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Database: UniProt
Entry: A0A0B2VIF9_TOXCA
LinkDB: A0A0B2VIF9_TOXCA
Original site: A0A0B2VIF9_TOXCA 
ID   A0A0B2VIF9_TOXCA        Unreviewed;       302 AA.
AC   A0A0B2VIF9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative cuticle collagen {ECO:0000313|EMBL:KHN81194.1};
GN   Name=col-155 {ECO:0000313|EMBL:KHN81194.1};
GN   ORFNames=Tcan_07072 {ECO:0000313|EMBL:KHN81194.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN81194.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN81194.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN81194.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN81194.1}.
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DR   EMBL; JPKZ01001576; KHN81194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VIF9; -.
DR   STRING; 6265.A0A0B2VIF9; -.
DR   OMA; HCKESAK; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
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; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF421; COLLAGEN-RELATED; 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:KHN81194.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..64
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          110..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..205
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..278
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  29432 MW;  47CA92D0638286D1 CRC64;
     MDLENRIKAY RFVAYSAVTF SVVAVLSVCV TLPMVYTYVH HVRRQMHNEI TFCKGSAKDI
     WAEVHELKNI QTARNRTTRQ AGYGEEAVSG GATSQAGACD ACCLPGPPGP AGPPGRPGMP
     GKPGAPGLPG SPGKPPSQPC EAVTPPPCKP CPAGPPGPPG PAGPPGDPGA PGEPGRAGAD
     APPGEPGPKG PPGPPGQPGA PGPAGDPGAP AISEPLTPGE PGPAGDPGPP GPPGPAGQPG
     SDGAPGPIGP KGPPGPAGQP GSDGAPGQPG PPGPPGTQGE KGICPKYCAI DGGVFFEDGT
     RR
//
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