SEC13_DEBHA
ID SEC13_DEBHA Reviewed; 297 AA.
AC Q6BIR1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; OrderedLocusNames=DEHA2G08338g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382139; CAG90373.1; -; Genomic_DNA.
DR RefSeq; XP_461910.1; XM_461910.1.
DR AlphaFoldDB; Q6BIR1; -.
DR SMR; Q6BIR1; -.
DR STRING; 4959.XP_461910.1; -.
DR EnsemblFungi; CAG90373; CAG90373; DEHA2G08338g.
DR GeneID; 2904793; -.
DR KEGG; dha:DEHA2G08338g; -.
DR VEuPathDB; FungiDB:DEHA2G08338g; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q6BIR1; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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; 2.
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..297
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000295414"
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..197
FT /note="WD 4"
FT REPEAT 204..246
FT /note="WD 5"
FT REPEAT 253..292
FT /note="WD 6"
SQ SEQUENCE 297 AA; 33046 MW; F0D7E045EE456649 CRC64;
MVTIGNAHDD LIHDAVLDYY GKRLATCSSD KTIKLFEVEG TENYKLVETL IGHEGPVWQV
AWAHPKFGSI LASCSYDGKA LIWKEQPETQ QWSIIAEHTV HQASVNSVSW APHELGAILL
CTSSDGKVSV VDFNDDGTTS HIIFDAHAIG VNSASWAPLS NNNTKGKDTN SIRRFVTCGS
DNLAKIWKFD SSKNAYIEEA VLEGHTDWVR DVCWSPSILI RSYIATASQD RTVLIWSQDN
NGKWQKQLLT EEMFPDVCWR CSWSLSGNIL AVSGGDNKVS LWKENLQGKW ESAGEVE
