COL38_CAEEL
ID COL38_CAEEL Reviewed; 287 AA.
AC Q20754;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cuticle collagen 38 {ECO:0000303|PubMed:29604168};
DE Flags: Precursor;
GN Name=col-38 {ECO:0000312|WormBase:F54C9.4};
GN ORFNames=F54C9.4 {ECO:0000312|WormBase:F54C9.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24569038; DOI=10.1534/g3.113.009522;
RA Jackson B.M., Abete-Luzi P., Krause M.W., Eisenmann D.M.;
RT "Use of an activated beta-catenin to identify Wnt pathway target genes in
RT caenorhabditis elegans, including a subset of collagen genes expressed in
RT late larval development.";
RL G3 (Bethesda) 4:733-747(2014).
RN [3] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=29604168; DOI=10.1002/dvg.23106;
RA Abete-Luzi P., Eisenmann D.M.;
RT "Regulation of C. elegans L4 cuticle collagen genes by the heterochronic
RT protein LIN-29.";
RL Genesis 56:0-0(2018).
CC -!- FUNCTION: Probable cuticular collagen-like protein (Probable). Nematode
CC cuticles are composed largely of collagen-like proteins (Probable). The
CC cuticle functions both as an exoskeleton and as a barrier to protect
CC the worm from its environment (Probable). Acts downstream of the Wnt
CC signaling pathway, perhaps in the formation of the adult cuticle
CC (PubMed:24569038). {ECO:0000269|PubMed:24569038,
CC ECO:0000305|PubMed:29604168}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000305|PubMed:29604168}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24569038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the hypodermal cells of the tail and
CC head, the seam cells, and in the hyp7 syncytial hypodermis in the
CC mid- to late-larval L4 stage, and young adult (PubMed:24569038,
CC PubMed:29604168). Not expressed in the cells of the developing vulva
CC (PubMed:24569038). {ECO:0000269|PubMed:24569038,
CC ECO:0000269|PubMed:29604168}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hypodermal or
CC cuticular rupture, typically in the anterior body region
CC (PubMed:24569038). Abnormal gap between the outer layer of hypodermis
CC and muscle and the internal organs, perhaps due to defects in cuticle
CC integrity (PubMed:24569038). {ECO:0000269|PubMed:24569038}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90250.1; -; Genomic_DNA.
DR PIR; T22637; T22637.
DR RefSeq; NP_495810.1; NM_063409.4.
DR AlphaFoldDB; Q20754; -.
DR SMR; Q20754; -.
DR STRING; 6239.F54C9.4; -.
DR EPD; Q20754; -.
DR PaxDb; Q20754; -.
DR PeptideAtlas; Q20754; -.
DR EnsemblMetazoa; F54C9.4.1; F54C9.4.1; WBGene00000615.
DR GeneID; 174370; -.
DR KEGG; cel:CELE_F54C9.4; -.
DR UCSC; F54C9.4; c. elegans.
DR CTD; 174370; -.
DR WormBase; F54C9.4; CE20864; WBGene00000615; col-38.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196078; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; Q20754; -.
DR OMA; CPARAKK; -.
DR OrthoDB; 1585475at2759; -.
DR PhylomeDB; Q20754; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000615; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
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; 3.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Nucleus; Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..287
FT /note="Cuticle collagen 38"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455698"
FT DOMAIN 145..200
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 215..273
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT REGION 95..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 28423 MW; 849CB997CF8B7227 CRC64;
MSKYLVPVCA SISLVAVFGA LVAMHSIVVD IDTMREEIVT GVHDMKVMSD DAWNRMIGFT
KPSLDSESRS AAFASVFRNK RSAYPSQCNC DANSQGCPPG PPGPPGLPGG RGDQGPSGDK
GRDGASGVSL AVTHHLPGGC IQCPQGPPGE TGPDGDIGEP GFPGASGSAG QCGEDGAPGE
AGITGEQGPQ GEPGTEGSEG PTGQDGTIGG PGLPGQPGTP GWPGSQGEPG KNGDSGVDGE
QGPQGPQGPD GQPGRDADNG QPGLPGKDGS IGPDANYCPC PARAKKH
