COMA1_HUMAN
ID COMA1_HUMAN Reviewed; 1626 AA.
AC Q8NFW1; B7ZMH0; C9K0G4; Q8IVT9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Collagen alpha-1(XXII) chain;
DE Flags: Precursor;
GN Name=COL22A1;
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), TISSUE SPECIFICITY, AND VARIANT
RP GLY-320.
RC TISSUE=Cartilage;
RX PubMed=15016833; DOI=10.1074/jbc.m400536200;
RA Koch M., Schulze J., Hansen U., Ashwodt T., Keene D.R., Brunken W.J.,
RA Burgeson R.E., Bruckner P., Bruckner-Tuderman L.;
RT "A novel marker of tissue junctions, collagen XXII.";
RL J. Biol. Chem. 279:22514-22521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 753-1626 (ISOFORMS 2/3), AND VARIANTS GLY-320 AND
RP ASP-938.
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).
CC -!- FUNCTION: Acts as a cell adhesion ligand for skin epithelial cells and
CC fibroblasts.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NFW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFW1-2; Sequence=VSP_031087;
CC Name=3;
CC IsoId=Q8NFW1-3; Sequence=VSP_038200, VSP_031087;
CC -!- TISSUE SPECIFICITY: Restrictive expression is observed at tissue
CC junctions such as the myotendinous junction in skeletal and heart
CC muscle, the articular cartilage-synovial fluid junction, or the border
CC between the anagen hair follicle and the dermis in the skin. It is
CC deposited in the basement membrane zone of the myotendinous junction
CC and the hair follicle and associated with the extrafibrillar matrix in
CC cartilage. {ECO:0000269|PubMed:15016833}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; AF406780; AAN03620.1; -; mRNA.
DR EMBL; AC068476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042075; AAH42075.1; -; mRNA.
DR EMBL; BC144535; AAI44536.1; -; mRNA.
DR CCDS; CCDS6376.1; -. [Q8NFW1-1]
DR RefSeq; NP_690848.1; NM_152888.2. [Q8NFW1-1]
DR RefSeq; XP_011515185.1; XM_011516883.2. [Q8NFW1-2]
DR AlphaFoldDB; Q8NFW1; -.
DR SMR; Q8NFW1; -.
DR BioGRID; 127976; 3.
DR ComplexPortal; CPX-1763; Collagen type XXII trimer.
DR IntAct; Q8NFW1; 1.
DR STRING; 9606.ENSP00000303153; -.
DR GlyGen; Q8NFW1; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8NFW1; -.
DR PhosphoSitePlus; Q8NFW1; -.
DR BioMuta; COL22A1; -.
DR DMDM; 296434458; -.
DR jPOST; Q8NFW1; -.
DR MassIVE; Q8NFW1; -.
DR PaxDb; Q8NFW1; -.
DR PeptideAtlas; Q8NFW1; -.
DR PRIDE; Q8NFW1; -.
DR ProteomicsDB; 73370; -. [Q8NFW1-1]
DR ProteomicsDB; 73371; -. [Q8NFW1-2]
DR ProteomicsDB; 73372; -. [Q8NFW1-3]
DR Antibodypedia; 14343; 30 antibodies from 11 providers.
DR DNASU; 169044; -.
DR Ensembl; ENST00000303045.11; ENSP00000303153.6; ENSG00000169436.17. [Q8NFW1-1]
DR Ensembl; ENST00000435777.2; ENSP00000387655.2; ENSG00000169436.17. [Q8NFW1-3]
DR GeneID; 169044; -.
DR KEGG; hsa:169044; -.
DR MANE-Select; ENST00000303045.11; ENSP00000303153.6; NM_152888.3; NP_690848.1.
DR UCSC; uc003yvd.3; human. [Q8NFW1-1]
DR CTD; 169044; -.
DR DisGeNET; 169044; -.
DR GeneCards; COL22A1; -.
DR HGNC; HGNC:22989; COL22A1.
DR HPA; ENSG00000169436; Tissue enriched (pituitary).
DR MIM; 610026; gene.
DR neXtProt; NX_Q8NFW1; -.
DR OpenTargets; ENSG00000169436; -.
DR PharmGKB; PA134914705; -.
DR VEuPathDB; HostDB:ENSG00000169436; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159308; -.
DR HOGENOM; CLU_003584_0_0_1; -.
DR InParanoid; Q8NFW1; -.
DR OMA; PQVNCSC; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; Q8NFW1; -.
DR TreeFam; TF332934; -.
DR PathwayCommons; Q8NFW1; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q8NFW1; -.
DR BioGRID-ORCS; 169044; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; COL22A1; human.
DR GenomeRNAi; 169044; -.
DR Pharos; Q8NFW1; Tbio.
DR PRO; PR:Q8NFW1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8NFW1; protein.
DR Bgee; ENSG00000169436; Expressed in pituitary gland and 110 other tissues.
DR ExpressionAtlas; Q8NFW1; baseline and differential.
