SEC13_CANAL
ID SEC13_CANAL Reviewed; 298 AA.
AC Q5AEF2; A0A1D8PJN9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; OrderedLocusNames=CAALFM_C303170WA;
GN ORFNames=CaO19.316, CaO19.7948;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ANTIGENICITY.
RX PubMed=15378749; DOI=10.1002/pmic.200400929;
RA Fernandez-Arenas E., Molero G., Nombela C., Diez-Orejas R., Gil C.;
RT "Low virulent strains of Candida albicans: unravelling the antigens for a
RT future vaccine.";
RL Proteomics 4:3007-3020(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 {ECO:0000250}.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28348.1; -; Genomic_DNA.
DR RefSeq; XP_720011.2; XM_714918.2.
DR AlphaFoldDB; Q5AEF2; -.
DR SMR; Q5AEF2; -.
DR STRING; 237561.Q5AEF2; -.
DR PRIDE; Q5AEF2; -.
DR GeneID; 3638425; -.
DR KEGG; cal:CAALFM_C303170WA; -.
DR CGD; CAL0000177077; SEC13.
DR VEuPathDB; FungiDB:C3_03170W_A; -.
DR eggNOG; KOG1332; Eukaryota.
DR HOGENOM; CLU_032441_0_0_1; -.
DR InParanoid; Q5AEF2; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR PRO; PR:Q5AEF2; -.
DR Proteomes; UP000000559; Chromosome 3.
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; 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; 4.
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 1: Evidence at protein level;
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..298
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000295408"
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 298 AA; 33014 MW; A9A35F46C2A09AA2 CRC64;
MVTIGNAHDD LIHDAVLDYY GKRLATCSSD KTIKIFDLDG TDNYKLITTL TGHEGPVWQV
SWAHPKFGSI LASCSYDGKA LIWKEQPETQ QWSIIAEHTV HQASVNSVSW APHELGAVLL
CTSSDGKVSV VDFNDDGTTS HVIFDAHAIG ANSATWAPVS TSSKDSAALK QQRRIVSCGS
DNLAKIWKYD AANNTYVEEA KLEGHTDWVR DVAWSPSNLI RSYIATASQD RTVLIWTQDR
DGKWQKQLLT EEKFPDVCWR CSWSLSGNIL AVSGGDNKVS LWKENLQGKW ESAGEVDQ
