ID PRG4_HUMAN Reviewed; 1404 AA. AC Q92954; Q6DNC4; Q6DNC5; Q6ZMZ5; Q9BX49; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 24-JAN-2024, entry version 193. DE RecName: Full=Proteoglycan 4; DE AltName: Full=Lubricin; DE AltName: Full=Megakaryocyte-stimulating factor; DE AltName: Full=Superficial zone proteoglycan; DE Contains: DE RecName: Full=Proteoglycan 4 C-terminal part; DE Flags: Precursor; GN Name=PRG4; Synonyms=MSF, SZP; 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] (ISOFORM A), AND VARIANTS TRP-180 AND MET-1296. RA Turner K.J., Fitz L.J., Temple P., Jacobs K., Larson D., Leary A.C., RA Kelleher K., Giannotti J., Calvetti J., Fitzgerald M., Kriz M.J., RA Ferenz C., Grobholz J., Fraser H., Bean K., Norton C.R., Gesner T., RA Bhatia S., Kriz R., Hewick R., Clark S.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E). RC TISSUE=Synovial cell; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-193 AND 1148-1398. RA Jones A.R., Hughes C.E., Flannery C.R., Caterson B.; RT "Cloning and production of recombinant PRG4/cartilage superficial zone RT proteoglycan (SZP) N- and C-terminal domains."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-90; 158-258 AND 1209-1295, AND RP IDENTIFICATION (ISOFORM C). RX PubMed=9920774; DOI=10.1006/bbrc.1998.0104; RA Flannery C.R., Hughes C.E., Schumacher B.L., Tudor D., Aydelotte M.B., RA Kuettner K.E., Caterson B.; RT "Articular cartilage superficial zone protein (SZP) is homologous to RT megakaryocyte stimulating factor precursor and is a multifunctional RT proteoglycan with potential growth-promoting, cytoprotective, and RT lubricating properties in cartilage metabolism."; RL Biochem. Biophys. Res. Commun. 254:535-541(1999). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-376 (ISOFORM F), FUNCTION, AND SUBCELLULAR RP LOCATION. RC TISSUE=Fetal liver; RX PubMed=14976050; DOI=10.1182/blood-2003-06-1825; RA Liu Y.J., Lu S.H., Xu B., Yang R.C., Ren Q., Liu B., Li B., Lu M., RA Yan F.Y., Han Z.B., Han Z.C.; RT "Hemangiopoietin, a novel human growth factor for the primitive cells of RT both hematopoietic and endothelial cell lineages."; RL Blood 103:4449-4456(2004). RN [7] RP PURIFICATION. RC TISSUE=Urine; RA Turner K.J., Fitz L.J., Temple P., Jacobs K., Larson D., Leary A.C., RA Kelleher K., Giannotti J., Calvetti J., Fitzgerald M., Kriz M.-J., RA Ferenz C., Grobholz J., Fraser H., Bean K., Norton C.R., Gesner T., RA Bhatia S., Kriz R., Hewick R., Clark S.C.; RT "Purification, biochemical characterization, and cloning of a novel RT megakaryocyte stimulating factor that has megakaryocyte colony stimulating RT activity."; RL Blood 78:279A-279A(1991). RN [8] RP GENE STRUCTURE. RA Merberg D.M., Fitz L.J., Temple P., Giannotti J., Murtha P., Fitzgerald M., RA Scaltreto H., Kelleher K., Preissner K., Kriz R., Jacobs K., Turner K.; RT "A comparison of vitronectin and megakaryocyte stimulating factor."; RL (In) Preissner K.T., Rosenblatt S., Kost C., Wegerhoff J., Mosher D.F. RL (eds.); RL Biology of vitronectins and their receptors, pp.45-52, Elsevier Science RL Publishers B.V., Amsterdam (1993). RN [9] RP GLYCOSYLATION. RX PubMed=8185311; DOI=10.1006/abbi.1994.1219; RA Schumacher B.L., Block J.A., Schmid T.M., Aydelotte M.B., Kuettner K.E.; RT "A novel proteoglycan synthesized and secreted by chondrocytes of the RT superficial zone of articular cartilage."; RL Arch. Biochem. Biophys. 311:144-152(1994). RN [10] RP TISSUE SPECIFICITY, AND INVOLVEMENT IN CACP. RX PubMed=10545950; DOI=10.1038/15496; RA Marcelino J., Carpten J.D., Suwairi W.M., Gutierrez O.M., Schwartz S., RA Robbins C., Sood R., Makalowska I., Baxevanis A., Johnstone B., Laxer R.M., RA Zemel L., Kim C.A., Herd J.K., Ihle J., Williams C., Johnson M., Raman V., RA Alonso L.G., Brunoni D., Gerstein A., Papadopoulos N., Bahabri S.A., RA Trent J.M., Warman M.L.; RT "CACP, encoding a secreted proteoglycan, is mutated in camptodactyly- RT arthropathy-coxa vara-pericarditis syndrome."; RL Nat. Genet. 