ID   SC232_CANGA             Reviewed;         757 AA.
AC   Q6FSI6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein transport protein SEC23-2;
GN   Name=SEC232; OrderedLocusNames=CAGL0H00242g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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 (By similarity). {ECO:0000250}.
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.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC       COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR380954; CAG59739.1; -; Genomic_DNA.
DR   RefSeq; XP_446808.1; XM_446808.1.
DR   AlphaFoldDB; Q6FSI6; -.
DR   SMR; Q6FSI6; -.
DR   STRING; 5478.XP_446808.1; -.
DR   PRIDE; Q6FSI6; -.
DR   EnsemblFungi; CAG59739; CAG59739; CAGL0H00242g.
DR   GeneID; 2888615; -.
DR   KEGG; cgr:CAGL0H00242g; -.
DR   CGD; CAL0132036; CAGL0H00242g.
DR   VEuPathDB; FungiDB:CAGL0H00242g; -.
DR   eggNOG; KOG1986; Eukaryota.
DR   HOGENOM; CLU_008658_3_0_1; -.
DR   InParanoid; Q6FSI6; -.
DR   OMA; FPPHYAE; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein transport; 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:0003400; P:regulation of COPII vesicle coating; IEA:EnsemblFungi.
DR   GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR   CDD; cd11287; Sec23_C; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR037364; Sec23.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR037550; Sec23_C.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR11141; PTHR11141; 1.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF81811; SSF81811; 1.
DR   SUPFAM; SSF82754; SSF82754; 1.
DR   SUPFAM; SSF82919; SSF82919; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..757
FT                   /note="Protein transport protein SEC23-2"
FT                   /id="PRO_0000295457"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   757 AA;  84408 MW;  70B003AA224F9370 CRC64;
     MDFEANEDLN GVRFSWNVFP SSKTDANKNV VPVGCLYTPL KEIEDLQIAS YNPVVCAGPQ
     CKAILNPYCA IDPRSSSWTC PICNSRNHLP PQYANMTQEN MPIELQQTTV EYITNKPVQI
     PPIFFFVVDI TAEQENLDAL KESIITSLSL LPPNALIGFM TYGNVVQLYD LSCDIIERCS
     VFRGDREYQF DQLVEMLTGQ KPSNTMAPLA NGKITPLSLN RFFLPLEQVE FKLNQLLESM
     SPDQWSVPAG HRPLRATGSA LNIATLLLQG CYKNVASRII LFASGPGTVA PGLIVNTELK
     DPIRSHHDID SDRAPHYKKA CKFYNSIAER VAENGHTVDV FAGCYDQVGM SEMKKMTDST
     GGVLLLTDAF STAIFKQSYL RLFSKDEEGY LTMVFNGNLA VKTSKDLKLQ GLIGHASAVK
     KTDATNVSDS EIGIGSTSVW KMSALSPHHT YGIFFEIANP NAVSPITTDR ANLAYTQFIT
     QYQHASGTNR VRVTTVANQM LPFGTPAIAA SFDQEAAAVL MARIAVFKAE TDDGADVIRW
     LDRTLIKLCQ KYADYNKDDP ASFRLAPNFS LYPQFTYYLR RSQFLSVFNN SPDETAFYRH
     IFTREDTTNS LIMIQPTLTS FSMEEDPQPV LLDSISVKPN TILLLDTFFF ILIYHGEQIA
     QWRKAGYQDD PQYADFKALL EEPKVEAAEL LVDRFPLPRF IDTEAGGSQA RFLLSKLNPS
     DNYQDMARGG STIVLTDDVS LQNFMAHLQQ VTVSGQP