UCMA_ACINA
ID UCMA_ACINA Reviewed; 139 AA.
AC B9TQX1; P85209;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 16.
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:ABX09786.1};
DE Short=GRP {ECO:0000303|PubMed:18836183};
DE Flags: Precursor;
GN Name=ucma; Synonyms=grp;
OS Acipenser naccarii (Adriatic sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=42330;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABX09786.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 66-85, TISSUE
RP SPECIFICITY, AND GAMMA-CARBOXYGLUTAMATION AT GLU-72; GLU-76; GLU-85;
RP GLU-89; GLU-92; GLU-93; GLU-97; GLU-99; GLU-103; GLU-104; GLU-105; GLU-108;
RP GLU-111; GLU-115; GLU-118 AND GLU-122.
RC TISSUE=Branchial arch region {ECO:0000269|PubMed:18836183};
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 -!- TISSUE SPECIFICITY: Detected in all tissues tested: heart, liver,
CC kidney, muscle, gonads, brain, ganoid plate, anterior kidney, spleen,
CC spine, cleithrum, head plate, operculum, skull, mandibula, branchial
CC arches, anterior vertebra, and posterior vertebra. Expression is
CC highest in the cartilaginous tissues (skull, mandibula, branchial
CC arches, anterior vertebra and posterior vertebra), with the highest
CC levels found in posterior vertebra. Found in mature and immature
CC chondrocytes within the vertebra and mandibula, and in the chordoblast
CC layer of the notochord in vertebra. {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; EU022751; ABX09786.1; -; mRNA.
DR EMBL; EU482149; ACD03736.1; -; Genomic_DNA.
DR AlphaFoldDB; B9TQX1; -.
DR PRIDE; B9TQX1; -.
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 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Extracellular matrix;
KW Gamma-carboxyglutamic acid; Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..139
FT /note="Unique cartilage matrix-associated protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000371234"
FT PROPEP 27..65
FT /note="Ucma-N"
FT /evidence="ECO:0000269|PubMed:18836183"
FT /id="PRO_0000371235"
FT CHAIN 66..139
FT /note="Unique cartilage matrix-associated protein C-
FT terminal fragment"
FT /evidence="ECO:0000269|PubMed:18836183"
FT /id="PRO_0000371236"
FT REGION 60..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..123
FT /evidence="ECO:0000255"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 85
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 89
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 92
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 93
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 97
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 99
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 103
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 104
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 105
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 108
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 111
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 115
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 118
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
FT MOD_RES 122
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18836183"
SQ SEQUENCE 139 AA; 16998 MW; 43D214F731EECB93 CRC64;
MNWNQIIFIS LIATVLILAI ANEAESAAVR TDKSDIKRED GENMKKRIFM QESEATAFLK
RRGRRSTKSK DEVNAENRQR LAADERRREY YEEQRNEFEN YVEEERDEQQ ERNREKTEQW
REYHYDGLYP SYQYNRHHI
