ID A0A0R3RQG4_9BILA Unreviewed; 443 AA.
AC A0A0R3RQG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:EEL_0000392101-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000392101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000392101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0R3RQG4; -.
DR STRING; 1147741.A0A0R3RQG4; -.
DR WBParaSite; EEL_0000392101-mRNA-1; EEL_0000392101-mRNA-1; EEL_0000392101.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF354; COLLAGEN; 1.
DR Pfam; PF01391; Collagen; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 46503 MW; 0278E0B6C793E284 CRC64;
MDLSAREKAY QFAIITALII AALPLVAFIA LTPTVNRYMS IVDRQLQNDF FFCEFNTIFE
HLNCSQNFES CQERWRQSSR KVRSLPIKVG EEMPTAATFL VNYSPSLEIV ESEQVAARNN
GQPSQPNEAT KAETDLKQSV INKLTEDSVA IWHNTGVITT DFSNTAGVAT EPESAHFRIH
RFLPPTKKNF QGLPVTHAPV TQTVHDSMTE ANGSDRKCRC SASPGPKGMP GRKGLKGTPG
AQGAPGFPAR MPCELPVDLK KICADPCPVG KQGKQGPTVA LRKSKNALAI QFFPMCFSAL
GLPGDKGATG IPGVHGKNGE DGKIGPPGPR GPPGIPGLDG DIGEPGIDAT PIPFIPGPPG
PAGEVGPVGP PGPRGMPGID GPPGPTGKRG PPGEDGLPGS RGSAGLPGPV GKVGPDGNVG
VCPTYCATDG GVFFVKPPEW FED
//