ID Q19079_CAEEL Unreviewed; 302 AA. AC Q19079; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 13-SEP-2023, entry version 148. 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}. CC -!- SIMILARITY: Belongs to the cuticular collagen family. CC {ECO:0000256|ARBA:ARBA00010667}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284606; CCD68819.1; -; Genomic_DNA. DR PIR; T15936; T15936. DR AlphaFoldDB; Q19079; -. DR STRING; 6239.EGAP7.1; -. DR EPD; Q19079; -. DR PaxDb; Q19079; -. DR PeptideAtlas; Q19079; -. DR EnsemblMetazoa; EGAP7.1.1; EGAP7.1.1; WBGene00001065. DR KEGG; cel:CELE_EGAP7.1; -. DR UCSC; EGAP7.1; c. elegans. DR AGR; WB:WBGene00001065; -. DR CTD; 180529; -. 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 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 InterPro; IPR008160; Collagen. DR PANTHER; PTHR24637; COLLAGEN; 1. DR PANTHER; PTHR24637:SF382; COLLAGEN-RELATED; 1. DR Pfam; PF01484; Col_cuticle_N; 1. DR Pfam; PF01391; Collagen; 1. DR SMART; SM01088; Col_cuticle_N; 1. PE 3: Inferred from homology; 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 //