COMP_MOUSE
ID COMP_MOUSE Reviewed; 755 AA.
AC Q9R0G6; G3X8Q4;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cartilage oligomeric matrix protein {ECO:0000305};
DE Short=COMP;
DE Flags: Precursor;
GN Name=Comp {ECO:0000312|MGI:MGI:88469};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cartilage;
RX PubMed=11052496; DOI=10.1002/jor.1100180412;
RA Fang C., Carlson C.S., Leslie M.P., Tulli H., Stolerman E., Perris R.,
RA Ni L., Di Cesare P.E.;
RT "Molecular cloning, sequencing, and tissue and developmental expression of
RT mouse cartilage oligomeric matrix protein (COMP).";
RL J. Orthop. Res. 18:593-603(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21624478; DOI=10.1016/j.joca.2011.04.016;
RA Heinonen J., Taipaleenmaeki H., Roering P., Takatalo M., Harkness L.,
RA Sandholm J., Uusitalo-Jaervinen H., Kassem M., Kiviranta I.,
RA Laitala-Leinonen T., Saeaemaenen A.M.;
RT "Snorc is a novel cartilage specific small membrane proteoglycan expressed
RT in differentiating and articular chondrocytes.";
RL Osteoarthritis Cartilage 19:1026-1035(2011).
RN [6]
RP FUNCTION, MUTAGENESIS OF VAL-65, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=32686688; DOI=10.1038/s41467-020-17378-z;
RA Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L.,
RA Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S.,
RA Yang Y., Gao B.;
RT "Mutations in COMP cause familial carpal tunnel syndrome.";
RL Nat. Commun. 11:3642-3642(2020).
RN [7]
RP ERRATUM OF PUBMED:32747625.
RX PubMed=32747625; DOI=10.1038/s41467-020-17845-7;
RA Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L.,
RA Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S.,
RA Yang Y., Gao B.;
RT "Author Correction: Mutations in COMP cause familial carpal tunnel
RT syndrome.";
RL Nat. Commun. 11:3931-3931(2020).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-71, AND DISULFIDE BONDS.
RX PubMed=12426368; DOI=10.1093/emboj/cdf628;
RA Ozbek S., Engel J., Stetefeld J.;
RT "Storage function of cartilage oligomeric matrix protein: the crystal
RT structure of the coiled-coil domain in complex with vitamin D(3).";
RL EMBO J. 21:5960-5968(2002).
CC -!- FUNCTION: Plays a role in the structural integrity of cartilage via its
CC interaction with other extracellular matrix proteins such as the
CC collagens and fibronectin (PubMed:32686688). Can mediate the
CC interaction of chondrocytes with the cartilage extracellular matrix
CC through interaction with cell surface integrin receptors. Could play a
CC role in the pathogenesis of osteoarthritis. Potent suppressor of
CC apoptosis in both primary chondrocytes and transformed cells.
CC Suppresses apoptosis by blocking the activation of caspase-3 and by
CC inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and
CC XIAP) (By similarity). Essential for maintaining a vascular smooth
CC muscle cells (VSMCs) contractile/differentiated phenotype under
CC physiological and pathological stimuli. Maintains this phenotype of
CC VSMCs by interacting with ITGA7 (By similarity).
CC {ECO:0000250|UniProtKB:P35444, ECO:0000250|UniProtKB:P49747,
CC ECO:0000269|PubMed:32686688}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P49747};
CC Note=Binds 11-14 calcium ions per subunit.
CC {ECO:0000250|UniProtKB:P49747};
CC -!- SUBUNIT: Pentamer; disulfide-linked. Exists in a more compact
CC conformation in the presence of calcium and shows a more extended
CC conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and
CC FN1. Binding to FN1 requires the presence of divalent cations (Ca(2+),
CC Mg(2+) or Mn(2+)). The greatest amount of binding is seen in the
CC presence of Mn(2+). Interacts with MATN1, MATN3, MATN4 and ACAN. Binds
CC heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes
CC significantly its binding to ACAN and abolishes its binding to MATN3,
CC MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX,
CC and interaction with these collagens is dependent on the presence of
CC zinc ions. Interacts with ADAMTS12 (By similarity). Interacts with
CC ITGA7 (By similarity). {ECO:0000250|UniProtKB:P35444,
CC ECO:0000250|UniProtKB:P49747}.
