COL36_CAEEL
ID COL36_CAEEL Reviewed; 307 AA.
AC P34803;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cuticle collagen 36;
GN Name=col-36; ORFNames=C27H5.5;
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 [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; L15418; AAA17445.1; -; Unassigned_DNA.
DR EMBL; FO080695; CCD65892.1; -; Genomic_DNA.
DR PIR; T37287; T37287.
DR RefSeq; NP_495487.1; NM_063086.3.
DR AlphaFoldDB; P34803; -.
DR STRING; 6239.C27H5.5a; -.
DR PaxDb; P34803; -.
DR PRIDE; P34803; -.
DR EnsemblMetazoa; C27H5.5.1; C27H5.5.1; WBGene00000613.
DR GeneID; 174178; -.
DR KEGG; cel:CELE_C27H5.5; -.
DR UCSC; C27H5.5; c. elegans.
DR CTD; 174178; -.
DR WormBase; C27H5.5; CE06893; WBGene00000613; col-36.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196361; -.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; P34803; -.
DR OMA; EEGSCDH; -.
DR OrthoDB; 1545625at2759; -.
DR PRO; PR:P34803; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000613; Expressed in material anatomical entity 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 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.
FT CHAIN 1..307
FT /note="Cuticle collagen 36"
FT /id="PRO_0000127593"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..105
FT /note="Triple-helical region"
FT REGION 116..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..150
FT /note="Triple-helical region"
FT REGION 167..187
FT /note="Triple-helical region"
FT REGION 194..226
FT /note="Triple-helical region"
FT REGION 231..257
FT /note="Triple-helical region"
FT REGION 260..295
FT /note="Triple-helical region"
FT COMPBIAS 201..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 30126 MW; 9C7206CC18660F0B CRC64;
MKIDKEDDQQ QQMRRVAFFA VAVSTAAVIS SIVTLPMIYS YVQSFQSHLI METEFCKTRA
RDMWVEMQVL HKSGVTRSRR DAGYKEGSGS GGSGSGGYGG PTGAGADIGP TCCPCQQGPA
GPPGPAGDTG PNGNDGHHGA PGVPGKEGSI LSSALPPSEP CIICPPGPQG AVGQQGPKGP
PGPKGKSQER AADGKNGEPG MIGPPGPPGG VGEPGPPGPA GQPGRVIQVN GAAGPAGPRG
VKGPPGPKGL PGIAGLTEIG GQGPPGDAGG PGPVGGQGPP GPQGPQGPPG DEGSCDHCPE
PRTPPGY