
DR   HGNC; HGNC:7539; MXRA5.
DR   HPA; ENSG00000101825; Tissue enhanced (cervix).
DR   MalaCards; MXRA5; -.
DR   MIM; 211980; phenotype.
DR   MIM; 300938; gene.
DR   neXtProt; NX_Q9NR99; -.
DR   OpenTargets; ENSG00000101825; -.
DR   PharmGKB; PA31340; -.
DR   VEuPathDB; HostDB:ENSG00000101825; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000159942; -.
DR   HOGENOM; CLU_000580_0_0_1; -.
DR   InParanoid; Q9NR99; -.
DR   OMA; KMNCMAM; -.
DR   OrthoDB; 2918193at2759; -.
DR   PhylomeDB; Q9NR99; -.
DR   TreeFam; TF326318; -.
DR   PathwayCommons; Q9NR99; -.
DR   SignaLink; Q9NR99; -.
DR   BioGRID-ORCS; 25878; 8 hits in 771 CRISPR screens.
DR   ChiTaRS; MXRA5; human.
DR   GeneWiki; MXRA5; -.
DR   GenomeRNAi; 25878; -.
DR   Pharos; Q9NR99; Tbio.
DR   PRO; PR:Q9NR99; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9NR99; Protein.
DR   Bgee; ENSG00000101825; Expressed in tendon of biceps brachii and 174 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0071559; P:response to transforming growth factor beta; IMP:UniProtKB.
DR   CDD; cd00096; Ig; 4.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 12.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   PANTHER; PTHR45842:SF12; KEKKON 5, ISOFORM A; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR   Pfam; PF07679; I-set; 6.
DR   Pfam; PF13927; Ig_3; 5.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00409; IG; 12.
DR   SMART; SM00408; IGc2; 12.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 12.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 12.
DR   Genevisible; Q9NR99; HS.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..2828
FT                   /note="Matrix-remodeling-associated protein 5"
FT                   /id="PRO_0000254131"
FT   DOMAIN          27..55
FT                   /note="LRRNT"
FT   REPEAT          56..77
FT                   /note="LRR 1"
FT   REPEAT          80..101
FT                   /note="LRR 2"
FT   REPEAT          104..125
FT                   /note="LRR 3"
FT   REPEAT          128..149
FT                   /note="LRR 4"
FT   REPEAT          152..173
FT                   /note="LRR 5"
FT   REPEAT          184..205
FT                   /note="LRR 6"
FT   DOMAIN          217..277
FT                   /note="LRRCT"
FT   DOMAIN          481..571
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          575..669
FT                   /note="Ig-like C2-type 2"
FT   REPEAT          1410..1434
FT                   /note="LRR 7"
FT   DOMAIN          1853..1946
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          1950..2041
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          2046..2140
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          2146..2239
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          2242..2343
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          2345..2432
FT                   /note="Ig-like C2-type 8"
FT   DOMAIN          2440..2534
FT                   /note="Ig-like C2-type 9"
FT   DOMAIN          2542..2630
FT                   /note="Ig-like C2-type 10"
FT   DOMAIN          2637..2722
FT                   /note="Ig-like C2-type 11"
FT   DOMAIN          2733..2828
FT                   /note="Ig-like C2-type 12"
FT   REGION          671..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1479..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1536..1566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1579..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1669..1689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1700..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1119..1147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1148..1168
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        702
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313"
FT   CARBOHYD        1403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1735
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2007
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2056
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        501..555
