COL7_CAEEL
ID COL7_CAEEL Reviewed; 316 AA.
AC P18832; Q93210;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cuticle collagen 7;
DE Flags: Precursor;
GN Name=col-7; ORFNames=C15A11.5;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
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).
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; Z79694; CAB01961.1; -; Genomic_DNA.
DR EMBL; M25478; AAA27992.1; -; Genomic_DNA.
DR PIR; T19291; T19291.
DR RefSeq; NP_492090.1; NM_059689.5.
DR AlphaFoldDB; P18832; -.
DR SMR; P18832; -.
DR STRING; 6239.C15A11.5; -.
DR PaxDb; P18832; -.
DR EnsemblMetazoa; C15A11.5.1; C15A11.5.1; WBGene00000596.
DR GeneID; 172494; -.
DR KEGG; cel:CELE_C15A11.5; -.
DR UCSC; C15A11.5; c. elegans.
DR CTD; 172494; -.
DR WormBase; C15A11.5; CE08173; WBGene00000596; col-7.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196071; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; P18832; -.
DR OMA; HRNVSRH; -.
DR OrthoDB; 1490155at2759; -.
DR PRO; PR:P18832; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000596; Expressed in adult organism and 1 other tissue.
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 Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 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..34
FT /evidence="ECO:0000255"
FT CHAIN 35..316
FT /note="Cuticle collagen 7"
FT /id="PRO_0000006422"
FT REGION 78..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..126
FT /note="Triple-helical region"
FT REGION 139..198
FT /note="Triple-helical region"
FT REGION 204..263
FT /note="Triple-helical region"
FT REGION 281..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 48..60
FT /note="Missing (in Ref. 2; AAA27992)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="G -> P (in Ref. 2; AAA27992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 31240 MW; 7C311F63FCBD702B CRC64;
MSSATFLSVM AGLSGIVVFG ALISVFHIYS DINSFVEDSH RELGEFKGFA NDAWNSMINQ
DDSVRMARSV FGRRRQKKQS QCNCGQQASN CPAGPPGPPG ASGDKGHDGQ PGQAGKPGQP
GVAGPSHHQK QECIKCPQGL PGPAGVPGQP GPKGPNGNPG APAQGGGQGP PGPPGPAGSA
GSPGQAGAPG NPGSPGKSGQ RGRGLPGPSG APGPQGPPGA PGQPGSGNAP GPAGPPGPAG
PNGQPGHPGQ DGQPGAPGND GTPGSDAAYC PCPTRSSVLR HRNVNRHRAA ASKKRVVAKK
RVAKKRVVAA RRHVQA