ID   CRTAP_CHICK             Reviewed;         271 AA.
AC   Q90830;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cartilage-associated protein;
DE   AltName: Full=Dualin;
DE   Flags: Precursor;
GN   Name=CRTAP; Synonyms=CASP;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9217321; DOI=10.1242/jcs.110.12.1351;
RA   Castagnola P., Gennari M., Morello R., Tonachini L., Marin O., Gaggero A.,
RA   Cancedda R.;
RT   "Cartilage associated protein (CASP) is a novel developmentally regulated
RT   chick embryo protein.";
RL   J. Cell Sci. 110:1351-1359(1997).
CC   -!- FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen
CC       prolyl residues. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q90830; Q6JHU8: P3H1; NbExp=3; IntAct=EBI-1169253, EBI-1169258;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Found in articular chondrocytes. Expressed in a
CC       variety of tissues.
CC   -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR   EMBL; X97607; CAA66206.1; -; mRNA.
DR   RefSeq; NP_990431.1; NM_205100.1.
DR   AlphaFoldDB; Q90830; -.
DR   IntAct; Q90830; 2.
DR   STRING; 9031.ENSGALP00000036750; -.
DR   PaxDb; Q90830; -.
DR   GeneID; 395992; -.
DR   KEGG; gga:395992; -.
DR   CTD; 10491; -.
DR   VEuPathDB; HostDB:geneid_395992; -.
DR   eggNOG; KOG4459; Eukaryota.
DR   InParanoid; Q90830; -.
DR   PRO; PR:Q90830; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:UniProtKB.
DR   GO; GO:0018400; P:peptidyl-proline hydroxylation to 3-hydroxy-L-proline; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 1.
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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..271
FT                   /note="Cartilage-associated protein"
FT                   /id="PRO_0000006321"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   271 AA;  31494 MW;  A56343DBF604914C CRC64;
     MWRTLLAALL ATAGAQYERY SFRSFPRDEL MPLESAYRYG LDQYSTENWP ESVSYLEVSM
     RLYRLLRDTE AFCHHNCSSA GPLTAPPPAD GELAELRLLA GVLRRAQCLR RCKQGLPAFR
     QAQPGRELLE EFQRREPYKY LQFAYFKANN LPKAIAAAHT FLLKHPDDEM MQRNMAYYKS
     IPDAEEHIKD LETKPYENLF VRAVRAYNGD NWRTSISDME LALPDFFKTY DDCIAACEGS
     REIKDFKDFY LSIADHYIEV LACKVQFDIT T