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SEC13_LODEL
ID   SEC13_LODEL             Reviewed;         304 AA.
AC   A5DXE2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein transport protein SEC13;
GN   Name=SEC13; ORFNames=LELG_02029;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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; CH981525; EDK43850.1; -; Genomic_DNA.
DR   RefSeq; XP_001527200.1; XM_001527150.1.
DR   AlphaFoldDB; A5DXE2; -.
DR   SMR; A5DXE2; -.
DR   STRING; 379508.A5DXE2; -.
DR   EnsemblFungi; EDK43850; EDK43850; LELG_02029.
DR   GeneID; 5233653; -.
DR   KEGG; lel:LELG_02029; -.
DR   VEuPathDB; FungiDB:LELG_02029; -.
DR   eggNOG; KOG1332; Eukaryota.
DR   HOGENOM; CLU_032441_0_1_1; -.
DR   InParanoid; A5DXE2; -.
DR   OMA; TVDTGHE; -.
DR   OrthoDB; 944756at2759; -.
DR   Proteomes; UP000001996; 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..304
FT                   /note="Protein transport protein SEC13"
FT                   /id="PRO_0000295417"
FT   REPEAT          7..46
FT                   /note="WD 1"
FT   REPEAT          52..93
FT                   /note="WD 2"
FT   REPEAT          100..141
FT                   /note="WD 3"
FT   REPEAT          146..201
FT                   /note="WD 4"
FT   REPEAT          208..250
FT                   /note="WD 5"
FT   REPEAT          257..296
FT                   /note="WD 6"
SQ   SEQUENCE   304 AA;  33750 MW;  F3F50C914879FB06 CRC64;
     MVTIGNAHED LIHDAVLDYY GKRLATCSSD KTIKIYDIEG TENYKLTATL TGHEGPIWQV
     AWAHPKFGSI LASCSYDGKV LIWKEQQDTQ QWSIIAEHTI HQASVNSVSW APHELGAVLL
     CTSSDGKVSV VDFNDDGTTS HVIFDAHAIG VNSASWAPFT AASSTSSKDA NTLKQHRRFV
     TCGSDNLVKI WKYDTALETY AEEAKLEGHT DWVRDVAWSP SNLVRPYIAT ASQDCTVLIW
     TQDKDGKWQS QPLTEEKFPD VCWRCSWSLS GNILAVSGGD NKVTLWKENL QGKWESAGEV
     ELIK
 
 
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