COOA1_HUMAN
ID COOA1_HUMAN Reviewed; 1714 AA.
AC Q17RW2; C9J1X6; Q14BD7; Q59EX5; Q5VY50; Q7Z5L5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Collagen alpha-1(XXIV) chain;
DE Flags: Precursor;
GN Name=COL24A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS VAL-61;
RP SER-546 AND SER-731.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-61.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 827-1714 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May participate in regulating type I collagen fibrillogenesis
CC at specific anatomical locations during fetal development.
CC {ECO:0000269|PubMed:12874293}.
CC -!- INTERACTION:
CC Q17RW2; Q92624: APPBP2; NbExp=6; IntAct=EBI-2529266, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q17RW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q17RW2-2; Sequence=VSP_031090;
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AY244357; AAP80185.1; -; mRNA.
DR EMBL; AC099561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73193.1; -; Genomic_DNA.
DR EMBL; BC113654; AAI13655.1; -; mRNA.
DR EMBL; BC117170; AAI17171.1; -; mRNA.
DR EMBL; AB209686; BAD92923.1; -; mRNA.
DR CCDS; CCDS41353.1; -. [Q17RW2-1]
DR RefSeq; NP_690850.2; NM_152890.5. [Q17RW2-1]
DR AlphaFoldDB; Q17RW2; -.
DR BioGRID; 129112; 1.
DR ComplexPortal; CPX-1765; Collagen type XXIV trimer.
DR IntAct; Q17RW2; 3.
DR MINT; Q17RW2; -.
DR STRING; 9606.ENSP00000359603; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyGen; Q17RW2; 3 sites.
DR iPTMnet; Q17RW2; -.
DR PhosphoSitePlus; Q17RW2; -.
DR BioMuta; COL24A1; -.
DR DMDM; 290457636; -.
DR EPD; Q17RW2; -.
DR jPOST; Q17RW2; -.
DR MassIVE; Q17RW2; -.
DR PaxDb; Q17RW2; -.
DR PeptideAtlas; Q17RW2; -.
DR PRIDE; Q17RW2; -.
DR ProteomicsDB; 61168; -. [Q17RW2-1]
DR ProteomicsDB; 61169; -. [Q17RW2-2]
DR Antibodypedia; 33574; 28 antibodies from 9 providers.
DR DNASU; 255631; -.
DR Ensembl; ENST00000370571.7; ENSP00000359603.2; ENSG00000171502.15. [Q17RW2-1]
DR GeneID; 255631; -.
DR KEGG; hsa:255631; -.
DR MANE-Select; ENST00000370571.7; ENSP00000359603.2; NM_152890.7; NP_690850.2.
DR UCSC; uc001dlj.4; human. [Q17RW2-1]
DR CTD; 255631; -.
DR DisGeNET; 255631; -.
DR GeneCards; COL24A1; -.
DR HGNC; HGNC:20821; COL24A1.
DR HPA; ENSG00000171502; Tissue enhanced (brain).
DR MIM; 610025; gene.
DR neXtProt; NX_Q17RW2; -.
DR OpenTargets; ENSG00000171502; -.
DR PharmGKB; PA134932695; -.
DR VEuPathDB; HostDB:ENSG00000171502; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000162448; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; Q17RW2; -.
DR OMA; IQGKRGH; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; Q17RW2; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; Q17RW2; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q17RW2; -.
DR BioGRID-ORCS; 255631; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; COL24A1; human.
DR GenomeRNAi; 255631; -.
DR Pharos; Q17RW2; Tbio.
DR PRO; PR:Q17RW2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q17RW2; protein.
DR Bgee; ENSG00000171502; Expressed in Brodmann (1909) area 23 and 108 other tissues.
DR ExpressionAtlas; Q17RW2; baseline and differential.
DR Genevisible; Q17RW2; HS.
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:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 13.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1714
FT /note="Collagen alpha-1(XXIV) chain"
FT /id="PRO_0000317616"
FT DOMAIN 141..217
FT /note="Laminin G-like"
FT DOMAIN 487..542
FT /note="Collagen-like 1"
FT DOMAIN 552..611
FT /note="Collagen-like 2"
FT DOMAIN 660..719
FT /note="Collagen-like 3"
FT DOMAIN 741..797
FT /note="Collagen-like 4"
FT DOMAIN 798..857
FT /note="Collagen-like 5"
