UCMA_MOUSE
ID UCMA_MOUSE Reviewed; 138 AA.
AC Q14BU0; C9W8R6; C9W8R7; C9W8R8; C9W8R9; Q9D1A9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Unique cartilage matrix-associated protein;
DE AltName: Full=Upper zone of growth plate and 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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 65-71,
RP FUNCTION, SULFATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=18156182; DOI=10.1074/jbc.m702792200;
RA Surmann-Schmitt C., Dietz U., Kireva T., Adam N., Park J., Tagariello A.,
RA Onnerfjord P., Heinegard D., Schlotzer-Schrehardt U., Deutzmann R.,
RA von der Mark K., Stock M.;
RT "Ucma, a novel secreted cartilage-specific protein with implications in
RT osteogenesis.";
RL J. Biol. Chem. 283:7082-7093(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=19819238; DOI=10.1016/j.yexcr.2009.10.002;
RA Le Jeune M., Tomavo N., Tian T.V., Flourens A., Marchand N., Camuzeaux B.,
RA Mallein-Gerin F., Duterque-Coquillaud M.;
RT "Identification of four alternatively spliced transcripts of the Ucma/GRP
RT gene, encoding a new Gla-containing protein.";
RL Exp. Cell Res. 316:203-215(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:0000269|PubMed:18156182}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18156182, ECO:0000269|PubMed:19819238}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates
CC of misfolded proteins, at the centrosome.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton
CC {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates
CC of misfolded proteins, at the centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Ucma/GRP-F1;
CC IsoId=Q14BU0-1; Sequence=Displayed;
CC Name=2; Synonyms=Ucma/GRP-F2;
CC IsoId=Q14BU0-2; Sequence=VSP_035051;
CC Name=3; Synonyms=Ucma/GRP-F3;
CC IsoId=Q14BU0-3; Sequence=VSP_040807;
CC Name=4; Synonyms=Ucma/GRP-F4;
CC IsoId=Q14BU0-4; Sequence=VSP_035051, VSP_040807;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in resting chondrocytes.
CC {ECO:0000269|PubMed:18156182}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed in the developing mouse
CC skeleton between day 13.5 dpc of embryonic development and 5 months of
CC postnatal development. Absent in undifferentiated mesenchymal cells.
CC Isoforms 1 and 3 are significantly increased with the onset of
CC chondrogenesis, whereas Isoforms 2 and 4 are detected at a later stage.
CC {ECO:0000269|PubMed:18156182, ECO:0000269|PubMed:19819238}.
CC -!- INDUCTION: Expression inhibited by TGFB1, and weakly inhibited by BMP2.
CC {ECO:0000269|PubMed:19819238}.
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 -!- PTM: Sulfated on one or two tyrosine residues within the tryptic
CC peptide 121-135. {ECO:0000269|PubMed:18156182}.
CC -!- SIMILARITY: Belongs to the UCMA family. {ECO:0000305}.
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DR EMBL; EF529510; ABP88975.1; -; mRNA.
DR EMBL; EU368184; ABY65726.1; -; mRNA.
DR EMBL; FJ217397; ACO35746.1; -; mRNA.
DR EMBL; FJ217398; ACO35747.1; -; mRNA.
DR EMBL; FJ217399; ACO35748.1; -; mRNA.
DR EMBL; FJ217400; ACO35749.1; -; mRNA.
DR EMBL; AK003750; BAB22978.2; -; mRNA.
DR EMBL; AL928662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX682541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL07955.1; -; Genomic_DNA.
DR EMBL; BC115608; AAI15609.1; -; mRNA.
DR EMBL; BC115609; AAI15610.1; -; mRNA.
