SEC13_PICGU
ID SEC13_PICGU Reviewed; 290 AA.
AC A5DHD9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; ORFNames=PGUG_02690;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408157; EDK38592.2; -; Genomic_DNA.
DR RefSeq; XP_001484961.1; XM_001484911.1.
DR AlphaFoldDB; A5DHD9; -.
DR SMR; A5DHD9; -.
DR STRING; 4929.XP_001484961.1; -.
DR EnsemblFungi; EDK38592; EDK38592; PGUG_02690.
DR GeneID; 5127033; -.
DR KEGG; pgu:PGUG_02690; -.
DR VEuPathDB; FungiDB:PGUG_02690; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; A5DHD9; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; 3.
DR SMART; SM00320; WD40; 6.
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..290
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000295421"
FT REPEAT 7..46
FT /note="WD 1"
FT REPEAT 52..93
FT /note="WD 2"
FT REPEAT 99..140
FT /note="WD 3"
FT REPEAT 145..189
FT /note="WD 4"
FT REPEAT 196..238
FT /note="WD 5"
FT REPEAT 245..284
FT /note="WD 6"
SQ SEQUENCE 290 AA; 32238 MW; 222E22E98706F1EB CRC64;
MVTIANAHDE LIHDAVLDYY GKRLATCSSD KTIKIFEVEG TENYQLTETL VGHEGPVWQV
AWAHPKFGSI LASCSYDGKV LVWKESPDRS WSIISEHKVH QASVNSVSWA PHELGAVLLC
TSSDGRVSVV DFNDDGTSTH IIFEAHKIGV NSASWAPVDT KSPVRRFVTG GSDNLAKVWS
LDASKSTYVE EAKLEGHTDW VRDVCWSPSA LVRSYIATAS QDRTVLIWHQ DGEGKWQKQK
LTEELFPDVC WRCSWSFSGN ILAVSGGDNK VSLWKENLQG KWESAGEVDQ
