ID   SEC23_YARLI             Reviewed;         758 AA.
AC   Q6C5L5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein transport protein SEC23;
GN   Name=SEC23; OrderedLocusNames=YALI0E16995g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79640.2; -; Genomic_DNA.
DR   RefSeq; XP_504047.2; XM_504047.2.
DR   AlphaFoldDB; Q6C5L5; -.
DR   SMR; Q6C5L5; -.
DR   STRING; 4952.CAG79640; -.
DR   EnsemblFungi; CAG79640; CAG79640; YALI0_E16995g.
DR   GeneID; 2911646; -.
DR   KEGG; yli:YALI0E16995g; -.
DR   VEuPathDB; FungiDB:YALI0_E16995g; -.
DR   HOGENOM; CLU_008658_3_0_1; -.
DR   InParanoid; Q6C5L5; -.
DR   OMA; FPPHYAE; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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..758
FT                   /note="Protein transport protein SEC23"
FT                   /id="PRO_0000295474"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   758 AA;  84305 MW;  9170FD996AAF92A1 CRC64;
     MDFEEFEEKD GVRFSWNCIP STRIEASRTV VPISALYTPL KEKPNLPVLQ YEPIACRPPC
     RAVLNSFCQV DLRARAWVCP FCLSRNQLPP QYRDITPENL PHELRPECTT VEYVLSRPAP
     NPIFLFVVDT CLDAENLTAL KDHLVATLSL IPENALVGLI TFGAMAQVHE IGYRECGKSF
     VFRGNRDYTA KQVQEQLGLN QPIGHRVPQQ GGHPQAQGAA ARFLLPLQNA EFALTNVLEG
     LQKDPWPVAA DRRPIRCTGV ALGIALGLLE TSFPNCGARV MLFAGGAPTE GPGMIVGPEL
     KEPIRSHHEI EKDTAKHSKA ATKFYEGLAK RATTHGQAVD IFAGCYDQIG MHEMRSLPNS
     TGGALVLCDA FSTSIFKSSL TKMFARDANN FLQMGFNATF DVVPSKELKV SGLIGHAVSM
     NKKNPSVADT EIGIGQTSSW KMCSITPAHT YATFFEVAQQ QGTPAGQIPP GYVQFLTHYH
     HSSTQQRLRV TTVAKALVPG GDPHIASSFD QEAAAVLMTR IAIFKSETED GNDIMRWTDK
     MLIRLCQKFA DYRKDDASSF RLAHNFSLYP QFMFHLRRSQ FLQVFNNSPD ETAFYRHCLN
     RENLNNSLIM IQPTLLSYSL EQEQPVPVLL DSVSIKPDHI LLLDTFFHIL IFHGETIANW
     RNQGYQEKEE YANFAELLQA PRMEVQDLLV DRFPLPRFID TDAGGSQARF LLSKLNPSNT
     HQSDSGYGTP GSAVVLTDDV SLQTFMSHLQ KLSVAASS