ID   SEC24_LODEL             Reviewed;         964 AA.
AC   A5DSK2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24; ORFNames=LELG_00338;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981524; EDK42160.1; -; Genomic_DNA.
DR   RefSeq; XP_001527818.1; XM_001527768.1.
DR   AlphaFoldDB; A5DSK2; -.
DR   SMR; A5DSK2; -.
DR   STRING; 379508.A5DSK2; -.
DR   EnsemblFungi; EDK42160; EDK42160; LELG_00338.
DR   GeneID; 5235992; -.
DR   KEGG; lel:LELG_00338; -.
DR   VEuPathDB; FungiDB:LELG_00338; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   InParanoid; A5DSK2; -.
DR   OMA; TFPRDQS; -.
DR   OrthoDB; 330236at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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   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; 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..964
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295490"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..287
FT                   /note="Zinc finger-like"
FT   REGION          792..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   964 AA;  105640 MW;  DE816AA6A97542EF CRC64;
     MSGRRRAYPQ PQYSAAAPSG ISSPPVSQFQ QQQQQPGQPG QPQAGFQGAY GAAAGVPAYG
     ADQLLGQFQQ MSVGNGAAVG TPQQQFQQPQ YPQAQYQQTQ QQQQQAPQVN PQLSYDPYQP
     QPQAGIYGQG MGGIPPAAGV GAGAQPVASY GAYGQASNLA GGVQLNALYT TDLSRDLPPP
     IAELSYQPPP ITLADTATII PGSKTANASS DYFRSTLNVV PNNSSLLKKS KLPLALVVKP
     YNALKIPDEN VPVTCDTVIS RCRRCRGYIN PFITLAENGR RWRCNFCNLL NDIPSAFEYD
     EISGQVKNKF DRVELNHSVV EFIAPKEYMA RAPQPIVYVF IIDVSVHAVS SGLTGTITRT
     ILESLDRIPN ENKTARVAFI GVDTNLHYFR FNEGLDGTEI MVVADIDEPF LPSPGGLLVN
     LDENREAIEK LLYDFPSFFE STANQGFALG PALKAGHKLI SNVGGKLVCF AATLPNIGEG
     KLSVRDEASV AGKPKEAKAL LTPADSFYKS FAVNCNSSQV TVDLFLTSAA YQDVATLANL
     PRFTAGQTHF YPAWTSNKYE DVAKLSKEVS DHLSQDIALE AVLRVRGSTG FRMSSFYGNF
     FNRSSDLCSF PTFPRDQSYL IEMSIEETIN KPVVYFQAAV LHSTSFGERR IRVMNLALPT
     SSKLVDVYAS ADQLAITNYF THKAIEKALS SSLPEAREYL ISRVVDILNI YRKELVAGNV
     SGASPLQIST NLRMLPLLLF CLTKNLAFRS DRVPSDHRAA ALNNLGSLPI PQLIKSIYPT
     VYSLHNMPDS CGLPGVKEES EEDGNDDNDE QGVEVDVVLP EPINDSKSSW ENYGLYLIDN
     GSELFLWVSG NVVPGLIQDV FGTENLYEIP TGKTELPEYS IEESEFNYRV RQIIGKVREQ
     PDSIIWKNLY VVVGASSNEP IEISQQRDLM ALRMWASSCL VEDKTGSEPS YRDFLTSLKS
     KVSQ