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        599..651
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1875..1928
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1972..2025
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2069..2122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2168..2221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2265..2324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2368..2418
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2466..2518
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2564..2616
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2659..2711
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2755..2810
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         98
FT                   /note="A -> D (in LNCR; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072405"
FT   VARIANT         481
FT                   /note="P -> H (in LNCR; uncertain significance;
FT                   dbSNP:rs759222135)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072406"
FT   VARIANT         611
FT                   /note="W -> C (in LNCR; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072407"
FT   VARIANT         764
FT                   /note="V -> L (in dbSNP:rs5983120)"
FT                   /id="VAR_056057"
FT   VARIANT         824
FT                   /note="I -> V (in dbSNP:rs5983119)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_060357"
FT   VARIANT         862
FT                   /note="S -> N (in LNCR)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072408"
FT   VARIANT         1028
FT                   /note="V -> F (in LNCR; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072409"
FT   VARIANT         1128
FT                   /note="A -> V (in dbSNP:rs1635246)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_060358"
FT   VARIANT         1163
FT                   /note="R -> H (in dbSNP:rs139106444)"
FT                   /evidence="ECO:0000269|PubMed:23092983"
FT                   /id="VAR_076257"
FT   VARIANT         1394
FT                   /note="G -> D (in dbSNP:rs1726199)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_060359"
FT   VARIANT         1484
FT                   /note="T -> A (in dbSNP:rs12396910)"
FT                   /id="VAR_056058"
FT   VARIANT         1491
FT                   /note="P -> A (in LNCR; uncertain significance;
FT                   dbSNP:rs754393038)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072410"
FT   VARIANT         1665
FT                   /note="P -> S (in dbSNP:rs1974522)"
FT                   /id="VAR_056059"
FT   VARIANT         2000
FT                   /note="G -> S (in dbSNP:rs1635242)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_060360"
FT   VARIANT         2300
FT                   /note="R -> H (in LNCR; uncertain significance;
FT                   dbSNP:rs776590689)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072411"
FT   VARIANT         2349
FT                   /note="R -> W (in LNCR; uncertain significance;
FT                   dbSNP:rs369042203)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072412"
FT   VARIANT         2426
FT                   /note="E -> D (in dbSNP:rs148675322)"
FT                   /evidence="ECO:0000269|PubMed:26566883"
FT                   /id="VAR_076437"
FT   VARIANT         2531
FT                   /note="L -> V (in dbSNP:rs1726208)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_028821"
FT   VARIANT         2663
FT                   /note="G -> W (in dbSNP:rs143264543)"
FT                   /evidence="ECO:0000269|PubMed:23092983"
FT                   /id="VAR_076258"
FT   VARIANT         2678
FT                   /note="H -> R (in LNCR; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072413"
FT   VARIANT         2716
FT                   /note="E -> A (in LNCR; uncertain significance;
FT                   dbSNP:rs1419255508)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072414"
FT   VARIANT         2763
