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SEC13_ASPNC
ID   SEC13_ASPNC             Reviewed;         308 AA.
AC   A2QHM1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein transport protein sec13;
GN   Name=sec13; ORFNames=An04g00360;
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: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules. It also functions as a component of the
CC       nuclear pore complex (NPC). NPC components, collectively referred to as
CC       nucleoporins (NUPs), can play the role of both NPC structural
CC       components and of docking or interaction partners for transiently
CC       associated nuclear transport factors. Sec13 is required for efficient
CC       mRNA export from the nucleus to the cytoplasm and for correct nuclear
CC       pore biogenesis and distribution (By similarity).
CC       {ECO:0000250|UniProtKB:Q04491}.
CC   -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC       sec23/24 complex, the sec13/31 complex, and the protein sar1. Component
CC       of the nuclear pore complex (NPC). NPC constitutes the exclusive means
CC       of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC       ions and small molecules and the active, nuclear transport receptor-
CC       mediated bidirectional transport of macromolecules such as proteins,
CC       RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC       nuclear envelope. Due to its 8-fold rotational symmetry, all subunits
CC       are present with 8 copies or multiples thereof.
CC       {ECO:0000250|UniProtKB:Q04491}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q04491}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR   EMBL; AM270062; CAK38491.1; -; Genomic_DNA.
DR   RefSeq; XP_001401399.1; XM_001401362.2.
DR   AlphaFoldDB; A2QHM1; -.
DR   SMR; A2QHM1; -.
DR   PaxDb; A2QHM1; -.
DR   EnsemblFungi; CAK38491; CAK38491; An04g00360.
DR   GeneID; 4990436; -.
DR   KEGG; ang:ANI_1_162184; -.
DR   VEuPathDB; FungiDB:An04g00360; -.
DR   HOGENOM; CLU_032441_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 6L.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061700; C:GATOR2 complex; IEA:EnsemblFungi.
DR   GO; GO:0031080; C:nuclear pore outer ring; IEA:EnsemblFungi.
DR   GO; GO:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR   GO; GO:0090114; P:COPII-coated vesicle budding; IEA:EnsemblFungi.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0051664; P:nuclear pore localization; IEA:EnsemblFungi.
DR   GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:EnsemblFungi.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR037596; Sec13.
DR   InterPro; IPR037363; Sec13/Seh1_fam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR11024; PTHR11024; 1.
DR   PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT   CHAIN           1..308
FT                   /note="Protein transport protein sec13"
FT                   /id="PRO_0000295405"
FT   REPEAT          10..49
FT                   /note="WD 1"
FT   REPEAT          54..95
FT                   /note="WD 2"
FT   REPEAT          109..150
FT                   /note="WD 3"
FT   REPEAT          154..208
FT                   /note="WD 4"
FT   REPEAT          215..257
FT                   /note="WD 5"
FT   REPEAT          263..302
FT                   /note="WD 6"
SQ   SEQUENCE   308 AA;  33985 MW;  F5D6F645EB438EFD CRC64;
     MAAQVISNSG HDEMIHDAGL DYYGRRLATC SSDKTIKIFE IEGETHRLIE TLKGHEGAVW
     CVAWAHPKFG TILASSSYDG KVLIWREQHQ NATSPVAGGA WTKVFDFSLH TASVNMVSWA
     PHESGCLLAC ASSDGHVSVL EFRDNSWTHQ IFHAHGMGVN SISWAPAAAP GSLISSNPGP
     GQQRRFVTGG SDNLLKIWDY NPETKTYNNT QTLEGHSDWV RDVAWSPSVL SKSYIASASQ
     DKTVRIWTSD ASNPGQWTSQ QLEFDTVLWR VSWSPSGNIL AVSGGDNKVS LWKENLKGQW
     EKVKDIEE
 
 
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