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Database: UniProt
Entry: A0A0K0G1G9_STRVS
LinkDB: A0A0K0G1G9_STRVS
Original site: A0A0K0G1G9_STRVS 
ID   A0A0K0G1G9_STRVS        Unreviewed;       341 AA.
AC   A0A0K0G1G9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:SVE_1856000.1};
OS   Strongyloides venezuelensis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1856000.1};
RN   [1] {ECO:0000313|Proteomes:UP000035680}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A, De Silva N.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SVE_1856000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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; A0A0K0G1G9; -.
DR   STRING; 75913.A0A0K0G1G9; -.
DR   WBParaSite; SVE_1856000.1; SVE_1856000.1; SVE_1856000.
DR   Proteomes; UP000035680; Unassembled WGS sequence.
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; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF315; CUTICLE COLLAGEN 40; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..67
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          105..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..314
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  31558 MW;  07D34DAEF4BD110A CRC64;
     MADKIQIAEA ASMKRLAFFG IAISTIATMT AVIAIPMVYT YLQHIESSIK VEVDFCSHRS
     QGLMEELQRL EAQVGVSRRN KRYSEQHQRL GRRNQILRGA ATYDGGSGGS SYSSGPAVSA
     ASSGGAGGAG GAGGAGGAGG AGGAGGCCGG CSYGPPGPPG KDGADGKDGT DGQAGKPGDD
     GSDAAAPESA AAEPCQTCPA GPPGPAGNPG PKGPNGNPGA AGAPGNNGAP GEAGAPGPAG
     PAGSDGAPGN PGAPGPAGTV NEVPGAAGPP GPPGPPGPPG ADGEPGAPGA GSDGPPGPAG
     DPGPSGPPGN PGAPGSAGEP GAAGEGGSCG HCPPPRTAPG Y
//
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