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Database: UniProt
Entry: COL6_CAEEL
LinkDB: COL6_CAEEL
Original site: COL6_CAEEL 
ID   COL6_CAEEL              Reviewed;         329 AA.
AC   P18831; Q23437;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Cuticle collagen 6;
DE   AltName: Full=Protein roller-8;
GN   Name=rol-8; Synonyms=col-6; ORFNames=ZK1290.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=2753356; DOI=10.1016/0378-1119(89)90173-x;
RA   Cox G.N., Fields C., Kramer J.M., Rosenzweig B., Hirsh D.;
RT   "Sequence comparisons of developmentally regulated collagen genes of
RT   Caenorhabditis elegans.";
RL   Gene 76:331-344(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Nematode cuticles are composed largely of collagen-like
CC       proteins. The cuticle functions both as an exoskeleton and as a barrier
CC       to protect the worm from its environment.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=P18831-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=P18831-2; Sequence=VSP_001238;
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; M25477; AAA27991.1; -; Genomic_DNA.
DR   EMBL; FO080700; CCD65932.1; -; Genomic_DNA.
DR   EMBL; FO080700; CCD65931.1; -; Genomic_DNA.
DR   PIR; JS0167; JS0167.
DR   PIR; T34507; T34507.
DR   RefSeq; NP_495582.1; NM_063181.5. [P18831-1]
DR   RefSeq; NP_871912.1; NM_182112.3.
DR   AlphaFoldDB; P18831; -.
DR   SMR; P18831; -.
DR   BioGRID; 39560; 1.
DR   STRING; 6239.ZK1290.3a.1; -.
DR   EPD; P18831; -.
DR   PaxDb; 6239-ZK1290-3a; -.
DR   PeptideAtlas; P18831; -.
DR   EnsemblMetazoa; ZK1290.3.1; ZK1290.3.1; WBGene00004398. [P18831-1]
DR   GeneID; 174226; -.
DR   KEGG; cel:CELE_ZK1290.3; -.
DR   UCSC; ZK1290.3a; c. elegans. [P18831-1]
DR   AGR; WB:WBGene00004398; -.
DR   WormBase; ZK1290.3a; CE29156; WBGene00004398; rol-8. [P18831-1]
DR   WormBase; ZK1290.3b; CE32085; WBGene00004398; rol-8. [P18831-2]
DR   eggNOG; KOG3544; Eukaryota.
DR   HOGENOM; CLU_001074_4_2_1; -.
DR   InParanoid; P18831; -.
DR   OMA; RDMWLEM; -.
DR   OrthoDB; 2882978at2759; -.
DR   PhylomeDB; P18831; -.
DR   PRO; PR:P18831; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004398; Expressed in material anatomical entity and 3 other cell types or tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF286; CUTICLE COLLAGEN 6; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Collagen; Cuticle; Disulfide bond;
KW   Reference proteome; Repeat.
FT   CHAIN           1..329
FT                   /note="Cuticle collagen 6"
FT                   /id="PRO_0000127590"
FT   REGION          142..171
FT                   /note="Triple-helical region"
FT   REGION          146..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..212
FT                   /note="Triple-helical region"
FT   REGION          216..248
FT                   /note="Triple-helical region"
FT   REGION          253..279
FT                   /note="Triple-helical region"
FT   REGION          282..320
FT                   /note="Triple-helical region"
FT   COMPBIAS        196..210
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..290
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         197..261
FT                   /note="MGPKGPPGPKGSPGEPPQDGKSGDDGMAGQPGPIGRPGRDGMKGAPGAAGRL
FT                   IPVPGPQGAPGKP -> I (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001238"
FT   CONFLICT        245
FT                   /note="A -> R (in Ref. 1; AAA27991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  32476 MW;  E1D0B6EF68322E97 CRC64;
     MDVKETEEQR QMRRIAFVAV VVSTAAVIAS VVTLPMLYNY VQSFQSHLMV ETDYCKARSR
     DMWLEMTALQ AGKGMGHRMK RAWLFGQWIP ETSAGGGGSG NGGGNYGSGA STGGGANTAG
     YGGYGAAVNA EPAAVCCTCN QGAAGPPGPE GPPGNDGKDG RNGNDGKNGR DAEVLPAPAS
     EPCIICPTGA PGPMGAMGPK GPPGPKGSPG EPPQDGKSGD DGMAGQPGPI GRPGRDGMKG
     APGAAGRLIP VPGPQGAPGK PGPIGPPGPK GNPGPDGQSY QGPPGPPGDS GTPGHEGRAG
     PNGPAGPPGD NGEKGDCGHC PPPRTPPGY
//
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