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Database: UniProt
Entry: A0A0B2V6V2_TOXCA
LinkDB: A0A0B2V6V2_TOXCA
Original site: A0A0B2V6V2_TOXCA 
ID   A0A0B2V6V2_TOXCA        Unreviewed;       405 AA.
AC   A0A0B2V6V2;
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:KHN79181.1};
GN   Name=col-155 {ECO:0000313|EMBL:KHN79181.1};
GN   ORFNames=Tcan_14071 {ECO:0000313|EMBL:KHN79181.1};
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:KHN79181.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN79181.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN79181.1};
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:KHN79181.1}.
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DR   EMBL; JPKZ01001939; KHN79181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2V6V2; -.
DR   STRING; 6265.A0A0B2V6V2; -.
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   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF421; COLLAGEN-RELATED; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000313|EMBL:KHN79181.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..39
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          104..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..153
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  41009 MW;  1DFE9A5D465DDAA9 CRC64;
     MNFDSRIKAY RLVAYSAVAF SIVAVLSVCV TLPLVYYFVH HVRKSMHNEV IFCKGSAKDI
     WSEVHQLKGA ATAWKRPARQ TGYTDGSKAG GGCESCCLPG PAGLPGPSGR PGSPGKPGAP
     GLPGNPGRPP VGTCDVATPP PCKPCPPGPP GPSGQSGAAG YAAAPGKPGN PGLPGPIGAS
     GTKGPAGLVG KRGAPGAPGN AGANAQSEPL LPGPPGPVGD QGPRGTPGPA GYPGSRGAPG
     PAGPKGPDGC CGRPGNDGMP ERQDVPGTSG QGGERGICPK YCAGTAKDIW AEVHDMKNVI
     TAKNRTTRQV GRSDCSACCV SGRAGPTGRP GKPGNAGKPG APGTPGIPTR PSNRAKQMFR
     SDFAEWRPYA SLTNLTHRLL PISENIHRGV DPQTFVHFLH RSLSD
//
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