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COL40_CAEEL
ID   COL40_CAEEL             Reviewed;         302 AA.
AC   P34804; O17374;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Cuticle collagen 40;
GN   Name=col-40; ORFNames=T13B5.4;
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=8299960; DOI=10.1016/0378-1119(93)90021-t;
RA   Levy A.D., Kramer J.M.;
RT   "Identification, sequence and expression patterns of the Caenorhabditis
RT   elegans col-36 and col-40 collagen-encoding genes.";
RL   Gene 137:281-285(1993).
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; L15419; AAA17726.1; -; Genomic_DNA.
DR   EMBL; FO080410; CCD63495.1; -; Genomic_DNA.
DR   PIR; T32458; T32458.
DR   PIR; T37286; T37286.
DR   RefSeq; NP_493913.2; NM_061512.2.
DR   AlphaFoldDB; P34804; -.
DR   SMR; P34804; -.
DR   STRING; 6239.T13B5.4; -.
DR   PaxDb; P34804; -.
DR   EnsemblMetazoa; T13B5.4.1; T13B5.4.1; WBGene00000617.
DR   GeneID; 173495; -.
DR   KEGG; cel:CELE_T13B5.4; -.
DR   UCSC; T13B5.4; c. elegans.
DR   CTD; 173495; -.
DR   WormBase; T13B5.4; CE45752; WBGene00000617; col-40.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000196518; -.
DR   HOGENOM; CLU_001074_4_2_1; -.
DR   InParanoid; P34804; -.
DR   OMA; FHRFETV; -.
DR   OrthoDB; 1601318at2759; -.
DR   PRO; PR:P34804; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000617; Expressed in adult organism and 1 other tissue.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0042302; F:structural constituent of cuticle; NAS:UniProtKB.
DR   GO; GO:0040002; P:collagen and cuticulin-based cuticle development; NAS:UniProtKB.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
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   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat.
FT   CHAIN           1..302
FT                   /note="Cuticle collagen 40"
FT                   /id="PRO_0000127594"
FT   REGION          79..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..143
FT                   /note="Triple-helical region"
FT   REGION          119..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..185
FT                   /note="Triple-helical region"
FT   REGION          189..221
FT                   /note="Triple-helical region"
FT   REGION          226..252
FT                   /note="Triple-helical region"
FT   REGION          255..290
FT                   /note="Triple-helical region"
FT   COMPBIAS        163..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2..18
FT                   /note="EEKQKIAEAESLKKLAF -> KLTEN (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30..31
FT                   /note="TA -> Q (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="V -> VQYFLKVHGVKKNYFQV (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="C -> S (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="G -> E (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="A -> P (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="A -> P (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179..181
FT                   /note="AGA -> EGAPGE (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="G -> R (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191..193
FT                   /note="EGP -> VGE (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202..203
FT                   /note="PA -> TS (in Ref. 1; AAA17726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   302 AA;  28130 MW;  1C8E998B133D3160 CRC64;
     MEEKQKIAEA ESLKKLAFFG ISVSTIATLT AIIAVPMLYN YMQHVQSSLQ NEVEFCKHRT
     DGLWDEFHRF ETVKGVDSRI KRDTRSRRGG YAEGGAAAGG GGGGGGSCCS CGIGAAGPAG
     APGKDGAPGE DGKAGNPGTA GSDAEAAAAP TASDFCFDCP PGPAGPAGGP GPAGPPGPAG
     ADGNTPSGGG EGPAGPPGPP GPAGNPGTDG APGNPGAPGQ VTETPGTPGP AGAAGPPGPP
     GPAGNPGSAG ASEPGPAGPA GDAGPDGAPG NAGAPGAPGE AGAPGSGGGC DHCPPPRTAP
     GY
 
 
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