SEC13_MAGO7
ID SEC13_MAGO7 Reviewed; 289 AA.
AC A4REK3; G4NB29;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; ORFNames=MGG_14666;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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; CM001235; EHA48791.1; -; Genomic_DNA.
DR RefSeq; XP_003718375.1; XM_003718327.1.
DR AlphaFoldDB; A4REK3; -.
DR SMR; A4REK3; -.
DR STRING; 318829.MGG_14666T0; -.
DR PRIDE; A4REK3; -.
DR EnsemblFungi; MGG_14666T0; MGG_14666T0; MGG_14666.
DR GeneID; 5050789; -.
DR KEGG; mgr:MGG_14666; -.
DR VEuPathDB; FungiDB:MGG_14666; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; A4REK3; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
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; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
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..289
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000295418"
FT REPEAT 1..36
FT /note="WD 1"
FT REPEAT 41..82
FT /note="WD 2"
FT REPEAT 87..128
FT /note="WD 3"
FT REPEAT 132..186
FT /note="WD 4"
FT REPEAT 195..237
FT /note="WD 5"
FT REPEAT 244..283
FT /note="WD 6"
SQ SEQUENCE 289 AA; 31915 MW; 06ECEB0BE53232FA CRC64;
MIHDAVLDYY GRRLATCSSD RTIKIFEVEG ETHRLTETLK GHEGAVWCVA WAHPKYGNIL
ASSGYDGKVF IWREQGGAWQ KIFDFALHKA SVNIVSWSPH ESGCLLACAS SDGHVSVLEF
KDNSFDHQTF LAHGQGVNSV SWAPSTAPGS IISTNATPAA QRRFVTGGSD NTLKIWSWDA
ASAQYRCEEG GVLSGHTDWV LDVDWSPTVL QKSYIASASQ DRTVRIWTSD SSNPGVWQSR
VLKEFDTTVW RVSWSLSGNV LAVSSGDNKV TLWKENLKGE WACVNSLED