CC -!- INTERACTION:
CC Q9R0G6; P58397: ADAMTS12; Xeno; NbExp=3; IntAct=EBI-9028018, EBI-9028051;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:32686688}.
CC -!- TISSUE SPECIFICITY: Expressed in cartilage, including nasal, knee
CC epiphyseal and rib tissues. Abundantly expressed in chondrocyte and
CC tendon extracellular matrix (at protein level) (PubMed:32686688).
CC {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:32686688}.
CC -!- DEVELOPMENTAL STAGE: In knee epiphyseal cartilage, expression is
CC detected from 12.5 dpc onwards, with significant up-regulation at 16.5
CC dpc and again at postnatal day 5. Expressed at least until 10 months of
CC age. {ECO:0000269|PubMed:21624478}.
CC -!- DOMAIN: The cell attachment motif mediates the attachment to
CC chondrocytes. It mediates the induction of both the IAP family of
CC survival proteins and the antiapoptotic response.
CC {ECO:0000250|UniProtKB:P49747}.
CC -!- DOMAIN: The TSP C-terminal domain mediates interaction with FN1 and
CC ACAN. {ECO:0000250|UniProtKB:P49747}.
CC -!- DOMAIN: Each of the eight TSP type-3 repeats binds two calcium ions.
CC The TSP C-terminal domain binds three calcium ions.
CC {ECO:0000250|UniProtKB:P49747}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; AF033530; AAD01972.1; -; mRNA.
DR EMBL; AC158553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466569; EDL28815.1; -; Genomic_DNA.
DR CCDS; CCDS22367.1; -.
DR RefSeq; NP_057894.2; NM_016685.2.
DR PDB; 1MZ9; X-ray; 1.70 A; A/B/C/D/E=28-71.
DR PDB; 3V2N; X-ray; 1.80 A; A/B/C/D/E=28-71.
DR PDB; 3V2P; X-ray; 1.87 A; A/B/C/D/E=28-71.
DR PDB; 3V2Q; X-ray; 2.20 A; A/B/C/D/E=28-71.
DR PDB; 3V2R; X-ray; 2.75 A; A/B/C/D/E=28-71.
DR PDBsum; 1MZ9; -.
DR PDBsum; 3V2N; -.
DR PDBsum; 3V2P; -.
DR PDBsum; 3V2Q; -.
DR PDBsum; 3V2R; -.
DR AlphaFoldDB; Q9R0G6; -.
DR SMR; Q9R0G6; -.
DR BioGRID; 198833; 23.
DR ComplexPortal; CPX-3026; Thrombospondin 5 complex.
DR IntAct; Q9R0G6; 2.
DR STRING; 10090.ENSMUSP00000003659; -.
DR GlyGen; Q9R0G6; 2 sites.
DR iPTMnet; Q9R0G6; -.
DR PhosphoSitePlus; Q9R0G6; -.
DR CPTAC; non-CPTAC-3351; -.
DR MaxQB; Q9R0G6; -.
DR PaxDb; Q9R0G6; -.
DR PRIDE; Q9R0G6; -.
DR ProteomicsDB; 283790; -.
DR ABCD; Q9R0G6; 1 sequenced antibody.
DR Antibodypedia; 15160; 398 antibodies from 30 providers.
DR DNASU; 12845; -.
DR Ensembl; ENSMUST00000003659; ENSMUSP00000003659; ENSMUSG00000031849.
DR GeneID; 12845; -.
DR KEGG; mmu:12845; -.
DR UCSC; uc009mad.2; mouse.
DR CTD; 1311; -.
DR MGI; MGI:88469; Comp.
DR VEuPathDB; HostDB:ENSMUSG00000031849; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000162169; -.
DR HOGENOM; CLU_009257_1_1_1; -.
DR InParanoid; Q9R0G6; -.
DR OMA; RSQRFCP; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; Q9R0G6; -.
DR TreeFam; TF324917; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 12845; 3 hits in 77 CRISPR screens.
DR EvolutionaryTrace; Q9R0G6; -.
DR PRO; PR:Q9R0G6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R0G6; protein.
DR Bgee; ENSMUSG00000031849; Expressed in humerus cartilage element and 98 other tissues.
