ID Q19079_CAEEL Unreviewed; 302 AA.
AC Q19079;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE SubName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000313|EMBL:CCD68819.1};
GN Name=dpy-3 {ECO:0000313|EMBL:CCD68819.1,
GN ECO:0000313|WormBase:EGAP7.1};
GN ORFNames=CELE_EGAP7.1 {ECO:0000313|EMBL:CCD68819.1}, EGAP7.1
GN {ECO:0000313|WormBase:EGAP7.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD68819.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD68819.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD68819.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000256|ARBA:ARBA00011518}.
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DR EMBL; BX284606; CCD68819.1; -; Genomic_DNA.
DR PIR; T15936; T15936.
DR RefSeq; NP_508395.1; NM_075994.4.
DR AlphaFoldDB; Q19079; -.
DR STRING; 6239.EGAP7.1.1; -.
DR EPD; Q19079; -.
DR PaxDb; 6239-EGAP7-1; -.
DR PeptideAtlas; Q19079; -.
DR EnsemblMetazoa; EGAP7.1.1; EGAP7.1.1; WBGene00001065.
DR GeneID; 180529; -.
DR KEGG; cel:CELE_EGAP7.1; -.
DR UCSC; EGAP7.1; c. elegans.
DR AGR; WB:WBGene00001065; -.
DR WormBase; EGAP7.1; CE07013; WBGene00001065; dpy-3.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; Q19079; -.
DR OMA; CKTRSRE; -.
DR OrthoDB; 2883858at2759; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001065; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
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 PANTHER; PTHR24637:SF382; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|EMBL:CCD68819.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..65
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 73..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 29617 MW; 3191CAB5A23BBAEE CRC64;
MEQKCAPRRS LRLLAIASAT LAIVSMLATV IIVPLVYNHV QHLQSVMNSE VDFCKTRSRD
LWREMVTVQS ATGGIPARTA RRTRRDNYGA QPIAANPPSS AAGSCCTCQV GPPGPPGPPG
RDGRPGAPGR PGNPGPPGRD GALLPGPPPK PPCQKCPPGP PGPAGPPGPK GLPGPQGDAG
TSGQDGVPGL PGPPGPSGPQ GAPGVPGEKG PTGEPGKVIN GAPPGPPGPP GPPGPQGPPG
PPGKDGQPGK AGPPGLPGDP GEKGSDGLPG PHGGTGPRGP PGQPGSCDHC PPPRTGPGYA
RR
//
