CRTAP_MOUSE
ID CRTAP_MOUSE Reviewed; 400 AA.
AC Q9CYD3; O88698; Q8C8C5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cartilage-associated protein;
DE Flags: Precursor;
GN Name=Crtap; Synonyms=Casp;
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].
RC TISSUE=Embryo;
RX PubMed=10429950; DOI=10.1016/s0945-053x(99)00002-5;
RA Morello R., Tonachini L., Monticone M., Viggiano L., Rocchi M.,
RA Cancedda R., Castagnola P.;
RT "cDNA cloning, characterization and chromosome mapping of Crtap encoding
RT the mouse cartilage associated protein.";
RL Matrix Biol. 18:319-324(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN OSTEOCHONDRODYSPLASIA.
RX PubMed=17055431; DOI=10.1016/j.cell.2006.08.039;
RA Morello R., Bertin T.K., Chen Y., Hicks J., Tonachini L., Monticone M.,
RA Castagnola P., Rauch F., Glorieux F.H., Vranka J., Baechinger H.P.,
RA Pace J.M., Schwarze U., Byers P.H., Weis M., Fernandes R.J., Eyre D.R.,
RA Yao Z., Boyce B.F., Lee B.;
RT "CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive
RT osteogenesis imperfecta.";
RL Cell 127:291-304(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen
CC prolyl residues. {ECO:0000269|PubMed:17055431}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Found in articular chondrocytes. Expressed in a
CC variety of tissues. {ECO:0000269|PubMed:17055431}.
CC -!- DISEASE: Note=Defects in Crtap are a cause of osteochondrodysplasia
CC characterized by severe osteoporosis and decreased osteoid production.
CC {ECO:0000269|PubMed:17055431}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR EMBL; AJ006469; CAA07053.1; -; mRNA.
DR EMBL; AK017797; BAB30938.1; -; mRNA.
DR EMBL; AK047506; BAC33076.1; -; mRNA.
DR EMBL; BC049890; AAH49890.1; -; mRNA.
DR CCDS; CCDS23592.1; -.
DR RefSeq; NP_064306.2; NM_019922.2.
DR AlphaFoldDB; Q9CYD3; -.
DR STRING; 10090.ENSMUSP00000081941; -.
DR GlyConnect; 2188; 1 N-Linked glycan (1 site).
DR GlyGen; Q9CYD3; 2 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q9CYD3; -.
DR EPD; Q9CYD3; -.
DR MaxQB; Q9CYD3; -.
DR PaxDb; Q9CYD3; -.
DR PeptideAtlas; Q9CYD3; -.
DR PRIDE; Q9CYD3; -.
DR ProteomicsDB; 285365; -.
DR Antibodypedia; 27879; 260 antibodies from 29 providers.
DR DNASU; 56693; -.
DR Ensembl; ENSMUST00000084881; ENSMUSP00000081941; ENSMUSG00000032431.
DR GeneID; 56693; -.
DR KEGG; mmu:56693; -.
DR UCSC; uc009rxg.2; mouse.
DR CTD; 10491; -.
DR MGI; MGI:1891221; Crtap.
DR VEuPathDB; HostDB:ENSMUSG00000032431; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000153814; -.
DR HOGENOM; CLU_029887_0_1_1; -.
DR InParanoid; Q9CYD3; -.
DR OMA; DPNDEVM; -.
DR OrthoDB; 607176at2759; -.
DR PhylomeDB; Q9CYD3; -.
DR TreeFam; TF320837; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 56693; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Crtap; mouse.
DR PRO; PR:Q9CYD3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CYD3; protein.
DR Bgee; ENSMUSG00000032431; Expressed in vault of skull and 252 other tissues.
DR Genevisible; Q9CYD3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:CAFA.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:1901874; P:negative regulation of post-translational protein modification; ISO:MGI.
DR GO; GO:0018400; P:peptidyl-proline hydroxylation to 3-hydroxy-L-proline; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR033212; Crtap.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13986:SF3; PTHR13986:SF3; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..400
FT /note="Cartilage-associated protein"
FT /id="PRO_0000006320"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="T -> A (in Ref. 1; CAA07053)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="S -> N (in Ref. 1; CAA07053)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..80
FT /note="SE -> RQ (in Ref. 2; BAB30938)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="SR -> VA (in Ref. 2; BAB30938)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> T (in Ref. 2; BAB30938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 46169 MW; F6080CEC275CC5A4 CRC64;
MGPRSPTAAL LVLLCVGCAP TPGRGQYERY SFRSFPRDEL MPLESAYRHA LDQYSGEHWA
ESVGYLEVSL RLHRLLRDSE AFCHRNCSAA TPAPAPAGPA SHAELRLFGS VLRRAQCLKR
CKQGLPAFRQ SQPSRSVLAD FQQREPYKFL QFAYFKANDL PKAIAAAHTY LLKHPDDEMM
KRNMEYYKSL PGAEDHIKDL ETKSYESLFV RAVRAYNGEN WRTSISDMEL ALPDFLKAFY
ECLAACEGSR EIKDFKDFYL SIADHYVEVL ECKIRCEETL TPVIGGYPVE KFVATMYHYL
QFAYYKLNDL KNAAPCAVSY LLFDQSDRVM QQNLVYYQYH RDKWGLSDEH FQPRPEAVQF
FNVTTLQKEL YDFAQEHLMD DDEGEVVEYV DDLLETEESA
