CO155_CAEEL
ID CO155_CAEEL Reviewed; 299 AA.
AC Q21184; A9UJN5; Q20807;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative cuticle collagen 155;
DE Flags: Precursor;
GN Name=col-155; ORFNames=F55C10.3;
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 [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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; Z74036; CAA98487.2; -; Genomic_DNA.
DR EMBL; Z74039; CAA98487.2; JOINED; Genomic_DNA.
DR PIR; T22706; T22706.
DR RefSeq; NP_505888.2; NM_073487.3.
DR AlphaFoldDB; Q21184; -.
DR SMR; Q21184; -.
DR STRING; 6239.F55C10.3; -.
DR PaxDb; Q21184; -.
DR EnsemblMetazoa; F55C10.3.1; F55C10.3.1; WBGene00000728.
DR GeneID; 186301; -.
DR KEGG; cel:CELE_F55C10.3; -.
DR UCSC; F55C10.3; c. elegans.
DR CTD; 186301; -.
DR WormBase; F55C10.3; CE05953; WBGene00000728; col-155.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196049; -.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; Q21184; -.
DR OMA; IPCKKPL; -.
DR PhylomeDB; Q21184; -.
DR PRO; PR:Q21184; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000728; Expressed in larva and 3 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; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..299
FT /note="Putative cuticle collagen 155"
FT /id="PRO_0000127604"
FT REGION 103..132
FT /note="Triple-helical region"
FT REGION 107..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..177
FT /note="Triple-helical region"
FT REGION 181..202
FT /note="Triple-helical region"
FT REGION 216..278
FT /note="Triple-helical region"
FT COMPBIAS 113..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 29307 MW; 0C4207091777AD6F CRC64;
MEFEQRIKAY RFVAYSAVAF SVVAVLSVCI TLPMVHNYVH HVKRTMNQEV QFCRGSAKDI
WTEVNELKSI QHANRTARQS GYDAGVNGGS ASTGGCDACC LPGAAGPAGT PGKPGRPGKP
GAPGLPGNPG HPPQQPCDPI TPPPCQPCPQ GPPGPPGPPG PSGDAGGNGN PGSPGQDGQP
GAPGNKGPSG PNGNPGAPGA PGQPGQDAPS EPITPGAPGP QGTPGPQGPP GQPGQPGHDG
QPGAPGPKGP NGNPGQPGAD GNPGAPGQSG TPGGVGEKGI CPKYCAIDGG VFFEDGTRR