DR ExpressionAtlas; Q9R0G6; baseline and differential.
DR Genevisible; Q9R0G6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0036122; F:BMP binding; IPI:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0005499; F:vitamin D binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0098868; P:bone growth; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:1990079; P:cartilage homeostasis; IDA:UniProtKB.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0035988; P:chondrocyte proliferation; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0003416; P:endochondral bone growth; IMP:MGI.
DR GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR GO; GO:0060173; P:limb development; IMP:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR GO; GO:0050881; P:musculoskeletal movement; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1900047; P:negative regulation of hemostasis; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:MGI.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IMP:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0035989; P:tendon development; IMP:MGI.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IMP:MGI.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IMP:MGI.
DR CDD; cd16077; TSP-5cc; 1.
DR Gene3D; 4.10.1080.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028492; TSP-5.
DR InterPro; IPR039081; TSP-5_cc.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; PTHR10199:SF88; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Calcium; Cell adhesion; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Heparin-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..755
FT /note="Cartilage oligomeric matrix protein"
FT /id="PRO_0000035858"
FT DOMAIN 85..124
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 125..177
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 178..220
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..265
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 266..298
FT /note="TSP type-3 1"
FT REPEAT 299..334
FT /note="TSP type-3 2"
FT REPEAT 335..357
FT /note="TSP type-3 3"
FT REPEAT 358..393
FT /note="TSP type-3 4"
FT REPEAT 394..416
FT /note="TSP type-3 5"
FT REPEAT 417..454
FT /note="TSP type-3 6"
FT REPEAT 455..490
FT /note="TSP type-3 7"
FT REPEAT 491..526
FT /note="TSP type-3 8"
FT DOMAIN 530..744
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 21..84
FT /note="COMP N-terminal"
FT REGION 296..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..755
FT /note="Mediates cell survival and induction of the IAP
FT family of survival proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 353..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68
FT /note="Interchain (with C-71)"
FT /evidence="ECO:0000269|PubMed:12426368,
FT ECO:0007744|PDB:1MZ9, ECO:0007744|PDB:3V2N,
FT ECO:0007744|PDB:3V2P, ECO:0007744|PDB:3V2Q,
FT ECO:0007744|PDB:3V2R"
FT DISULFID 71
FT /note="Interchain (with C-68)"
FT /evidence="ECO:0000269|PubMed:12426368,
FT ECO:0007744|PDB:1MZ9, ECO:0007744|PDB:3V2N,
FT ECO:0007744|PDB:3V2P, ECO:0007744|PDB:3V2Q,
FT ECO:0007744|PDB:3V2R"
FT DISULFID 89..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 94..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 112..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 129..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 152..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 182..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 189..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 207..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 227..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 235..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 253..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 280..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 290..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 326..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 349..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 385..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 408..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 446..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 482..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 518..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 65
FT /note="V->E: Equivalent to human variant V66E involved in
FT CTS2 disease. Reduces secretion in tendon cells and nhibits
FT oligomerization. Mutant mice develop inflammation and
FT fibrosis in Achilles tendons and carpal tunnel. They show
FT compromised regenerative capability of tendons."
FT /evidence="ECO:0000269|PubMed:32686688"
FT CONFLICT 53..54
FT /note="QQ -> HE (in Ref. 1; AAD01972)"
FT /evidence="ECO:0000305"
FT HELIX 30..66
FT /evidence="ECO:0007829|PDB:1MZ9"
SQ SEQUENCE 755 AA; 82342 MW; 24C2F113E7945C0F CRC64;
MGPTACVLVL ALAILRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL LRQQVKEITF
LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC SETATGARCG PCPPGYTGNG
SHCTDVNECN AHPCFPRVRC INTSPGFHCE ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN
ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN
CVLERDGSRS CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED
VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR SKKNDDQKDT
DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG VGDACDNCPQ KDNPDQRDVD
HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP NSAQQDSDHD GKGDACDDDD DNDGVPDSRD
NCRLVPNPGQ EDNDRDGVGD ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE
GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN ALWHTGDTAS
QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG PELVADSNVV LDTAMRGGRL
GVFCFSQENI IWANLRYRCN DTIPEDYESH RLQRV