23:319-322(1999). RN [11] RP TISSUE SPECIFICITY, AND IDENTIFICATION (ISOFORMS B; C AND D). RX PubMed=11124536; DOI=10.1159/000056791; RA Ikegawa S., Sano M., Koshizuka Y., Nakamura Y.; RT "Isolation, characterization and mapping of the mouse and human PRG4 RT (proteoglycan 4) genes."; RL Cytogenet. Cell Genet. 90:291-297(2000). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND GLYCOSYLATION. RX PubMed=10743795; RA Jay G.D., Britt D.E., Cha C.-J.; RT "Lubricin is a product of megakaryocyte stimulating factor gene expression RT by human synovial fibroblasts."; RL J. Rheumatol. 27:594-600(2000). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1159. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP GLYCOSYLATION AT SER-123; SER-136; THR-240; THR-253; THR-277; THR-291; RP THR-305; SER-306; THR-310; SER-317; THR-324; THR-332; THR-338; THR-367; RP SER-373; THR-376; THR-384; THR-385; SER-388; THR-391; THR-399; THR-400; RP THR-407; THR-408; THR-415; THR-423; SER-427; THR-430; THR-438; THR-439; RP THR-446; THR-447; THR-454; THR-455; THR-477; THR-478; THR-485; THR-493; RP THR-494; THR-501; THR-502; THR-509; THR-525; SER-529; THR-532; THR-540; RP THR-541; SER-553; THR-555; THR-563; THR-564; THR-571; THR-572; THR-579; RP THR-580; THR-587; THR-588; THR-595; THR-603; THR-604; THR-611; THR-612; RP THR-616; THR-619; THR-627; THR-676; THR-683; THR-684; THR-691; THR-692; RP THR-699; THR-700; THR-704; THR-707; THR-723; THR-724; THR-736; THR-768; RP THR-769; THR-776; THR-777; THR-792; THR-793; THR-805; SER-812; THR-829; RP THR-837; THR-838; SER-892; THR-900; THR-930; THR-931; SER-962; THR-963; RP THR-968; THR-975; THR-978; THR-979; THR-980; THR-1039 AND THR-1161, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25187573; DOI=10.1074/mcp.m114.040865; RA Ali L., Flowers S.A., Jin C., Bennet E.P., Ekwall A.K., Karlsson N.G.; RT "The O-glycomap of lubricin, a novel mucin responsible for joint RT lubrication, identified by site-specific glycopeptide analysis."; RL Mol. Cell. Proteomics 13:3396-3409(2014). RN [17] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=32144329; DOI=10.1038/s41598-020-61161-5; RA Huang S., Thomsson K.A., Jin C., Alweddi S., Struglics A., Rolfson O., RA Bjoerkman L.I., Kalamajski S., Schmidt T.A., Jay G.D., Krawetz R., RA Karlsson N.G., Eisler T.; RT "Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of RT Lubricin, a Synovial Mucin."; RL Sci. Rep. 10:4215-4215(2020). CC -!- FUNCTION: Plays a role in boundary lubrication within articulating CC joints. Prevents protein deposition onto cartilage from synovial fluid CC by controlling adhesion-dependent synovial growth and inhibiting the CC adhesion of synovial cells to the cartilage surface. CC -!- FUNCTION: Isoform F plays a role as a growth factor acting on the CC primitive cells of both hematopoietic and endothelial cell lineages. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14976050, CC ECO:0000269|PubMed:32144329}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=A; CC IsoId=Q92954-1; Sequence=Displayed; CC Name=B; CC IsoId=Q92954-2; Sequence=VSP_016467; CC Name=C; CC IsoId=Q92954-3; Sequence=VSP_016468; CC Name=D; CC IsoId=Q92954-4; Sequence=VSP_016467, VSP_016468; CC Name=E; CC IsoId=Q92954-5; Sequence=VSP_016467, VSP_016470; CC Name=F; Synonyms=Hemangiopoietin, HAPO; CC IsoId=Q92954-6; Sequence=VSP_016469; CC -!- TISSUE SPECIFICITY: Highly expressed in synovial tissue, cartilage and CC liver and weakly in heart and lung. Isoform B is expressed in kidney, CC lung, liver, heart and brain. Isoform C and isoform D are widely CC expressed. {ECO:0000269|PubMed:10545950, ECO:0000269|PubMed:11124536}. CC -!- PTM: N-glycosylated (PubMed:16335952). {ECO:0000269|PubMed:16335952}. CC -!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate and CC keratan sulfate. O-glycosylated with sialylated oligosaccharides which CC are predominantly represented by the monosialylated core type I CC structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of CC disialylated O-glycans (PubMed:25187573). CC {ECO:0000269|PubMed:25187573}. CC -!