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UCMA_SPAAU
ID   UCMA_SPAAU              Reviewed;         133 AA.
AC   B9TQX2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Unique cartilage matrix-associated protein {ECO:0000250|UniProtKB:Q14BU0};
DE   Contains:
DE     RecName: Full=Unique cartilage matrix-associated protein C-terminal fragment {ECO:0000250|UniProtKB:Q14BU0};
DE              Short=Ucma-C {ECO:0000250|UniProtKB:Q14BU0};
DE     AltName: Full=Gla-rich protein {ECO:0000303|PubMed:18836183, ECO:0000312|EMBL:ABX09787.1};
DE              Short=GRP {ECO:0000303|PubMed:18836183};
DE   Flags: Precursor;
GN   Name=ucma; Synonyms=grp;
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1] {ECO:0000312|EMBL:ABX09787.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18836183; DOI=10.1074/jbc.m802761200;
RA   Viegas C.S.B., Simes D.C., Laize V., Williamson M.K., Price P.A.,
RA   Cancela M.L.;
RT   "Gla-rich protein (GRP), a new vitamin K-dependent protein identified from
RT   sturgeon cartilage and highly conserved in vertebrates.";
RL   J. Biol. Chem. 283:36655-36664(2008).
CC   -!- FUNCTION: May be involved in the negative control of osteogenic
CC       differentiation of osteochondrogenic precursor cells in peripheral
CC       zones of fetal cartilage and at the cartilage-bone interface.
CC       {ECO:0000250|UniProtKB:Q14BU0}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q14BU0}.
CC   -!- PTM: Proteolytically cleaved by a furin-like convertase to generate a
CC       persistent C-terminal fragment found in almost the entire cartilage
CC       matrix, and affecting osteoblast differentiation.
CC       {ECO:0000250|UniProtKB:Q14BU0}.
CC   -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:Q14BU0}.
CC   -!- SIMILARITY: Belongs to the UCMA family. {ECO:0000305}.
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DR   EMBL; EU022752; ABX09787.1; -; mRNA.
DR   AlphaFoldDB; B9TQX2; -.
DR   Ensembl; ENSSAUT00010054830; ENSSAUP00010052141; ENSSAUG00010021640.
DR   GeneTree; ENSGT00390000011492; -.
DR   OMA; QLREFHY; -.
DR   Proteomes; UP000472265; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:InterPro.
DR   InterPro; IPR031386; UCMA.
DR   PANTHER; PTHR28647; PTHR28647; 1.
DR   Pfam; PF17085; UCMA; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Extracellular matrix; Gamma-carboxyglutamic acid;
KW   Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..133
FT                   /note="Unique cartilage matrix-associated protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000371240"
FT   PROPEP          27..62
FT                   /note="Ucma-N"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT                   /id="PRO_0000371241"
FT   CHAIN           63..133
FT                   /note="Unique cartilage matrix-associated protein C-
FT                   terminal fragment"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT                   /id="PRO_0000371242"
FT   REGION          87..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          80..120
FT                   /evidence="ECO:0000255"
FT   MOD_RES         69
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         73
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         82
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         86
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         89
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         90
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         94
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         96
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         100
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         101
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         105
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         108
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         112
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         115
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT   MOD_RES         119
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:B9TQX1"
SQ   SEQUENCE   133 AA;  15920 MW;  3A71C14E22C7FE68 CRC64;
     MSWTRVVVLS LLTTLLFLTF SSVVDSAAVR DDSKAGHPKG PARQVFVPES EASNFFKRRS
     RRSPRSYAEL QAEQRVKIAA NERWREYNEE QRNEHENYAE EARDESDERS RETHEQIREY
     HYDGLYPRYH WFH
 
 
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