COOA1_MOUSE
ID COOA1_MOUSE Reviewed; 1733 AA.
AC Q30D77; B2RT51; E9QNS5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Collagen alpha-1(XXIV) chain;
DE Flags: Precursor;
GN Name=Col24a1;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=16373341; DOI=10.1074/jbc.m509923200;
RA Matsuo N., Tanaka S., Gordon M.K., Koch M., Yoshioka H., Ramirez F.;
RT "CREB-AP1 protein complexes regulate transcription of the collagen XXIV
RT gene (Col24a1) in osteoblasts.";
RL J. Biol. Chem. 281:5445-5452(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 DEVELOPMENTAL STAGE.
RC TISSUE=Cartilage;
RX PubMed=12874293; DOI=10.1074/jbc.m302112200;
RA Koch M., Laub F., Zhou P., Hahn R.A., Tanaka S., Burgeson R.E.,
RA Gerecke D.R., Ramirez F., Gordon M.K.;
RT "Collagen XXIV, a vertebrate fibrillar collagen with structural features of
RT invertebrate collagens: selective expression in developing cornea and
RT bone.";
RL J. Biol. Chem. 278:43236-43244(2003).
CC -!- FUNCTION: Involved in osteoblast differentiation.
CC {ECO:0000269|PubMed:16373341}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed in skeleton. Found at ossification
CC centers of the craniofacial, axial and appendicular skeleton. Also
CC expressed in retina and to a lower extent in cornea, skin and tendon.
CC {ECO:0000269|PubMed:16373341}.
CC -!- DEVELOPMENTAL STAGE: Expression is confined to the developing eye and
CC skeleton. First level of expression are detectable around 15 dpc.
CC {ECO:0000269|PubMed:12874293}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; DQ157748; ABA39881.1; -; mRNA.
DR EMBL; AC123711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139134; AAI39135.1; -; mRNA.
DR CCDS; CCDS17892.1; -.
DR RefSeq; NP_082046.2; NM_027770.3.
DR RefSeq; XP_006502160.1; XM_006502097.3.
DR RefSeq; XP_006502161.1; XM_006502098.3.
DR RefSeq; XP_011238534.1; XM_011240232.2.
DR AlphaFoldDB; Q30D77; -.
DR SMR; Q30D77; -.
DR ComplexPortal; CPX-3001; Collagen type XXIV trimer.
DR STRING; 10090.ENSMUSP00000029848; -.
DR GlyGen; Q30D77; 4 sites.
DR iPTMnet; Q30D77; -.
DR PhosphoSitePlus; Q30D77; -.
DR PaxDb; Q30D77; -.
DR PRIDE; Q30D77; -.
DR ProteomicsDB; 283605; -.
DR DNASU; 71355; -.
DR Ensembl; ENSMUST00000029848; ENSMUSP00000029848; ENSMUSG00000028197.
DR GeneID; 71355; -.
DR KEGG; mmu:71355; -.
DR UCSC; uc008rqm.1; mouse.
DR CTD; 255631; -.
DR MGI; MGI:1918605; Col24a1.
DR VEuPathDB; HostDB:ENSMUSG00000028197; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000163583; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; Q30D77; -.
DR OMA; IQGKRGH; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; Q30D77; -.
DR TreeFam; TF344135; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 71355; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Col24a1; mouse.
DR PRO; PR:Q30D77; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q30D77; protein.
DR Bgee; ENSMUSG00000028197; Expressed in hindlimb long bone and 126 other tissues.
DR ExpressionAtlas; Q30D77; baseline and differential.
DR Genevisible; Q30D77; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 2.
