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Unique cartilage matrix-associated protein (Upper zone of growth plate and cartilage matrix associated protein) [Cleaved into: Unique cartilage matrix-associated protein C-terminal fragment (Ucma-C) (Gla-rich protein) (GRP)]

 UCMA_MOUSE              Reviewed;         138 AA.
Q14BU0; C9W8R6; C9W8R7; C9W8R8; C9W8R9; Q9D1A9;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
22-AUG-2006, sequence version 1.
22-NOV-2017, entry version 79.
RecName: Full=Unique cartilage matrix-associated protein;
AltName: Full=Upper zone of growth plate and cartilage matrix associated protein;
Contains:
RecName: Full=Unique cartilage matrix-associated protein C-terminal fragment;
Short=Ucma-C;
AltName: Full=Gla-rich protein;
Short=GRP;
Flags: Precursor;
Name=Ucma;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 65-71,
FUNCTION, SULFATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
STRAIN=C57BL/6J;
PubMed=18156182; DOI=10.1074/jbc.M702792200;
Surmann-Schmitt C., Dietz U., Kireva T., Adam N., Park J.,
Tagariello A., Onnerfjord P., Heinegard D., Schlotzer-Schrehardt U.,
Deutzmann R., von der Mark K., Stock M.;
"Ucma, a novel secreted cartilage-specific protein with implications
in osteogenesis.";
J. Biol. Chem. 283:7082-7093(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=19819238; DOI=10.1016/j.yexcr.2009.10.002;
Le Jeune M., Tomavo N., Tian T.V., Flourens A., Marchand N.,
Camuzeaux B., Mallein-Gerin F., Duterque-Coquillaud M.;
"Identification of four alternatively spliced transcripts of the
Ucma/GRP gene, encoding a new Gla-containing protein.";
Exp. Cell Res. 316:203-215(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: May be involved in the negative control of osteogenic
differentiation of osteochondrogenic precursor cells in peripheral
zones of fetal cartilage and at the cartilage-bone interface.
{ECO:0000269|PubMed:18156182}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:18156182, ECO:0000269|PubMed:19819238}.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Golgi apparatus.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted. Golgi apparatus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton
{ECO:0000305}. Note=Colocalizes with aggresomes, which are
aggregates of misfolded proteins, at the centrosome.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytoskeleton
{ECO:0000305}. Note=Colocalizes with aggresomes, which are
aggregates of misfolded proteins, at the centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Ucma/GRP-F1;
IsoId=Q14BU0-1; Sequence=Displayed;
Name=2; Synonyms=Ucma/GRP-F2;
IsoId=Q14BU0-2; Sequence=VSP_035051;
Name=3; Synonyms=Ucma/GRP-F3;
IsoId=Q14BU0-3; Sequence=VSP_040807;
Name=4; Synonyms=Ucma/GRP-F4;
IsoId=Q14BU0-4; Sequence=VSP_035051, VSP_040807;
-!- TISSUE SPECIFICITY: Predominantly expressed in resting
chondrocytes. {ECO:0000269|PubMed:18156182}.
-!- DEVELOPMENTAL STAGE: Transiently expressed in the developing mouse
skeleton between day E13.5 of embryonic development and 5 months
of postnatal development. Absent in undifferentiated mesenchymal
cells. Isoforms 1 and 3 are significantly increased with the onset
of chondrogenesis, whereas Isoforms 2 and 4 are detected at a
later stage. {ECO:0000269|PubMed:18156182,
ECO:0000269|PubMed:19819238}.
-!- INDUCTION: Expression inhibited by TGFB1, and weakly inhibited by
BMP2. {ECO:0000269|PubMed:19819238}.
-!- PTM: Proteolytically cleaved by a furin-like convertase to
generate a persistent C-terminal fragment found in almost the
entire cartilage matrix, and affecting osteoblast differentiation.
-!- PTM: Sulfated on one or two tyrosine residues within the tryptic
peptide 121-135. {ECO:0000269|PubMed:18156182}.
-!- SIMILARITY: Belongs to the UCMA family. {ECO:0000305}.
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EMBL; EF529510; ABP88975.1; -; mRNA.
EMBL; EU368184; ABY65726.1; -; mRNA.
EMBL; FJ217397; ACO35746.1; -; mRNA.
EMBL; FJ217398; ACO35747.1; -; mRNA.
EMBL; FJ217399; ACO35748.1; -; mRNA.
EMBL; FJ217400; ACO35749.1; -; mRNA.
EMBL; AK003750; BAB22978.2; -; mRNA.