FT                   /note="A -> G (in LNCR; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22696596"
FT                   /id="VAR_072415"
FT   CONFLICT        55
FT                   /note="K -> R (in Ref. 1; AAF86402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1565
FT                   /note="Q -> R (in Ref. 1; AAF86402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2245
FT                   /note="I -> V (in Ref. 5; CAB43220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2353
FT                   /note="Y -> C (in Ref. 5; CAB43220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2640
FT                   /note="N -> S (in Ref. 5; CAB43220)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2828 AA;  312150 MW;  0534732CE87C9A8F CRC64;
     MPKRAHWGAL SVVLILLWGH PRVALACPHP CACYVPSEVH CTFRSLASVP AGIAKHVERI
     NLGFNSIQAL SETSFAGLTK LELLMIHGNE IPSIPDGALR DLSSLQVFKF SYNKLRVITG
     QTLQGLSNLM RLHIDHNKIE FIHPQAFNGL TSLRLLHLEG NLLHQLHPST FSTFTFLDYF
     RLSTIRHLYL AENMVRTLPA SMLRNMPLLE NLYLQGNPWT CDCEMRWFLE WDAKSRGILK
     CKKDKAYEGG QLCAMCFSPK KLYKHEIHKL KDMTCLKPSI ESPLRQNRSR SIEEEQEQEE
     DGGSQLILEK FQLPQWSISL NMTDEHGNMV NLVCDIKKPM DVYKIHLNQT DPPDIDINAT
     VALDFECPMT RENYEKLWKL IAYYSEVPVK LHRELMLSKD PRVSYQYRQD ADEEALYYTG
     VRAQILAEPE WVMQPSIDIQ LNRRQSTAKK VLLSYYTQYS QTISTKDTRQ ARGRSWVMIE
     PSGAVQRDQT VLEGGPCQLS CNVKASESPS IFWVLPDGSI LKAPMDDPDS KFSILSSGWL
     RIKSMEPSDS GLYQCIAQVR DEMDRMVYRV LVQSPSTQPA EKDTVTIGKN PGESVTLPCN
     ALAIPEAHLS WILPNRRIIN DLANTSHVYM LPNGTLSIPK VQVSDSGYYR CVAVNQQGAD
     HFTVGITVTK KGSGLPSKRG RRPGAKALSR VREDIVEDEG GSGMGDEENT SRRLLHPKDQ
     EVFLKTKDDA INGDKKAKKG RRKLKLWKHS EKEPETNVAE GRRVFESRRR INMANKQINP
     ERWADILAKV RGKNLPKGTE VPPLIKTTSP PSLSLEVTPP FPAISPPSAS PVQTVTSAEE
     SSADVPLLGE EEHVLGTISS ASMGLEHNHN GVILVEPEVT STPLEEVVDD LSEKTEEITS
     TEGDLKGTAA PTLISEPYEP SPTLHTLDTV YEKPTHEETA TEGWSAADVG SSPEPTSSEY
     EPPLDAVSLA ESEPMQYFDP DLETKSQPDE DKMKEDTFAH LTPTPTIWVN DSSTSQLFED
     STIGEPGVPG QSHLQGLTDN IHLVKSSLST QDTLLIKKGM KEMSQTLQGG NMLEGDPTHS
     RSSESEGQES KSITLPDSTL GIMSSMSPVK KPAETTVGTL LDKDTTTATT TPRQKVAPSS
     TMSTHPSRRR PNGRRRLRPN KFRHRHKQTP PTTFAPSETF STQPTQAPDI KISSQVESSL
     VPTAWVDNTV NTPKQLEMEK NAEPTSKGTP RRKHGKRPNK HRYTPSTVSS RASGSKPSPS
     PENKHRNIVT PSSETILLPR TVSLKTEGPY DSLDYMTTTR KIYSSYPKVQ ETLPVTYKPT
     SDGKEIKDDV ATNVDKHKSD ILVTGESITN AIPTSRSLVS TMGEFKEESS PVGFPGTPTW
     NPSRTAQPGR LQTGIPVTTS GENLTDPPLL KELEDVDFTS EFLSSLTVST PFHQEEAGSS
     TTLSSIKVEV ASSQAETTTL DQDHLETTVA ILLSETRPQN HTPTAARMKE PASSSPSTIL
     MSLGQTTTTK PALPSPRISQ ASRDSKENVF LNYVGNPETE ATPVNNEGTQ HMSGPNELST
     PSSDQDAFNL STKLELEKQV FGSRSLPRGP DSQRQDGRVH ASHQLTRVPA KPILPTATVR
     LPEMSTQSAS RYFVTSQSPR HWTNKPEITT YPSGALPENK QFTTPRLSST TIPLPLHMSK
     PSIPSKFTDR RTDQFNGYSK VFGNNNIPEA RNPVGKPPSP RIPHYSNGRL PFFTNKTLSF
     PQLGVTRRPQ IPTSPAPVMR ERKVIPGSYN RIHSHSTFHL DFGPPAPPLL HTPQTTGSPS
     TNLQNIPMVS STQSSISFIT SSVQSSGSFH QSSSKFFAGG PPASKFWSLG EKPQILTKSP
     QTVSVTAETD TVFPCEATGK PKPFVTWTKV STGALMTPNT RIQRFEVLKN GTLVIRKVQV
     QDRGQYMCTA SNLHGLDRMV VLLSVTVQQP QILASHYQDV TVYLGDTIAM ECLAKGTPAP
     QISWIFPDRR VWQTVSPVEG RITLHENRTL SIKEASFSDR GVYKCVASNA AGADSLAIRL
     HVAALPPVIH QEKLENISLP PGLSIHIHCT AKAAPLPSVR WVLGDGTQIR PSQFLHGNLF
     VFPNGTLYIR NLAPKDSGRY ECVAANLVGS ARRTVQLNVQ RAAANARITG TSPRRTDVRY
     GGTLKLDCSA SGDPWPRILW RLPSKRMIDA LFSFDSRIKV FANGTLVVKS VTDKDAGDYL
     CVARNKVGDD YVVLKVDVVM KPAKIEHKEE NDHKVFYGGD LKVDCVATGL PNPEISWSLP
     DGSLVNSFMQ SDDSGGRTKR YVVFNNGTLY FNEVGMREEG DYTCFAENQV GKDEMRVRVK
     VVTAPATIRN KTYLAVQVPY GDVVTVACEA KGEPMPKVTW LSPTNKVIPT SSEKYQIYQD
     GTLLIQKAQR SDSGNYTCLV RNSAGEDRKT VWIHVNVQPP KINGNPNPIT TVREIAAGGS
     RKLIDCKAEG IPTPRVLWAF PEGVVLPAPY YGNRITVHGN GSLDIRSLRK SDSVQLVCMA
     RNEGGEARLI LQLTVLEPME KPIFHDPISE KITAMAGHTI SLNCSAAGTP TPSLVWVLPN
     GTDLQSGQQL QRFYHKADGM LHISGLSSVD AGAYRCVARN AAGHTERLVS LKVGLKPEAN
     KQYHNLVSII NGETLKLPCT PPGAGQGRFS WTLPNGMHLE GPQTLGRVSL LDNGTLTVRE
     ASVFDRGTYV CRMETEYGPS VTSIPVIVIA YPPRITSEPT PVIYTRPGNT VKLNCMAMGI
     PKADITWELP DKSHLKAGVQ ARLYGNRFLH PQGSLTIQHA TQRDAGFYKC MAKNILGSDS
     KTTYIHVF
//