PRG4_HUMAN
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 03-AUG-2022, entry version 185.
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}.
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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 GlyGen; Q92954; 120 sites, 1 N-linked glycan (1 site), 17 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; Q92954; -.
DR PeptideAtlas; Q92954; -.
DR PRIDE; 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 Antibodypedia; 34454; 182 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 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; PHMIPRP; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q92954; -.
DR TreeFam; TF332780; -.
DR PathwayCommons; Q92954; -.
DR SignaLink; Q92954; -.
DR BioGRID-ORCS; 10216; 23 hits in 1061 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 113 other tissues.
DR ExpressionAtlas; Q92954; baseline and differential.
DR Genevisible; Q92954; HS.
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; 2.110.10.10; -; 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 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; SSF50923; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
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
