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TVP38_ASPNC
ID   TVP38_ASPNC             Reviewed;         415 AA.
AC   A2Q9P2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Golgi apparatus membrane protein tvp38;
GN   Name=tvp38; ORFNames=An01g08590;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Golgi membrane protein involved in vesicular trafficking and
CC       spindle migration.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC       protein.
CC   -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As
CC       there is no evidence that this domain associates with SNARE proteins,
CC       it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
CC       {ECO:0000250|UniProtKB:P36164}.
CC   -!- SIMILARITY: Belongs to the TVP38/TMEM64 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK43948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM269976; CAK43948.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001389281.2; XM_001389244.2.
DR   AlphaFoldDB; A2Q9P2; -.
DR   PaxDb; A2Q9P2; -.
DR   EnsemblFungi; CAK43948; CAK43948; An01g08590.
DR   GeneID; 4977165; -.
DR   KEGG; ang:ANI_1_1152014; -.
DR   VEuPathDB; FungiDB:An01g08590; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR032816; SNARE_assoc.
DR   Pfam; PF09335; SNARE_assoc; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..415
FT                   /note="Golgi apparatus membrane protein tvp38"
FT                   /id="PRO_5000219406"
FT   TOPO_DOM        1..81
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..157
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..273
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..258
FT                   /note="VTT domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36164"
FT   REGION          365..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   415 AA;  46250 MW;  FE8CA93BBB60F105 CRC64;
     MPADYSSTAR ALSVSTSSPE PLSPSEDEAY PPWSRRAPGR RNSASISGGR SATLRDQIID
     RATKTYHQIL ESWRKMNFWQ RVGAVAAFLL ANLLGIGFLV FTGKVFIWLQ PVAAQWEHSP
     LAYGVLWLCV FFVSFPPLVG WSTFGTMAGY IFGIWKGWLL YASATVLGST CSFIVSRTIL
     SKFVHRLMER DKRFAALSLT LKYDGLKLLC MIRLCPLPYS VCNGAVSTFP TVQPLMYGLA
     TALISPKLLV PAFIGNRLRV LSENNEEMSA GSKAVNICSI IVSICIGIFT GLYIYRRTLA
     RAKELEAKER EDIRRSLQAD HAAHRPHDAF SEDPEVNSAA ALLARDEEER IGFGDLDDDH
     VDLAIDDESG SETSPHRTQA SPYRDEFTDN DSDVFKDGDG THEEMYTLHT HVRRP
 
 
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