SEC13_PHANO
ID SEC13_PHANO Reviewed; 302 AA.
AC Q0UNA9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; ORFNames=SNOG_06755;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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; CH445334; EAT85406.1; -; Genomic_DNA.
DR RefSeq; XP_001797118.1; XM_001797066.1.
DR AlphaFoldDB; Q0UNA9; -.
DR SMR; Q0UNA9; -.
DR STRING; 13684.SNOT_06755; -.
DR EnsemblFungi; SNOT_06755; SNOT_06755; SNOG_06755.
DR GeneID; 5974008; -.
DR KEGG; pno:SNOG_06755; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q0UNA9; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
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:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
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:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
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; 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..302
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000295420"
FT REPEAT 14..53
FT /note="WD 1"
FT REPEAT 58..99
FT /note="WD 2"
FT REPEAT 104..145
FT /note="WD 3"
FT REPEAT 149..204
FT /note="WD 4"
FT REPEAT 211..253
FT /note="WD 5"
FT REPEAT 257..296
FT /note="WD 6"
SQ SEQUENCE 302 AA; 33034 MW; D7772316422EA472 CRC64;
MADNGQNVDL LSIEANEVQH DAVLDYYGRR LATCSSDKTI KIFEVEGDKH TLVETLRGHE
GPVWCVAWAH PKYGNILASS SYDGKVIIWR EQSSTWQKIY EVALHTASVN IVAWAPHEVG
CLLACASSDG NVSVLEFKDN AWSHVIFQAC GSGVNSVSWA PAVAPGQVVS ASGNQAGAAR
RFVTGGSDCQ VKLWDFSAET GSWQSTQILT GHTDWVRDVA WSPTVLSKSY IASASQDKTV
RIWTSSDLRD WKSTVLNVDA VAWRVSWSLS GNVLAVSTGD NRVSLWKERL SGGWECVKTI
EE