DR Genevisible; Q8NFW1; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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: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 Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 13.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Cytoplasm; Extracellular matrix;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1626
FT /note="Collagen alpha-1(XXII) chain"
FT /id="PRO_0000317615"
FT DOMAIN 38..213
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 239..427
FT /note="Laminin G-like"
FT DOMAIN 481..520
FT /note="Collagen-like 1"
FT DOMAIN 526..565
FT /note="Collagen-like 2"
FT DOMAIN 566..625
FT /note="Collagen-like 3"
FT DOMAIN 657..708
FT /note="Collagen-like 4"
FT DOMAIN 714..773
FT /note="Collagen-like 5"
FT DOMAIN 774..833
FT /note="Collagen-like 6"
FT DOMAIN 868..922
FT /note="Collagen-like 7"
FT DOMAIN 925..984
FT /note="Collagen-like 8"
FT DOMAIN 1047..1095
FT /note="Collagen-like 9"
FT DOMAIN 1118..1155
FT /note="Collagen-like 10"
FT DOMAIN 1156..1215
FT /note="Collagen-like 11"
FT DOMAIN 1249..1308
FT /note="Collagen-like 12"
FT DOMAIN 1315..1374
FT /note="Collagen-like 13"
FT DOMAIN 1387..1446
FT /note="Collagen-like 14"
FT DOMAIN 1495..1550
FT /note="Collagen-like 15"
FT DOMAIN 1575..1604
FT /note="Collagen-like 16"
FT REGION 506..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..731
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 341..627
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038200"
FT VAR_SEQ 1005..1024
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031087"
FT VARIANT 320
FT /note="S -> G (in dbSNP:rs2292927)"
FT /evidence="ECO:0000269|PubMed:15016833,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038562"
FT VARIANT 703
FT /note="P -> T (in dbSNP:rs10111520)"
FT /id="VAR_038563"
FT VARIANT 938
FT /note="A -> D (in dbSNP:rs4909444)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038564"
FT CONFLICT 753..767
FT /note="GKDGPNGPPGPPGTK -> CILAAKTAPGLKQLN (in Ref. 2;
FT AAH42075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1626 AA; 161145 MW; 91018ABA2DD670EC CRC64;
MAGLRGNAVA GLLWMLLLWS GGGGCQAQRA GCKSVHYDLV FLLDTSSSVG KEDFEKVRQW
VANLVDTFEV GPDRTRVGVV RYSDRPTTAF ELGLFGSQEE VKAAARRLAY HGGNTNTGDA
LRYITARSFS PHAGGRPRDR AYKQVAILLT DGRSQDLVLD AAAAAHRAGI RIFAVGVGEA
LKEELEEIAS EPKSAHVFHV SDFNAIDKIR GKLRRRLCEN VLCPSVRVEG DRFKHTNGGT
KEITGFDLMD LFSVKEILGK RENGAQSSYV RMGSFPVVQS TEDVFPQGLP DEYAFVTTFR
FRKTSRKEDW YIWQVIDQYS IPQVSIRLDG ENKAVEYNAV GAMKDAVRVV FRGSRVNDLF
DRDWHKMALS IQAQNVSLHI DCALVQTLPI EERENIDIQG KTVIGKRLYD SVPIDFDLQR
IVIYCDSRHA ELETCCDIPS GPCQVTVVTE PPPPPPPQRP PTPGSEQIGF LKTINCSCPA
GEKGEMGVAG PMGLPGPKGD IGAIGPVGAP GPKGEKGDVG IGPFGQGEKG EKGSLGLPGP
PGRDGSKGMR GEPGELGEPG LPGEVGMRGP QGPPGLPGPP GRVGAPGLQG ERGEKGTRGE
KGERGLDGFP GKPGDTGQQG RPGPSGVAGP QGEKGDVGPA GPPGVPGSVV QQEGLKGEQG
APGPRGHQGA PGPPGARGPI GPEGRDGPPG LQGLRGKKGD MGPPGIPGLL GLQGPPGPPG
VPGPPGPGGS PGLPGEIGFP GKPGPPGPTG PPGKDGPNGP PGPPGTKGEP GERGEDGLPG
KPGLRGEIGE QGLAGRPGEK GEAGLPGAPG FPGVRGEKGD QGEKGELGLP GLKGDRGEKG
EAGPAGPPGL PGTTSLFTPH PRMPGEQGPK GEKGDPGLPG EPGLQGRPGE LGPQGPTGPP
GAKGQEGAHG APGAAGNPGA PGHVGAPGPS GPPGSVGAPG LRGTPGKDGE RGEKGAAGEE
GSPGPVGPRG DPGAPGLPGP PGKGKDGEPG LRGSPGLPGP LGTKAACGKV RGSENCALGG
QCVKGDRGAP GIPGSPGSRG DPGIGVAGPP GPSGPPGDKG SPGSRGLPGF PGPQGPAGRD
GAPGNPGERG PPGKPGLSSL LSPGDINLLA KDVCNDCPPG PPGLPGLPGF KGDKGVPGKP
GREGTEGKKG EAGPPGLPGP PGIAGPQGSQ GERGADGEVG QKGDQGHPGV PGFMGPPGNP
GPPGADGIAG AAGPPGIQGS PGKEGPPGPQ GPSGLPGIPG EEGKEGRDGK PGPPGEPGKA
GEPGLPGPEG ARGPPGFKGH TGDSGAPGPR GESGAMGLPG QEGLPGKDGD TGPTGPQGPQ
GPRGPPGKNG SPGSPGEPGP SGTPGQKGSK GENGSPGLPG FLGPRGPPGE PGEKGVPGKE
GVPGKPGEPG FKGERGDPGI KGDKGPPGGK GQPGDPGIPG HKGHTGLMGP QGLPGENGPV
GPPGPPGQPG FPGLRGESPS METLRRLIQE ELGKQLETRL AYLLAQMPPA YMKSSQGRPG
PPGPPGKDGL PGRAGPMGEP GRPGQGGLEG PSGPIGPKGE RGAKGDPGAP GVGLRGEMGP
PGIPGQPGEP GYAKDGLPGI PGPQGETGPA GHPGLPGPPG PPGQCDPSQC AYFASLAARP
GNVKGP
