ID   SEC24_NEOFI             Reviewed;         919 AA.
AC   A1DP06;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=sec24; ORFNames=NFIA_058780;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16527.1; -; Genomic_DNA.
DR   RefSeq; XP_001258424.1; XM_001258423.1.
DR   AlphaFoldDB; A1DP06; -.
DR   SMR; A1DP06; -.
DR   STRING; 36630.CADNFIAP00004901; -.
DR   EnsemblFungi; EAW16527; EAW16527; NFIA_058780.
DR   GeneID; 4584940; -.
DR   KEGG; nfi:NFIA_058780; -.
DR   VEuPathDB; FungiDB:NFIA_058780; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   OMA; TFPRDQS; -.
DR   OrthoDB; 330236at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; 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: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..919
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295492"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   919 AA;  100197 MW;  670ED80A9FB4F06B CRC64;
     MASPQGGYPP QEGYGQPAGY GSPTQQHAGM AAGAPPQGHA GGKKKRAYAG EAFEIGSGAN
     AALGGQLPAG GSYGAYPPQP QAAGYQQPVY GADPSQMNAA APGYAAPATP GVAQMTQQFG
     AMGVTDPHLM PPQPPQAAVA PQAPRPVPLN QLYPTDLLTQ PFNVAELDYP PPPIVLPPGT
     SVYPSPTANC PPKYVRSTLN AVPTTHSLLK KSKLPFALVI QPYASLRDAE DPIPVIPDQV
     ISRCRRCRSY INPFVTFLDH GHRWRCNMCN LTNDVPQAFD WDAALQKPAD RSLRPDLNHA
     VVEFVAPQEY MVRPPQPLVY LFLIDVSYAS VTNGLLATSA RCIKESLDRI PNADRRTRLG
     FIAVDSSLHY FSIPRDGSEN SDPRMLVISD LDEPFLPIPG DLLVTLSECR ENIETFLDKL
     QEMFQNTQNN GCAMGSALRA GYKLIAPVGG KMTVLSSSLP NVGHGSLTMR EDKKVLGTSK
     ESSLLQTANS FYKSFAVECS KAQVSVDMFL FSSQYQDVAS LSNLPRYTGG QTYFYPGWNA
     ARGEDAIKFA REFSDYLSSE IGLEAVLRVR ATTGLRMNTF YGNFFNRSSD LCAFPAFPRD
     QAYVVEVAID ETVTKPIVCL QTAVLHTTCN GERRIRVLTL ALPTTQNLAD VYASADQQAI
     ATYFSHKAVE RVLSSGLEPA REALQAKAVE LLSTYRKELA GGSVSGGGLQ FPANLRGLPV
     LFLAMIKNLG LRKSAQIPTD MRSAALCLLS TLPLPLLIQY IYPKMYSLHD MPDNAGLPDE
     QTGEIVLPPP INLSSERIVP YGLYLIDDGQ TQFLWVGRDA VPQLLLDVFG LPDRSQLRVG
     KQNLPELDND FNQRVRAVIE KSRDHRSKGV GSIVVPHLYV VKEDGEPGLR LWAQTMLVED
     RADQSVSLVQ WMGSLREKV