ID H6WDG2_9PELO Unreviewed; 262 AA.
AC H6WDG2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Collagen {ECO:0000313|EMBL:AFA56037.1};
DE Flags: Fragment;
OS Caenorhabditis sinica.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1550068 {ECO:0000313|EMBL:AFA56037.1};
RN [1] {ECO:0000313|EMBL:AFA56037.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GXW0006 {ECO:0000313|EMBL:AFA56037.1};
RX PubMed=22320847; DOI=10.1111/j.1365-294X.2012.05475.x;
RA Cutter A.D., Wang G.X., Ai H., Peng Y.;
RT "Influence of finite-sites mutation, population subdivision and sampling
RT schemes on patterns of nucleotide polymorphism for species with molecular
RT hyperdiversity.";
RL Mol. Ecol. 21:1345-1359(2012).
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 ---------------------------------------------------------------------------
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; JQ219426; AFA56037.1; -; Genomic_DNA.
DR AlphaFoldDB; H6WDG2; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637:SF251; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|EMBL:AFA56037.1};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..54
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 94..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFA56037.1"
FT NON_TER 262
FT /evidence="ECO:0000313|EMBL:AFA56037.1"
SQ SEQUENCE 262 AA; 26086 MW; 9C28F2D2F73F71D3 CRC64;
STLGYIGAGV CLLGVFSALC SVGHIVQDIN NLRNEVESRV DEFKVLADDT WDRLLILQSP
TGESANPVPS LLRNKRFVYP GMCNCDSNSQ GCPAGAPGPP GNPGKRGDEG HPGEEGRRGA
SGISLAATHD IPGGCIKCPE GPAGPPGSDG EAGPEGFPGL QGPSGPSGED GAPGQEGAPG
DEGEQGPKGY DGTDGPDGQP GTTYFPGQPG QPGEPGWLGE TGLPGQHGEP GKDGEEGPKG
APGTPGNAGH DAFPGMPGQA GK
//