ID   A0A0B2VC87_TOXCA        Unreviewed;       297 AA.
AC   A0A0B2VC87;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Collagen alpha-5(VI) chain {ECO:0000313|EMBL:KHN79057.1};
GN   Name=COL6A5 {ECO:0000313|EMBL:KHN79057.1};
GN   ORFNames=Tcan_11129 {ECO:0000313|EMBL:KHN79057.1};
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:KHN79057.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN79057.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN79057.1};
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:KHN79057.1}.
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; JPKZ01001948; KHN79057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VC87; -.
DR   STRING; 6265.A0A0B2VC87; -.
DR   OMA; ERICECR; -.
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: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   Collagen {ECO:0000313|EMBL:KHN79057.1};
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   REGION          105..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..235
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  30110 MW;  CFE0279DBBEF0DF2 CRC64;
     MELSELSESR ESAYRVAIIV ALSVSFVPFV CLILLLPTIN QYVVNENRQI DDDITFCESE
     GTLLNEDRRE GTLGPPLESG VPATIDSPSA NNAFCSCKAA PGAKGLPGRK GMRGPRGAPG
     APGMPARIPC DPPVDLKKMC PDPCPPGEQG LQGPQGSPGE KGPPGVMGAH GKNGEDGRTG
     PPGPRGPPGI PGLDGDVGEP GIDAVPTPFI PGPPGPVGDM GPVGPPGPKG MPGIDGPPGP
     AGKRGPTGRN GLPGERGAPG LPGPIGDSGP DGEKGVRFSF VFFSFSSHLM FVLNCSV
//