- PTM: The disulfide bond between Cys-1146 and Cys-1403 is essential for CC protein cleavage. {ECO:0000250}. CC -!- PTM: Proteolytically cleaved by cathepsin CTSG. CC {ECO:0000269|PubMed:32144329}. CC -!- DISEASE: Camptodactyly-arthropathy-coxa vara-pericarditis syndrome CC (CACP) [MIM:208250]: An autosomal recessive disorder characterized by CC the association of congenital or early-onset camptodactyly and non- CC inflammatory arthropathy with synovial hyperplasia. Individuals with CC CACP have normal appearing joints at birth but with advancing age CC develop joint failure, non-inflammatory synoviocyte hyperplasia and CC subintimal fibrosis of the synovial capsule. Some patients also CC manifest progressive coxa vara deformity and/or non-inflammatory CC pericardial or pleural effusions. {ECO:0000269|PubMed:10545950}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- MISCELLANEOUS: Different forms varying in molecular weight have been CC observed. Such forms are possibly due to different levels of CC glycosylation and protein cleavage (By similarity). {ECO:0000250}. 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; U70136; AAB09089.1; -; mRNA. DR EMBL; AK131434; BAD18580.1; -; mRNA. DR EMBL; AL133553; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455089; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY653037; AAT74745.1; -; mRNA. DR EMBL; AY653038; AAT74746.1; -; mRNA. DR CCDS; CCDS1369.1; -. [Q92954-1] DR CCDS; CCDS44287.1; -. [Q92954-3] DR CCDS; CCDS44288.1; -. [Q92954-2] DR CCDS; CCDS81411.1; -. [Q92954-6] DR RefSeq; NP_001121180.2; NM_001127708.2. [Q92954-2] DR RefSeq; NP_001121181.2; NM_001127709.2. [Q92954-3] DR RefSeq; NP_001121182.2; NM_001127710.2. [Q92954-4] DR RefSeq; NP_001290161.1; NM_001303232.1. [Q92954-6] DR RefSeq; NP_005798.3; NM_005807.4. [Q92954-1] DR RefSeq; XP_016855491.1; XM_017000002.1. DR RefSeq; XP_016855492.1; XM_017000003.1. DR AlphaFoldDB; Q92954; -. DR SMR; Q92954; -. DR BioGRID; 115511; 6. DR IntAct; Q92954; 6. DR MINT; Q92954; -. DR STRING; 9606.ENSP00000399679; -. DR CarbonylDB; Q92954; -. DR GlyConnect; 762; 1 N-Linked glycan (1 site), 7 O-Linked glycans (43 sites). DR GlyCosmos; Q92954; 119 sites, 18 glycans. DR GlyGen; Q92954; 120 sites, 1 N-linked glycan (1 site), 18 O-linked glycans (60 sites). DR iPTMnet; Q92954; -. DR PhosphoSitePlus; Q92954; -. DR BioMuta; PRG4; -. DR DMDM; 83288393; -. DR EPD; Q92954; -. DR jPOST; Q92954; -. DR MassIVE; Q92954; -. DR MaxQB; Q92954; -. DR PaxDb; 9606-ENSP00000399679; -. DR PeptideAtlas; Q92954; -. DR ProteomicsDB; 75624; -. [Q92954-1] DR ProteomicsDB; 75625; -. [Q92954-2] DR ProteomicsDB; 75626; -. [Q92954-3] DR ProteomicsDB; 75627; -. [Q92954-4] DR ProteomicsDB; 75628; -. [Q92954-5] DR ProteomicsDB; 75629; -. [Q92954-6] DR Pumba; Q92954; -. DR Antibodypedia; 34454; 208 antibodies from 28 providers. DR DNASU; 10216; -. DR Ensembl; ENST00000367483.8; ENSP00000356453.4; ENSG00000116690.13. [Q92954-2] DR Ensembl; ENST00000367485.4; ENSP00000356455.4; ENSG00000116690.13. [Q92954-3] DR Ensembl; ENST00000445192.7; ENSP00000399679.3; ENSG00000116690.13. [Q92954-1] DR Ensembl; ENST00000635041.1; ENSP00000489292.1; ENSG00000116690.13. [Q92954-6] DR GeneID; 10216; -. DR KEGG; hsa:10216; -. DR MANE-Select; ENST00000445192.7; ENSP00000399679.3; NM_005807.6; NP_005798.3. DR UCSC; uc001grt.5; human. [Q92954-1] DR AGR; HGNC:9364; -. DR CTD; 10216; -. DR DisGeNET; 10216; -. DR GeneCards; PRG4; -. DR HGNC; HGNC:9364; PRG4. DR HPA; ENSG00000116690; Group enriched (adipose tissue, liver). DR MalaCards; PRG4; -. DR MIM; 208250; phenotype. DR MIM; 604283; gene. DR neXtProt; NX_Q92954; -. DR OpenTargets; ENSG00000116690; -. DR Orphanet; 2848; Camptodactyly-arthropathy-coxa-vara-pericarditis syndrome. DR PharmGKB; PA33736; -. DR VEuPathDB; HostDB:ENSG00000116690; -. DR eggNOG; KOG1565; Eukaryota. DR