DR CCDS; CCDS15661.1; -. [Q14BU0-2]
DR CCDS; CCDS50489.1; -. [Q14BU0-1]
DR CCDS; CCDS50490.1; -. [Q14BU0-3]
DR CCDS; CCDS84467.1; -. [Q14BU0-4]
DR RefSeq; NP_001107030.1; NM_001113558.2. [Q14BU0-1]
DR RefSeq; NP_001159404.1; NM_001165932.1. [Q14BU0-3]
DR RefSeq; NP_001298137.1; NM_001311208.1. [Q14BU0-4]
DR RefSeq; NP_081030.1; NM_026754.3. [Q14BU0-2]
DR AlphaFoldDB; Q14BU0; -.
DR STRING; 10090.ENSMUSP00000110662; -.
DR PaxDb; Q14BU0; -.
DR PRIDE; Q14BU0; -.
DR ProteomicsDB; 298117; -. [Q14BU0-1]
DR ProteomicsDB; 298119; -. [Q14BU0-3]
DR Antibodypedia; 24782; 79 antibodies from 24 providers.
DR Ensembl; ENSMUST00000027978; ENSMUSP00000027978; ENSMUSG00000026668. [Q14BU0-2]
DR Ensembl; ENSMUST00000115010; ENSMUSP00000110662; ENSMUSG00000026668. [Q14BU0-1]
DR Ensembl; ENSMUST00000167607; ENSMUSP00000126371; ENSMUSG00000026668. [Q14BU0-3]
DR Ensembl; ENSMUST00000195688; ENSMUSP00000141304; ENSMUSG00000026668. [Q14BU0-4]
DR GeneID; 68527; -.
DR KEGG; mmu:68527; -.
DR UCSC; uc008ife.2; mouse. [Q14BU0-2]
DR UCSC; uc008iff.2; mouse. [Q14BU0-1]
DR UCSC; uc012bov.1; mouse. [Q14BU0-3]
DR UCSC; uc012bow.1; mouse. [Q14BU0-4]
DR CTD; 221044; -.
DR MGI; MGI:1915777; Ucma.
DR VEuPathDB; HostDB:ENSMUSG00000026668; -.
DR eggNOG; ENOG502S1J9; Eukaryota.
DR GeneTree; ENSGT00390000011492; -.
DR HOGENOM; CLU_153982_0_0_1; -.
DR InParanoid; Q14BU0; -.
DR OMA; TMLQEGT; -.
DR OrthoDB; 1577653at2759; -.
DR PhylomeDB; Q14BU0; -.
DR TreeFam; TF332568; -.
DR BioGRID-ORCS; 68527; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q14BU0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q14BU0; protein.
DR Bgee; ENSMUSG00000026668; Expressed in otolith organ and 99 other tissues.
DR Genevisible; Q14BU0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0036122; F:BMP binding; ISO:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IBA:GO_Central.
DR GO; GO:0110150; P:negative regulation of biomineralization; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR InterPro; IPR031386; UCMA.
DR PANTHER; PTHR28647; PTHR28647; 1.
DR Pfam; PF17085; UCMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Extracellular matrix; Golgi apparatus;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..138
FT /note="Unique cartilage matrix-associated protein"
FT /id="PRO_0000347065"
FT PROPEP 28..64
FT /note="Ucma-N"
FT /evidence="ECO:0000269|PubMed:18156182"
FT /id="PRO_0000347066"
FT CHAIN 65..138
FT /note="Unique cartilage matrix-associated protein C-
FT terminal fragment"
FT /id="PRO_0000347067"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..122
FT /evidence="ECO:0000255"
FT VAR_SEQ 20..42
FT /note="MLQEGTSASVGSRQAAAEGVQEG -> S (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:19819238"
FT /id="VSP_035051"
FT VAR_SEQ 74..106
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19819238"
FT /id="VSP_040807"
SQ SEQUENCE 138 AA; 16579 MW; 11914F39960348DC CRC64;
MSWRRVILLS SLLALVLLCM LQEGTSASVG SRQAAAEGVQ EGVKQKIFMQ ESDASNFLKR
RGKRSPKSRD EVNAENRQRL RDDELRREYY EEQRNEFENF VEEQRDEQEE RTREAVEQWR
QWHYDGLYPS YLYNRQNI