EMBL; BX682541; CAM21763.1; -; Genomic_DNA.
EMBL; AL928662; CAM21763.1; JOINED; Genomic_DNA.
EMBL; BX682541; CAM21764.1; -; Genomic_DNA.
EMBL; AL928662; CAM21764.1; JOINED; Genomic_DNA.
EMBL; AL928662; CAM22576.1; -; Genomic_DNA.
EMBL; BX682541; CAM22576.1; JOINED; Genomic_DNA.
EMBL; AL928662; CAM22577.1; -; Genomic_DNA.
EMBL; BX682541; CAM22577.1; JOINED; Genomic_DNA.
EMBL; CH466542; EDL07955.1; -; Genomic_DNA.
EMBL; BC115608; AAI15609.1; -; mRNA.
EMBL; BC115609; AAI15610.1; -; mRNA.
CCDS; CCDS15661.1; -. [Q14BU0-2]
CCDS; CCDS50489.1; -. [Q14BU0-1]
CCDS; CCDS50490.1; -. [Q14BU0-3]
CCDS; CCDS84467.1; -. [Q14BU0-4]
RefSeq; NP_001107030.1; NM_001113558.2. [Q14BU0-1]
RefSeq; NP_001159404.1; NM_001165932.1. [Q14BU0-3]
RefSeq; NP_001298137.1; NM_001311208.1. [Q14BU0-4]
RefSeq; NP_081030.1; NM_026754.3. [Q14BU0-2]
UniGene; Mm.27791; -.
STRING; 10090.ENSMUSP00000110662; -.
PaxDb; Q14BU0; -.
PRIDE; Q14BU0; -.
Ensembl; ENSMUST00000027978; ENSMUSP00000027978; ENSMUSG00000026668. [Q14BU0-2]
Ensembl; ENSMUST00000115010; ENSMUSP00000110662; ENSMUSG00000026668. [Q14BU0-1]
Ensembl; ENSMUST00000167607; ENSMUSP00000126371; ENSMUSG00000026668. [Q14BU0-3]
Ensembl; ENSMUST00000195688; ENSMUSP00000141304; ENSMUSG00000026668. [Q14BU0-4]
GeneID; 68527; -.
KEGG; mmu:68527; -.
UCSC; uc008ife.2; mouse. [Q14BU0-2]
UCSC; uc008iff.2; mouse. [Q14BU0-1]
UCSC; uc012bov.1; mouse. [Q14BU0-3]
UCSC; uc012bow.1; mouse. [Q14BU0-4]
CTD; 221044; -.
MGI; MGI:1915777; Ucma.
eggNOG; ENOG410IY09; Eukaryota.
eggNOG; ENOG4111U8I; LUCA.
GeneTree; ENSGT00390000011492; -.
HOGENOM; HOG000253965; -.
HOVERGEN; HBG098812; -.
InParanoid; Q14BU0; -.
OMA; YLYNRHH; -.
OrthoDB; EOG091G10F8; -.
PhylomeDB; Q14BU0; -.
TreeFam; TF332568; -.
PRO; PR:Q14BU0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026668; -.
Genevisible; Q14BU0; MM.
GO; GO:0016235; C:aggresome; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
InterPro; IPR031386; UCMA.
PANTHER; PTHR28647; PTHR28647; 1.
Pfam; PF17085; UCMA; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Extracellular matrix;
Golgi apparatus; Reference proteome; Secreted; Signal; Sulfation.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 138 Unique cartilage matrix-associated
protein.
/FTId=PRO_0000347065.
PROPEP 28 64 Ucma-N. {ECO:0000269|PubMed:18156182}.
/FTId=PRO_0000347066.
CHAIN 65 138 Unique cartilage matrix-associated
protein C-terminal fragment.
/FTId=PRO_0000347067.
COILED 78 122 {ECO:0000255}.
VAR_SEQ 20 42 MLQEGTSASVGSRQAAAEGVQEG -> S (in isoform
2 and isoform 4).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:19819238}.
/FTId=VSP_035051.
VAR_SEQ 74 106 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:19819238}.
/FTId=VSP_040807.
SEQUENCE 138 AA; 16579 MW; 11914F39960348DC CRC64;
MSWRRVILLS SLLALVLLCM LQEGTSASVG SRQAAAEGVQ EGVKQKIFMQ ESDASNFLKR
RGKRSPKSRD EVNAENRQRL RDDELRREYY EEQRNEFENF VEEQRDEQEE RTREAVEQWR
QWHYDGLYPS YLYNRQNI


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