GeneTree; ENSGT00530000063751; -. DR HOGENOM; CLU_008106_0_0_1; -. DR InParanoid; Q92954; -. DR OMA; RRITDVW; -. DR OrthoDB; 5363430at2759; -. DR PhylomeDB; Q92954; -. DR TreeFam; TF332780; -. DR PathwayCommons; Q92954; -. DR SignaLink; Q92954; -. DR BioGRID-ORCS; 10216; 23 hits in 1138 CRISPR screens. DR ChiTaRS; PRG4; human. DR GeneWiki; PRG4; -. DR GenomeRNAi; 10216; -. DR Pharos; Q92954; Tbio. DR PRO; PR:Q92954; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q92954; Protein. DR Bgee; ENSG00000116690; Expressed in synovial joint and 114 other cell types or tissues. DR ExpressionAtlas; Q92954; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR CDD; cd00094; HX; 1. DR Gene3D; 4.10.410.20; -; 2. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1. DR InterPro; IPR000585; Hemopexin-like_dom. DR InterPro; IPR036375; Hemopexin-like_dom_sf. DR InterPro; IPR018487; Hemopexin-like_repeat. DR InterPro; IPR018486; Hemopexin_CS. DR InterPro; IPR020436; SMB_chordata. DR InterPro; IPR036024; Somatomedin_B-like_dom_sf. DR InterPro; IPR001212; Somatomedin_B_dom. DR PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR22917:SF1; PROTEOGLYCAN 4; 1. DR Pfam; PF00045; Hemopexin; 1. DR Pfam; PF01033; Somatomedin_B; 2. DR PRINTS; PR00022; SOMATOMEDINB. DR SMART; SM00120; HX; 2. DR SMART; SM00201; SO; 2. DR SUPFAM; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF90188; Somatomedin B domain; 2. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 2. DR PROSITE; PS00524; SMB_1; 2. DR PROSITE; PS50958; SMB_2; 2. DR Genevisible; Q92954; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Glycoprotein; Proteoglycan; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..1404 FT /note="Proteoglycan 4" FT /id="PRO_0000043232" FT CHAIN 1307..1404 FT /note="Proteoglycan 4 C-terminal part" FT /id="PRO_0000043233" FT DOMAIN 26..69 FT /note="SMB 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DOMAIN 66..108 FT /note="SMB 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT REPEAT 348..355 FT /note="1" FT REPEAT 356..363 FT /note="2; approximate" FT REPEAT 364..371 FT /note="3" FT REPEAT 372..378 FT /note="4; approximate" FT REPEAT 379..386 FT /note="5" FT REPEAT 387..393 FT /note="6; approximate" FT REPEAT 394..401 FT /note="7" FT REPEAT 402..409 FT /note="8" FT REPEAT 410..417 FT /note="9" FT REPEAT 418..425 FT /note="10" FT REPEAT 426..432 FT /note="11; approximate" FT REPEAT 433..440 FT /note="12" FT REPEAT 441..448 FT /note="13" FT REPEAT 449..456 FT /note="14" FT REPEAT 457..464 FT /note="15" FT REPEAT 465..471 FT /note="16; approximate" FT REPEAT 472..479 FT /note="17" FT REPEAT 480..487 FT /note="18; approximate" FT REPEAT 488..495 FT /note="19; approximate" FT REPEAT 496..503 FT /note="20" FT REPEAT 504..511 FT /note="21" FT REPEAT 512..519 FT /note="22" FT REPEAT 520..527 FT /note="23" FT REPEAT 528..534 FT /note="24; approximate" FT REPEAT 535..542 FT /note="25" FT REPEAT 543..549 FT /note="26; approximate" FT REPEAT 550..557 FT /note="27" FT REPEAT 558..565 FT /note="28" FT REPEAT 566..573 FT /note="29" FT REPEAT 574..581 FT /note="30" FT REPEAT 582..589 FT /note="31" FT REPEAT 590..597 FT /note="32" FT REPEAT 598..605 FT /note="33; approximate" FT REPEAT 606..613 FT /note="34" FT REPEAT 614..621 FT /note="35; approximate" FT REPEAT 622..629 FT /note="36; approximate" FT REPEAT 638..645 FT /note="37; approximate" FT REPEAT 662..669 FT /note="38; approximate" FT REPEAT 678..685 FT /note="39" FT REPEAT 686..693 FT /note="40" FT REPEAT 694..701 FT /note="41" FT REPEAT 702..709 FT /note="42; approximate" FT REPEAT 710..717 FT /note="43; approximate" FT REPEAT 718..725 FT /note="44" FT REPEAT 731..738 FT /note="45; approximate" FT REPEAT 739..746 FT /note="46; approximate" FT REPEAT 747..754 FT /note="47; approximate" FT REPEAT 755..762 FT /note="48; approximate" FT REPEAT 763..770 FT /note="49" FT REPEAT 771..778 FT /note="50" FT REPEAT 779..786 FT /note="51; approximate" FT REPEAT 787..794 FT /note="52" FT REPEAT 800..807 FT /note="53; approximate" FT REPEAT 808..815 FT /note="54; approximate" FT REPEAT 816..823 FT /note="55; approximate" FT REPEAT 824..831 FT /note="56; approximate" FT REPEAT 832..839 FT /note="57" FT REPEAT 840..847 FT /note="58" FT REPEAT 848..855 FT /note="59; approximate" FT REPEAT 1148..1191 FT /note="Hemopexin 1" FT REPEAT 1192..1239 FT /note="Hemopexin 2" FT REGION 111..966 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 348..855 FT /note="59 X 8 AA repeats of K-X-P-X-P-T-T-X" FT REGION 992..1104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..160 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..185 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..200 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 231..256 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..300 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 301..315 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..362 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..396 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 397..416 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..432 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 433..521 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 522..552 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 553..615 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 616..632 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 633..703 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 704..719 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 736..754 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 755..777 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 805..823 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 824..854 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 855..879 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 926..966 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1029..1049 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1050..1089 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1306..1307 FT /note="Cleavage; by subtilisin-like proprotein convertase FT 4" FT /evidence="ECO:0000250" FT CARBOHYD 123 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 136 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 206 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 253 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 277 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 291 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 305 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 306 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 310 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 317 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 324 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 332 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 338 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 367 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 373 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 376 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 384 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 385 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 388 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 391 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 399 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 400 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 407 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 408 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 415 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 423 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 427 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 430 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 438 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 439 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 446 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 