ID COL39_CAEEL Reviewed; 323 AA.
AC Q09455;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Cuticle collagen 39;
DE Flags: Precursor;
GN Name=col-39; ORFNames=C09G5.4;
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 [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; Z46791; CAA86757.1; -; Genomic_DNA.
DR PIR; T19142; T19142.
DR RefSeq; NP_496309.1; NM_063908.5.
DR AlphaFoldDB; Q09455; -.
DR SMR; Q09455; -.
DR STRING; 6239.C09G5.4.1; -.
DR EPD; Q09455; -.
DR PaxDb; 6239-C09G5-4; -.
DR PeptideAtlas; Q09455; -.
DR EnsemblMetazoa; C09G5.4.1; C09G5.4.1; WBGene00000616.
DR GeneID; 174651; -.
DR KEGG; cel:CELE_C09G5.4; -.
DR UCSC; C09G5.4; c. elegans.
DR AGR; WB:WBGene00000616; -.
DR WormBase; C09G5.4; CE01484; WBGene00000616; col-39.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196208; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; Q09455; -.
DR OMA; EQQECIK; -.
DR OrthoDB; 2878718at2759; -.
DR PRO; PR:Q09455; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000616; Expressed in larva and 2 other cell types or 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 PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF394; CUTICLE COLLAGEN 39; 1.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..323
FT /note="Cuticle collagen 39"
FT /id="PRO_0000006427"
FT REGION 80..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..125
FT /note="Triple-helical region"
FT REGION 138..200
FT /note="Triple-helical region"
FT REGION 203..265
FT /note="Triple-helical region"
FT COMPBIAS 142..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 31595 MW; F84F106EBBB9174C CRC64;
MTGPTCLAVV AGISGVFVFG ALFSVAQIYN DISSFADNAH RELGEFKGFA NDAWNSMVNH
DDATRVARSV FVRRHKKHSQ CNCGPQASNC PAGPPGPPGA PGDRGLDGQP GGAGNPGQPG
VAGPKSHEQQ ECIKCPAGSP GPAGAPGAPG PQGPNGQPGH PGQGGSQGPA GPRGPAGDAG
APGQVGAPGN PGQAGRGGQR SHGLPGPSGA PGPQGPSGAP GQPGQSGGQG QQGPAGPAGP
DGQPGQPGQD GQAGAPGNDG APGADAAYCP CPSRSGSSSA VETGAAEQGY RHRAVAARHR
NVIRRRVAKK RVVKKKRVVA RQA
//
