UCMA_RAT
ID UCMA_RAT Reviewed; 138 AA.
AC B9TQX4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
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:ABX09789.1};
DE Short=GRP {ECO:0000303|PubMed:18836183};
DE Flags: Precursor;
GN Name=Ucma {ECO:0000250|UniProtKB:Q14BU0};
GN Synonyms=Grp {ECO:0000312|EMBL:ABX09789.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABX09789.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
RN [2] {ECO:0000312|EMBL:EDL78670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL78670.1};
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.
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 -!- TISSUE SPECIFICITY: Detected in immature, proliferating, mature,
CC columnar and hypertrophic chondrocytes from ribs, tail, vertebra and
CC femur. {ECO:0000269|PubMed:18836183}.
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; EU022754; ABX09789.1; -; mRNA.
DR EMBL; CH473990; EDL78670.1; -; Genomic_DNA.
DR RefSeq; XP_017455982.1; XM_017600493.1.
DR AlphaFoldDB; B9TQX4; -.
DR STRING; 10116.ENSRNOP00000063022; -.
DR PaxDb; B9TQX4; -.
DR PRIDE; B9TQX4; -.
DR Ensembl; ENSRNOT00000066850; ENSRNOP00000063022; ENSRNOG00000017987.
DR GeneID; 291312; -.
DR CTD; 221044; -.
DR RGD; 1308977; Ucma.
DR eggNOG; ENOG502S1J9; Eukaryota.
DR GeneTree; ENSGT00390000011492; -.
DR HOGENOM; CLU_153982_0_0_1; -.
DR InParanoid; B9TQX4; -.
DR OMA; TMLQEGT; -.
DR PhylomeDB; B9TQX4; -.
DR TreeFam; TF332568; -.
DR PRO; PR:B9TQX4; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000017987; Expressed in pancreas and 12 other tissues.
DR GO; GO:0016235; C:aggresome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0036122; F:BMP binding; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; IBA:GO_Central.
DR GO; GO:0110150; P:negative regulation of biomineralization; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
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; Reference proteome; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..138
FT /note="Unique cartilage matrix-associated protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000371231"
FT PROPEP 28..64
FT /note="Ucma-N"
FT /evidence="ECO:0000250|UniProtKB:Q14BU0"
FT /id="PRO_0000371232"
FT CHAIN 65..138
FT /note="Unique cartilage matrix-associated protein C-
FT terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q14BU0"
FT /id="PRO_0000371233"
FT REGION 58..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..122
FT /evidence="ECO:0000255"
SQ SEQUENCE 138 AA; 16574 MW; 9C0E90D363D0086B CRC64;
MSWRQVILLS SLSALVLLCM LQEGTSASVG SRQAAGEEVQ EGMKQKIFMQ ESDASNFLKR
RGKRSPKSRD EVTAENRQKL RDDELRREYY EEQRNEFENF VEEQRDEQEE RTREAVEQWR
QWHYDGLYPS YLYNRQNI