UCMA_DICLA
ID UCMA_DICLA Reviewed; 133 AA.
AC B9TQX3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 20.
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:ABX09788.1};
DE Short=GRP {ECO:0000303|PubMed:18836183};
DE Flags: Precursor;
GN Name=ucma; Synonyms=grp;
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489;
RN [1] {ECO:0000312|EMBL:ABX09788.1}
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; EU022753; ABX09788.1; -; mRNA.
DR AlphaFoldDB; B9TQX3; -.
DR Proteomes; UP000694389; 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_0000371237"
FT PROPEP 27..62
FT /note="Ucma-N"
FT /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT /id="PRO_0000371238"
FT CHAIN 63..133
FT /note="Unique cartilage matrix-associated protein C-
FT terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:B9TQX1"
FT /id="PRO_0000371239"
FT REGION 57..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..121
FT /evidence="ECO:0000255"
FT COMPBIAS 65..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 102
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; 16109 MW; 59F4B2598E8C05DF CRC64;
MSWTRVVVLS SLTTLLILTF SSVVKSAAVR DDSKAGDPKG AARHVFMPES DASNFFKHRS
RRSPRYYSER QAEQRVRLSA NERRREYNEE QRNEFENYVE EERDEQNERS REKNEQVREY
HYDGLYPRYH WFH
