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Database: UniProt
Entry: A0A0B2VAE0_TOXCA
LinkDB: A0A0B2VAE0_TOXCA
Original site: A0A0B2VAE0_TOXCA 
ID   A0A0B2VAE0_TOXCA        Unreviewed;       472 AA.
AC   A0A0B2VAE0;
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=Cuticle collagen sqt-1 {ECO:0000313|EMBL:KHN80446.1};
GN   Name=sqt-1 {ECO:0000313|EMBL:KHN80446.1};
GN   ORFNames=Tcan_08731 {ECO:0000313|EMBL:KHN80446.1};
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:KHN80446.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN80446.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN80446.1};
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:KHN80446.1}.
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DR   EMBL; JPKZ01001742; KHN80446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VAE0; -.
DR   STRING; 6265.A0A0B2VAE0; -.
DR   OMA; FWIPRIR; -.
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   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF428; SCAVENGER RECEPTOR CLASS A MEMBER 3; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000313|EMBL:KHN80446.1};
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        38..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..90
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          213..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  49765 MW;  93802B9E84B87989 CRC64;
     MGSCRSQLFS RFTSISPLRD GRVVGVYMSS RGIPDGQLSG IVAITLSALA IVFTFISVPM
     LIAKLNEMQL KAVNDMQGFK KRSDQLWNDI QQIHNLLTPK HHAAALTADI LNSFETNQSL
     HATLIDNFNE NFWIPRIRRT KKKLISTKST RAGLQLLDGE LRPAKKKKTS GKTGDGSKFT
     DYMTGYGVPP SRSIETEYYG NLGGEIDHCE GPAGPPGEAG LDGIEGEPGR DGLPGQDGNT
     LYQNEDSCYI CPQGESGLPG MPGPPGAPGE KGEIGSPGEE GIRGKDSNTR GPPGDIGLPG
     VKGTPGIRGP SGPTVASGLG LRGPPGPPGQ PGPRGMTGFS GLNGLSEAGP DGPSGPRGTP
     GMDGVAGLEG PTGETGFPGE DAGYCSCPKR TKFVGRYMFG RDSVLQEASG ERKRIIGQMR
     RKAMAAQNAV QPLPITSGHT LKKNRKNSLV SFTMRNLGQM PIDGSPAVKK LF
//
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