DR Pfam; PF01391; Collagen; 12.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 2: Evidence at transcript level;
KW Collagen; Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1733
FT /note="Collagen alpha-1(XXIV) chain"
FT /id="PRO_0000317617"
FT DOMAIN 102..229
FT /note="Laminin G-like"
FT DOMAIN 506..561
FT /note="Collagen-like 1"
FT DOMAIN 577..636
FT /note="Collagen-like 2"
FT DOMAIN 679..738
FT /note="Collagen-like 3"
FT DOMAIN 742..801
FT /note="Collagen-like 4"
FT DOMAIN 802..861
FT /note="Collagen-like 5"
FT DOMAIN 886..945
FT /note="Collagen-like 6"
FT DOMAIN 946..1005
FT /note="Collagen-like 7"
FT DOMAIN 1006..1065
FT /note="Collagen-like 8"
FT DOMAIN 1072..1131
FT /note="Collagen-like 9"
FT DOMAIN 1135..1189
FT /note="Collagen-like 10"
FT DOMAIN 1191..1215
FT /note="Collagen-like 11"
FT DOMAIN 1220..1279
FT /note="Collagen-like 12"
FT DOMAIN 1316..1375
FT /note="Collagen-like 13"
FT DOMAIN 1376..1435
FT /note="Collagen-like 14"
FT DOMAIN 1439..1498
FT /note="Collagen-like 15"
FT DOMAIN 1534..1733
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 257..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1146
FT /note="T -> M (in Ref. 1; ABA39881 and 3; AAI39135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1733 AA; 175733 MW; 4DAA1E630EB923CE CRC64;
MHLGAYRTRH GKVSPTTETK LFLRFIVLCV VWISVHAQGQ GIDILQQLGL GGRDVRYTSS
VTAVPSSSWS TPLPQGVHLT DFGVILTDNA YIESPLVNIL PISLRQPLTV LIGLQSFKVN
NAFLFSIRNN NRLQFGVQLL PKKLIVHVGG KQTVTFNYSA HDERWHSFAI TVDHHVISMF
VECGKRHFSG ETTSDVQTFD PHSVFTLGSI NNSSAHFEGT VCQLEIMPST AASAEYCRHL
KQQCLRADAS QAQRNLPHTA GMPTRHPAHT PLPRGFPGTD SPQKRFTEQD SLPKGFDGTE
LPRETFADGK SIPNNRSNGS ATVHESQEHQ TPRAQLTSFH SGNISAVTLP NYRIQAKEIT
TKEETNLTLS VAHHLPSEAR MNEEGRINPL FAGFDNITQH EEAAGLPLPK KASSGFAHTN
QDTMKNLEKA LTANLYTNEL IEMERILNST LYRVMYGPSV DNHLELRKEG EFYPDATNPI
EGSYEPQAYD YYSYEDYNAV LDMEYLRGPK GDPGPPGPPG PMGIPGPSGK RGPRGIPGPH
GNPGLPGLPG PKGPKGDPGL SPGQAASGEK GDPGLLGLVG PPGLQGAKGL KGHPGLPGLR
GEHGLPGLAG NIGSPGYPGR QGLAGPEGNP GSKGVRGFIG SPGEVGQLGP EGERGTPGVR
GKKGPKGRQG FPGDFGDRGP AGLDGSPGLV GGTGPPGFPG VTGSVGPAGP TGPPGAPGPM
GLSGSRGPSG IKGDKGEQGV AGEPGEPGYP GDKGNIGSPG PPGIRGKSGP SGQPGDPGPQ
GPSGPPGPEG FPGDIGIPGQ NGPEGPKGHL GNRGPPGPPG LKGTQGEEGP IGPFGELGSR
GKPGRKGYMG EPGPEGLKGE VGDQGDIGKT GETGPVGLPG EVGITGSIGE KGERGSPGPL
GPQGEKGVMG YPGPPGAPGP MGPLGLPGLV GARGAPGSPG PKGQRGPRGP DGLAGDQGGH
GAKGEKGNQG KRGLPGLPGK AGSPGERGVQ GKPGFQGLPG SSGDVGPAGE PGPRGLPGIA
GLPGEMGVEG PPGTEGDSGL QGEPGAKGDG GPAGSAGATG EPGPRGEPGA PGEEGLQGKD
GLKGAPGGSG LPGEDGDKGE MGLPGTAGPV GRPGQMGLPG PEGIVGTPGQ RGRLGKKGDK
GQVGPTGEAG SRGPPGSVGE NGPKGARGTR GAVGPLGLMG PEGEPGIPGY RGHQGQPGPS
GLPGPKGEKG YPGEDSTVLG PPGPPGEPGP MGEQGETGEH GEEGYKGHMG VPGLRGATGQ
QGPPGEPGDQ GGQGPKGERG SEGPQGKRGV PGPSGKPGIP GVPGFPGPKG LQGYPGVDGM
SGYPGKPGLP GKQGLLGVPG SPGRTGVAGS PGPQGGKGAS GPPGSPGAPG PKGEQGLPGQ
PGVPGQRGHR GTPGDQGLRG APGLKGQPGE HGDQGLAGFQ GFPGPRGPEG DAGIVGIVGP
KGPIGQRGNT GPLGREGIIG PTGGTGPRGE KGFRGETGPQ GPRGQPGPPG PPGAPGPRRQ
MDINAAIRAL IESNSAQQME SYQNTEGTLI SHSSDIFKTL TYLSSLLSSI KNPLGTRENP
ARICKDLLSC QYKVSDGKYW IDPNLGCSSD AFEVFCNFSA GGQTCLSPVS VTKLEFGVSK
VQMNFLHLLS SEATHTITIH CLNTPRWSST WADGPELPIS FKGWNGQIFE ENTLLEPQVL
SDDCKIQDGS WHKAKFLFHT QNPNQLPVTE VQNLPHLGTE QKRYIESNSV CFL
