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 02-OCT-2024, entry version 170. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 jPOST; Q9NR99; -. DR MassIVE; Q9NR99; -. DR PaxDb; 9606-ENSP00000217939; -. DR PeptideAtlas; Q9NR99; -. DR ProteomicsDB; 82314; -. DR Pumba; Q9NR99; -. DR Antibodypedia; 362; 79 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; IPR050467; LRFN. 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. PE 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Leucine-rich repeat; Proteoglycan; KW Proteomics identification; 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 dbSNP:rs1921642741)" 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 //