UCMA_XENTR
ID UCMA_XENTR Reviewed; 138 AA.
AC Q28HK1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Unique cartilage matrix-associated protein;
DE Contains:
DE RecName: Full=Unique cartilage matrix-associated protein C-terminal fragment;
DE Short=Ucma-C;
DE AltName: Full=Gla-rich protein;
DE Short=GRP;
DE Flags: Precursor;
GN Name=ucma; ORFNames=TTpA007d02.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UCMA family. {ECO:0000305}.
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DR EMBL; CR760848; CAJ83238.1; -; mRNA.
DR EMBL; BC135882; AAI35883.1; -; mRNA.
DR RefSeq; NP_001016485.1; NM_001016485.2.
DR AlphaFoldDB; Q28HK1; -.
DR STRING; 8364.ENSXETP00000019992; -.
DR PaxDb; Q28HK1; -.
DR Ensembl; ENSXETT00000019992; ENSXETP00000019992; ENSXETG00000009114.
DR GeneID; 549239; -.
DR KEGG; xtr:549239; -.
DR CTD; 221044; -.
DR Xenbase; XB-GENE-5752310; ucma.
DR eggNOG; ENOG502S1J9; Eukaryota.
DR HOGENOM; CLU_153982_0_0_1; -.
DR InParanoid; Q28HK1; -.
DR OMA; MSWSHAT; -.
DR OrthoDB; 1613699at2759; -.
DR PhylomeDB; Q28HK1; -.
DR TreeFam; TF332568; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009114; Expressed in liver and 9 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048706; P:embryonic skeletal system development; IBA:GO_Central.
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..138
FT /note="Unique cartilage matrix-associated protein"
FT /id="PRO_0000371307"
FT PROPEP 28..64
FT /note="Ucma-N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000371308"
FT CHAIN 65..138
FT /note="Unique cartilage matrix-associated protein C-
FT terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000371309"
FT REGION 58..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..118
FT /evidence="ECO:0000255"
FT COMPBIAS 58..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 88
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 91
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 107
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 110
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 114
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 16455 MW; 60337F44F6E31711 CRC64;
MKRNQVLFLT CAAAVVFLAV LHVGESAAVR SKDDPAPDKK ESLKSKIFMQ GSEASNFFKK
RGKRSPKSQD EINAENRQRL SADERRREYY EEQRNEFENH VEEEQDEQEE RSREQIEQWR
QWHYDGLSPS YLYQRQNI
