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SEC13_CRYNB
ID   SEC13_CRYNB             Reviewed;         339 AA.
AC   P0CS51; Q55MW6; Q5KB95;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Protein transport protein SEC13;
GN   Name=SEC13; OrderedLocusNames=CNBH3180;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000042; EAL19219.1; -; Genomic_DNA.
DR   RefSeq; XP_773866.1; XM_768773.1.
DR   AlphaFoldDB; P0CS51; -.
DR   SMR; P0CS51; -.
DR   EnsemblFungi; EAL19219; EAL19219; CNBH3180.
DR   GeneID; 4937842; -.
DR   KEGG; cnb:CNBH3180; -.
DR   VEuPathDB; FungiDB:CNBH3180; -.
DR   HOGENOM; CLU_032441_0_0_1; -.
DR   Proteomes; UP000001435; Chromosome 8.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 4.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
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; Repeat;
KW   Translocation; Transport; WD repeat.
FT   CHAIN           1..339
FT                   /note="Protein transport protein SEC13"
FT                   /id="PRO_0000410338"
FT   REPEAT          21..60
FT                   /note="WD 1"
FT   REPEAT          66..107
FT                   /note="WD 2"
FT   REPEAT          124..165
FT                   /note="WD 3"
FT   REPEAT          170..229
FT                   /note="WD 4"
FT   REPEAT          236..279
FT                   /note="WD 5"
FT   REPEAT          294..333
FT                   /note="WD 6"
SQ   SEQUENCE   339 AA;  36823 MW;  2E588D8903B1B093 CRC64;
     MCLWPLIQSA QASKPVPVET QHEDMIHDAQ LDYYGKRLAT CSSDRTIRIF NVIKGEAKGE
     PVILKGHTAA VWQVSWAHPS FGSILASCSY DGRVFIWKEV GQGQGKGSGG ELQDGWERIK
     EHTLHTASVN SIAWAPYDLG PILACASSDG KVSVLSFQND GSIEVNIFPA HGTGANAISW
     APSVLSTVSG VSRSQQPSNS LAPQKRFVTA GSDNLIRIWG FDEEQKKWTE EETIKGHEDW
     VRDVAWAPNI GLPGMYIASA SQDRTVLIHS RPSPSSSWTS APLLPSLPQS QDPHFPDAVW
     RVSWSLAGNV LAVSCGDGKV SLWKEGVGKG WECVSDFSS
 
 
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