COL8_CAEEL
ID COL8_CAEEL Reviewed; 282 AA.
AC P18833; Q19359;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cuticle collagen 8;
DE Flags: Precursor;
GN Name=col-8; ORFNames=F11H8.3;
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].
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 -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; M25479; AAA27993.1; -; Genomic_DNA.
DR EMBL; FO080391; CCD63397.1; -; Genomic_DNA.
DR PIR; JS0168; JS0168.
DR PIR; T16036; T16036.
DR RefSeq; NP_498533.2; NM_066132.6.
DR AlphaFoldDB; P18833; -.
DR BioGRID; 41193; 1.
DR STRING; 6239.F11H8.3; -.
DR EPD; P18833; -.
DR PaxDb; P18833; -.
DR PeptideAtlas; P18833; -.
DR EnsemblMetazoa; F11H8.3.1; F11H8.3.1; WBGene00000597.
DR GeneID; 175981; -.
DR UCSC; F11H8.3; c. elegans.
DR CTD; 175981; -.
DR WormBase; F11H8.3; CE51260; WBGene00000597; col-8.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196588; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; P18833; -.
DR OMA; DEMFEFR; -.
DR OrthoDB; 1766544at2759; -.
DR PRO; PR:P18833; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000597; Expressed in adult organism and 2 other 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 Pfam; PF01484; Col_cuticle_N; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..282
FT /note="Cuticle collagen 8"
FT /id="PRO_0000006423"
FT REGION 86..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..124
FT /note="Triple-helical region"
FT REGION 141..269
FT /note="Triple-helical region"
FT CONFLICT 43
FT /note="R -> T (in Ref. 1; AAA27993)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="R -> C (in Ref. 1; AAA27993)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="R -> C (in Ref. 1; AAA27993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 28150 MW; 9A49862A5D88FEEC CRC64;
MLVCVFVALY TMMGLLTDIK QLQSDFDDEM FEFRAITKDT WQRIVTKHTY PGGVDEETIE
SHPPTFETLF GTRKARQAYP EQCNCGPKSE GCPAGPPGPP GEGGQSGEPG HDGDDGKPGA
PGVIVAITHD IPGGCIKCPP GRPGPRGPSG LVGPAGPAGD QGRHGPPGPT GGQGGPGEQG
DAGRPGAAGR PGPPGPRGEP GTEYRPGQAG RAGPPGPRGP PGPEGNPGGA GEDGNQGPVG
HPGVPGRPGI PGKSGTCGEH GGPGEPGPDA GYCPCPGRSY KA