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SC131_CANGA
ID   SC131_CANGA             Reviewed;         298 AA.
AC   Q6FNV4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Protein transport protein SEC13-1;
GN   Name=SEC131; OrderedLocusNames=CAGL0J08778g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380956; CAG61041.1; -; Genomic_DNA.
DR   RefSeq; XP_448090.1; XM_448090.1.
DR   AlphaFoldDB; Q6FNV4; -.
DR   SMR; Q6FNV4; -.
DR   STRING; 5478.XP_448090.1; -.
DR   EnsemblFungi; CAG61041; CAG61041; CAGL0J08778g.
DR   GeneID; 2889676; -.
DR   KEGG; cgr:CAGL0J08778g; -.
DR   CGD; CAL0133190; CAGL0J08778g.
DR   VEuPathDB; FungiDB:CAGL0J08778g; -.
DR   eggNOG; KOG1332; Eukaryota.
DR   HOGENOM; CLU_032441_0_1_1; -.
DR   InParanoid; Q6FNV4; -.
DR   OMA; TVDTGHE; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031080; C:nuclear pore outer ring; IEA:EnsemblFungi.
DR   GO; GO:0035859; C:Seh1-associated complex; 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; 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; 3.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
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..298
FT                   /note="Protein transport protein SEC13-1"
FT                   /id="PRO_0000295409"
FT   REPEAT          7..46
FT                   /note="WD 1"
FT   REPEAT          51..92
FT                   /note="WD 2"
FT   REPEAT          97..138
FT                   /note="WD 3"
FT   REPEAT          143..196
FT                   /note="WD 4"
FT   REPEAT          203..245
FT                   /note="WD 5"
FT   REPEAT          253..292
FT                   /note="WD 6"
SQ   SEQUENCE   298 AA;  32951 MW;  78F2C9A1CEA7029C CRC64;
     MVEIANAHND LIHDAVLDYY GKKLATCSSD KTIKIFEVEG ESHKLVDTLV GHEGPVWRVD
     WAHPKFGTIL ASCSYDGKVI IWKEENDRWS QIAVHAVHTA SVNSVQWAPH EYGALLLAAS
     SDGKVSVVEF KENGTATPLI FDAHAIGVNA ASWAPATVEG GNNPGEAPKE VRRFVTGGAD
     NLVKIWRYNP ETQSYLVEDT LEGHSDWVRD VAWSPSVLLR SYIASVSQDR TCNIWTQEDN
     TGPWVKTQLT PEEFPDVLWR ASWSLSGNIL AISGGDNKVT LWKENLNGKW ESAGEVNQ
 
 
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