ID   SEC24_KLULA             Reviewed;         924 AA.
AC   Q6CLE0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24; OrderedLocusNames=KLLA0F03729g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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. Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
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. SEC24 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382126; CAG97957.1; -; Genomic_DNA.
DR   RefSeq; XP_455249.1; XM_455249.1.
DR   AlphaFoldDB; Q6CLE0; -.
DR   SMR; Q6CLE0; -.
DR   STRING; 28985.XP_455249.1; -.
DR   EnsemblFungi; CAG97957; CAG97957; KLLA0_F03729g.
DR   GeneID; 2895337; -.
DR   KEGG; kla:KLLA0_F03729g; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   InParanoid; Q6CLE0; -.
DR   OMA; TFPRDQS; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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..924
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295489"
FT   REGION          244..269
FT                   /note="Zinc finger-like"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   924 AA;  102725 MW;  224B89E0BFF55167 CRC64;
     MSHHKKRVYP QAQYQIAEGI AQPIVGGGVP PQTVGAGQPQ FLTPAQQHLH QQIDQASNGI
     GNMQLHNVPV VDPTAFQQAG TPVQQPPYGG APQYGQPMNS GYGADNISGV QQQYQQPMQQ
     PYGQTYGQQQ QQPQYQQPGV GMAVGKPMNQ LYPVDLFQEL PPPITDLSLP PPPLMLPPEK
     MIVPNDTVNN CSDHLRCTLN AVPKNNSLLK KSKLPLAMVI RPYTKLTDSE CPVPTSEDGV
     VVRCRRCRAY LNPFVQVIEN GLRWRCNFCN LANNFPQAID MNGNRYERPE FNHSVVDFVA
     PKEYAVRPPP PSTYAFILDV SQASIKNGLL ATAARTLLES LDTIPNHDER TRISIICVDQ
     SLHYFRIPLD EEGDNIKMYD VADLDEPFLP SPTGLLVPLI EARSNIEKLL TSLPEIFQQN
     IQPRFALASA LKSALNLIRA QGGKIIVVGA TLANVGEGTL HKRNEKAVAN TSKEASTLLN
     TGDAFYKSFP IECNKYQVTV DMFMASDDYV DIASISNLGR FTGGQTHFYP GFSALNLIDV
     TKFSKEFSKH VSMDLSLEAV MRARGSSGLK MTGFYGHFFN RSSDLCALAT VPRDQSYVFE
     IGIDEQLTKD FVYIQIALLL TSNAAQRRIR VITIGIPTTD KLTEVYASAD QLAITAYFAQ
     KAVERAPSSG FEDTREFFNK SVQEVLATYK KEVLTSNTGG GAPLMLCSNL RMWPLLMHSL
     TKHMAFRSGI VPADHRAQAL NNLETLPLPY LIQNIYPTVY SLHDMPDEAG LPDEETGEIV
     LPQPINSTSS LLERYGLYLI DTGLDMFLWI GGDAVPELVT DVFGTPDIME IPIGKNELPL
     LDATEFNLRV RNVITKIREH DDVIFYKTLH IVRGASPSEP MNHPSAREVA SLRLWTASQL
     VEDKVQNSWN YREFLQNMKT RISK