447 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 454 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 455 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 477 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 478 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 485 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 493 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 494 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 501 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 502 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 509 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 525 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 529 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 532 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 540 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 541 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 553 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 555 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 563 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 564 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 571 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 572 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 579 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 580 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 587 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 588 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 595 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 603 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 604 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 611 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 612 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 616 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 619 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 627 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 676 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 683 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 684 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 691 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 692 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 699 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 700 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 704 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 707 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 723 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 724 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 736 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 768 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 769 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 776 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 777 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 792 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 793 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 805 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 812 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 829 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 837 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 838 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 892 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 900 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 930 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 931 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 962 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 963 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 968 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 975 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 978 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 979 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 980 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 1039 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT CARBOHYD 1159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1161 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:25187573" FT DISULFID 30..46 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 30..34 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 34..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 44..57 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 44..46 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 50..56 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 57..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 70..86 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 70..74 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 74..104 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 84..97 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 84..86 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 90..96 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 97..104 FT /note="Alternate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT DISULFID 1146..1403 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350" FT VAR_SEQ 26..66 FT /note="Missing (in isoform B, isoform D and isoform E)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016467" FT VAR_SEQ 107..199 FT /note="Missing (in isoform C and isoform D)" FT /evidence="ECO:0000305" FT /id="VSP_016468" FT VAR_SEQ 157..199 FT /note="Missing (in isoform F)" FT /evidence="ECO:0000303|PubMed:14976050" FT /id="VSP_016469" FT VAR_SEQ 412..841 FT /note="Missing (in isoform E)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016470" FT VARIANT 180 FT /note="R -> W (in dbSNP:rs2273779)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_024023" FT VARIANT 1130 FT /note="N -> S (in dbSNP:rs10158395)" FT /id="VAR_051559" FT VARIANT 1272 FT /note="I -> T (in dbSNP:rs1293985)" FT /id="VAR_051560" FT VARIANT 1296 FT /note="T -> M (in dbSNP:rs12134934)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_051561" FT CONFLICT 604 FT /note="T -> A (in Ref. 1; AAB09089)" FT /evidence="ECO:0000305" FT CONFLICT 1340 FT /note="S -> G (in Ref. 4; AAT74746)" FT /evidence="ECO:0000305" FT CONFLICT 1380 FT /note="V -> G (in Ref. 4; AAT74746)" FT /evidence="ECO:0000305" FT CONFLICT 1397..1404 FT /note="SKVWYNCP -> FK (in Ref. 4; AAT74746)" FT /evidence="ECO:0000305" SQ SEQUENCE 1404 AA; 151061 MW; 7FE71EA184B03972 CRC64; MAWKTLPIYL LLLLSVFVIQ QVSSQDLSSC AGRCGEGYSR DATCNCDYNC QHYMECCPDF KRVCTAELSC KGRCFESFER GRECDCDAQC KKYDKCCPDY ESFCAEVHNP TSPPSSKKAP PPSGASQTIK STTKRSPKPP NKKKTKKVIE SEEITEEHSV SENQESSSSS SSSSSSSTIR KIKSSKNSAA NRELQKKLKV KDNKKNRTKK KPTPKPPVVD EAGSGLDNGD FKVTTPDTST TQHNKVSTSP KITTAKPINP RPSLPPNSDT SKETSLTVNK ETTVETKETT TTNKQTSTDG KEKTTSAKET QSIEKTSAKD LAPTSKVLAK PTPKAETTTK GPALTTPKEP TPTTPKEPAS TTPKEPTPTT IKSAPTTPKE PAPTTTKSAP TTPKEPAPTT TKEPAPTTPK EPAPTTTKEP APTTTKSAPT TPKEPAPTTP KKPAPTTPKE PAPTTPKEPT PTTPKEPAPT TKEPAPTTPK EPAPTAPKKP APTTPKEPAP TTPKEPAPTT TKEPSPTTPK EPAPTTTKSA PTTTKEPAPT TTKSAPTTPK EPSPTTTKEP APTTPKEPAP TTPKKPAPTT PKEPAPTTPK EPAPTTTKKP APTTPKEPAP TTPKETAPTT PKKLTPTTPE KLAPTTPEKP APTTPEELAP TTPEEPTPTT PEEPAPTTPK AAAPNTPKEP APTTPKEPAP TTPKEPAPTT PKETAPTTPK GTAPTTLKEP APTTPKKPAP KELAPTTTKE PTSTTSDKPA PTTPKGTAPT TPKEPAPTTP KEPAPTTPKG TAPTTLKEPA PTTPKKPAPK ELAPTTTKGP TSTTSDKPAP TTPKETAPTT PKEPAPTTPK KPAPTTPETP PPTTSEVSTP TTTKEPTTIH KSPDESTPEL SAEPTPKALE NSPKEPGVPT TKTPAATKPE MTTTAKDKTT ERDLRTTPET TTAAPKMTKE TATTTEKTTE SKITATTTQV TSTTTQDTTP FKITTLKTTT LAPKVTTTKK TITTTEIMNK PEETAKPKDR ATNSKATTPK PQKPTKAPKK PTSTKKPKTM PRVRKPKTTP TPRKMTSTMP ELNPTSRIAE AMLQTTTRPN QTPNSKLVEV NPKSEDAGGA EGETPHMLLR PHVFMPEVTP DMDYLPRVPN QGIIINPMLS DETNICNGKP VDGLTTLRNG TLVAFRGHYF WMLSPFSPPS PARRITEVWG IPSPIDTVFT RCNCEGKTFF FKDSQYWRFT NDIKDAGYPK PIFKGFGGLT GQIVAALSTA KYKNWPESVY FFKRGGSIQQ YIYKQEPVQK CPGRRPALNY PVYGETTQVR RRRFERAIGP SQTHTIRIQY SPARLAYQDK GVLHNEVKVS ILWRGLPNVV TSAISLPNIR KPDGYDYYAF SKDQYYNIDV PSRTARAITT RSGQTLSKVW YNCP //