COL1_CAEEL
ID COL1_CAEEL Reviewed; 301 AA.
AC P08124; Q19763;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cuticle collagen 1;
DE AltName: Full=Protein dumpy-15;
DE AltName: Full=Protein squat-3;
DE Flags: Precursor;
GN Name=sqt-3; Synonyms=col-1, dpy-15; ORFNames=F23H12.4;
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=7139711; DOI=10.1016/0092-8674(82)90256-2;
RA Kramer J.M., Cox G.N., Hirsh D.;
RT "Comparisons of the complete sequences of two collagen genes from
RT Caenorhabditis elegans.";
RL Cell 30:599-606(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=2578467; DOI=10.1016/s0021-9258(18)89683-1;
RA Kramer J.M., Cox G.N., Hirsh D.;
RT "Expression of the Caenorhabditis elegans collagen genes col-1 and col-2 is
RT developmentally regulated.";
RL J. Biol. Chem. 260:1945-1951(1985).
RN [3]
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).
RN [4]
RP MUTAGENESIS OF ALA-288; ASP-290; GLY-291; ASP-297 AND THR-299.
RX PubMed=15579684; DOI=10.1534/genetics.104.027953;
RA Novelli J., Ahmed S., Hodgkin J.;
RT "Gene interactions in Caenorhabditis elegans define DPY-31 as a candidate
RT procollagen C-proteinase and SQT-3/ROL-4 as its predicted major target.";
RL Genetics 168:1259-1273(2004).
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; V00147; CAA23463.1; -; Genomic_DNA.
DR EMBL; J01047; AAA27988.1; -; Genomic_DNA.
DR EMBL; Z74472; CAA98942.1; -; Genomic_DNA.
DR PIR; A31219; A31219.
DR PIR; T21314; T21314.
DR RefSeq; NP_001256412.1; NM_001269483.1.
DR AlphaFoldDB; P08124; -.
DR BioGRID; 44716; 2.
DR STRING; 6239.F23H12.4a; -.
DR EPD; P08124; -.
DR PaxDb; P08124; -.
DR PeptideAtlas; P08124; -.
DR EnsemblMetazoa; F23H12.4a.1; F23H12.4a.1; WBGene00005018.
DR GeneID; 179693; -.
DR KEGG; cel:CELE_F23H12.4; -.
DR UCSC; F23H12.4; c. elegans.
DR CTD; 179693; -.
DR WormBase; F23H12.4a; CE05707; WBGene00005018; sqt-3.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000195912; -.
DR InParanoid; P08124; -.
DR OMA; FMKANSG; -.
DR OrthoDB; 1475900at2759; -.
DR PhylomeDB; P08124; -.
DR PRO; PR:P08124; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00005018; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P08124; baseline and differential.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
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; IMP:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
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 1: Evidence at protein level;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..301
FT /note="Cuticle collagen 1"
FT /id="PRO_0000006420"
FT REGION 105..134
FT /note="Triple-helical region"
FT REGION 109..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..179
FT /note="Triple-helical region"
FT REGION 183..209
FT /note="Triple-helical region"
FT REGION 218..283
FT /note="Triple-helical region"
FT COMPBIAS 109..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 289..290
FT /note="Cleavage; by dpy-31"
FT /evidence="ECO:0000303|PubMed:15579684"
FT MUTAGEN 288
FT /note="A->V: In e2809, e2889 and e2896; abnormal left-
FT twisted body."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 290
FT /note="D->G: In 2901; abnormal left-handed rolling."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 291
FT /note="G->E: In e2888, e2890 and sc8; abnormal left-twisted
FT body. At the restrictive temperature of 25 degrees Celsius,
FT lethal in a dpy-31 (ju345) mutant background."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 297
FT /note="D->G: In e2911; slightly shorter and stouter."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 299
FT /note="T->A: In e2906; temperature sensitive mutant. At the
FT restrictive temperature of 15 degrees Celsius, lethal at
FT the embryonic or early larval stages. At the permissive
FT temperature of 25 degrees Celsius, slightly shorter and
FT stouter."
FT /evidence="ECO:0000269|PubMed:15579684"
FT CONFLICT 57..61
FT /note="Missing (in Ref. 1; CAA23463 and 2; AAA27988)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> A (in Ref. 1; CAA23463 and 2; AAA27988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 29177 MW; 4A75B65540E50360 CRC64;
METDGRLKAY KFVAYAAVGF SIAAVASVLL TLPMVYSYVS HVRQQMHHEI NFCKGSAKDI
FAEVNYMKAN AGPVPPRNRT TRQAYGGPEV NPAPNLQCEG CCLPGPPGPA GAPGKPGKPG
RPGAPGTPGT PGKPPVAPCE PTTPPPCKPC PQGPPGPPGP PGAPGDPGEA GTPGRPGTDA
APGSPGPRGP PGPAGEAGAP GPAGEPGTPA ISEPLTPGAP GEPGDSGPPG PPGPPGAPGN
DGPPGPPGPK GAPGPDGPPG VDGQSGPPGP PGPAGTPGEK GICPKYCALD GGVFFEDGTR
R