FT DOMAIN 858..887
FT /note="Collagen-like 6"
FT DOMAIN 888..947
FT /note="Collagen-like 7"
FT DOMAIN 948..1007
FT /note="Collagen-like 8"
FT DOMAIN 1011..1052
FT /note="Collagen-like 9"
FT DOMAIN 1053..1112
FT /note="Collagen-like 10"
FT DOMAIN 1116..1170
FT /note="Collagen-like 11"
FT DOMAIN 1172..1196
FT /note="Collagen-like 12"
FT DOMAIN 1201..1249
FT /note="Collagen-like 13"
FT DOMAIN 1252..1306
FT /note="Collagen-like 14"
FT DOMAIN 1309..1353
FT /note="Collagen-like 15"
FT DOMAIN 1354..1413
FT /note="Collagen-like 16"
FT DOMAIN 1420..1479
FT /note="Collagen-like 17"
FT DOMAIN 1515..1714
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 487..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1459..1479
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_031090"
FT VARIANT 61
FT /note="A -> V (in dbSNP:rs11161747)"
FT /evidence="ECO:0000269|PubMed:12874293,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_062865"
FT VARIANT 151
FT /note="P -> L (in dbSNP:rs1027819)"
FT /id="VAR_055672"
FT VARIANT 293
FT /note="I -> T (in dbSNP:rs17128866)"
FT /id="VAR_055673"
FT VARIANT 481
FT /note="M -> L (in dbSNP:rs10493784)"
FT /id="VAR_055674"
FT VARIANT 546
FT /note="P -> S (in dbSNP:rs11161732)"
FT /evidence="ECO:0000269|PubMed:12874293"
FT /id="VAR_055675"
FT VARIANT 641
FT /note="R -> H (in dbSNP:rs60891279)"
FT /id="VAR_061116"
FT VARIANT 731
FT /note="P -> S (in dbSNP:rs641712)"
FT /evidence="ECO:0000269|PubMed:12874293"
FT /id="VAR_055676"
FT VARIANT 1423
FT /note="G -> R (in dbSNP:rs7520146)"
FT /id="VAR_038565"
FT CONFLICT 828..849
FT /note="GYAGEPGPEGLKGEVGDQGNIG -> ITVFATLYSFLTGRSRRSRKYW (in
FT Ref. 5; BAD92923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1714 AA; 175496 MW; 2AC82E13DB5BBD3D CRC64;
MHLRAHRTRR GKVSPTAKTK SLLHFIVLCV AGVVVHAQEQ GIDILHQLGL GGKDVRHSSP
ATAVPSASTP LPQGVHLTES GVIFKNDAYI ETPFVKILPV NLGQPFTILT GLQSHRVNNA
FLFSIRNKNR LQLGVQLLPK KLVVHIRGKQ PAVFNYSVHD EQWHSFAITI RNQSVSMFVE
CGKKYFSTET IPEVQTFDSN SVFTLGSMNN NSIHFEGIVC QLDIIPSAEA SADYCRYVKQ
QCRQADKYQP ETSIPCTTLI PTKIPEHSPP PKLFAEKVLS EDTFTEGKSI PNIIKNDSET
VYKRQEHQIS RSQLSSLQSG NVSAVDLTNH GIQAKEMITE EDTQTNFSLS VTTHRISEAK
MNTKEKFSSL LNMSDNITQH DDRVTGLSLF KKMPSILPQI KQDTITNLKK AITANLHTNE
LMEMQPILNT SLHRVTNEPS VDNHLDLRKE GEFYPDATYP IENSYETELY DYYYYEDLNT
MLEMEYLRGP KGDTGPPGPP GPAGIPGPSG KRGPRGIPGP HGNPGLPGLP GPKGPKGDPG
FSPGQPVPGE KGDQGLSGLM GPPGMQGDKG LKGHPGLPGL PGEQGIPGFA GNIGSPGYPG
RQGLAGPEGN PGPKGAQGFI GSPGEAGQLG PEGERGIPGI RGKKGFKGRQ GFPGDFGDRG
PAGLDGSPGL VGGTGPPGFP GLRGSVGPVG PIGPAGIPGP MGLSGNKGLP GIKGDKGEQG
TAGELGEPGY PGDKGAVGLP GPPGMRGKSG PSGQTGDPGL QGPSGPPGPE GFPGDIGIPG
QNGPEGPKGL LGNRGPPGPP GLKGTQGEEG PIGAFGELGP RGKPGQKGYA GEPGPEGLKG
EVGDQGNIGK IGETGPVGLP GEVGMTGSIG EKGERGSPGP LGPQGEKGVM GYPGPPGVPG
PIGPLGLPGH VGARGPPGSQ GPKGQRGSRG PDGLLGEQGI QGAKGEKGDQ GKRGPHGLIG
KTGNPGERGF QGKPGLQGLP GSTGDRGLPG EPGLRGLQGD VGPPGEMGME GPPGTEGESG
LQGEPGAKGD VGTAGSVGGT GEPGLRGEPG APGEEGLQGK DGLKGVPGGR GLPGEDGEKG
EMGLPGIIGP LGRSGQTGLP GPEGIVGIPG QRGRPGKKGD KGQIGPTGEV GSRGPPGKIG
KSGPKGARGT RGAVGHLGLM GPDGEPGIPG YRGHQGQPGP SGLPGPKGEK GYPGEDSTVL
GPPGPRGEPG PVGDQGERGE PGAEGYKGHV GVPGLRGATG QQGPPGEPGD QGEQGLKGER
GSEGNKGKKG APGPSGKPGI PGLQGLLGPK GIQGYHGADG ISGNPGKIGP PGKQGLPGIR
GGPGRTGLAG APGPPGVKGS SGLPGSPGIQ GPKGEQGLPG QPGIQGKRGH RGAQGDQGPC
GDPGLKGQPG EYGVQGLTGF QGFPGPKGPE GDAGIVGISG PKGPIGHRGN TGPLGREGII
GPTGRTGPRG EKGFRGETGP QGPRGQPGPP GPPGAPGPRK QMDINAAIQA LIESNTALQM
ESYQNTEVTL IDHSEEIFKT LNYLSNLLHS IKNPLGTRDN PARICKDLLN CEQKVSDGKY
WIDPNLGCPS DAIEVFCNFS AGGQTCLPPV SVTKLEFGVG KVQMNFLHLL SSEATHIITI
HCLNTPRWTS TQTSGPGLPI GFKGWNGQIF KVNTLLEPKV LSDDCKIQDG SWHKATFLFH
TQEPNQLPVI EVQKLPHLKT ERKYYIDSSS VCFL
