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SEC24_ASPCL
ID   SEC24_ASPCL             Reviewed;         919 AA.
AC   A1CUC3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein transport protein sec24;
GN   Name=sec24; ORFNames=ACLA_086070;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06910.1; -; Genomic_DNA.
DR   RefSeq; XP_001268336.1; XM_001268335.1.
DR   AlphaFoldDB; A1CUC3; -.
DR   SMR; A1CUC3; -.
DR   STRING; 5057.CADACLAP00007832; -.
DR   EnsemblFungi; EAW06910; EAW06910; ACLA_086070.
DR   GeneID; 4700388; -.
DR   KEGG; act:ACLA_086070; -.
DR   VEuPathDB; FungiDB:ACLA_086070; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   OMA; TFPRDQS; -.
DR   OrthoDB; 330236at2759; -.
DR   Proteomes; UP000006701; 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_0000295476"
FT   REGION          1..45
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;  100415 MW;  C79B3F95A5D4F87A CRC64;
     MAAPQGGYPP QEGYGQPGDY GSPTQQQPGV VAGAAHQGHA GGKKKRAYAG EAFGFGSGAN
     AALGGQPPAG GSYGVYPPQP QAAGYQQPVY GADPHQMNAA APGYATPASP GVAQMTQQFG
     AMGMTDPHLM PPQPQQAAVT PQAPRPVPLN QLYPTDLLTQ PFNVAELDYP PPPIVLPPGT
     SVYPSPQANC PPTYVRSTLN AVPTTHSLLK KSKLPFALVI QPYAALHDAE DPIQVIPDQV
     ISRCRRCRSY INPFVTFMDH GHRWRCNMCN LTNDVPQAFD WDSALQKPAD RSLRPDLNHA
     VVEFVAPQEY MVRPPQPLVY LFLIDVSYAS VTNGLLATSA RCIKESLDRI PNADRRTRLG
     FIAVDSSLHY FSIPRDGSEN SDPRMLVVSD LEEPFLPIPG DLLVTLSECR ENIETFLDKL
     QEMFQNTQNN GCAMGSALRA GYKLISPVGG KMTVLSSSLP NIGHGALTMR EDKKVLGTSK
     ESSLLQTANS FYKSFAVECS KAQVSVDMFL FSSQYQDVAS LSNLPRYTGG QTYFYPGWNA
     ARPEDAIKFA REFSEYLSSE IGLEAVLRVR ATTGLRMNTF YGNFFNRSSD LCAFPAFPRD
     QAYVVEVAID ETVTKPVVCL QTAVLHTTCN GERRIRVLTL ALPTTQNLAD VYASADQQAI
     ATYFSHKAVE RALSSGLEPA REALQAKAVE LLSTYRKELA GGSVSGGGLQ FPANLRGLPV
     LFLALIKNLG LRKSAQIPTD MRSAALCLLS TLPLPLLMQY IYPKMYSLHD MPDNAGLPDE
     QTGEIVLPPP VNLSSERIVP YGLYLIDDGQ TQFLWVGRDA VPQLLLDVFG LADRTQLRVG
     KQNLPELDND FNQRVRAVIE KSRDHRSKGV GSIVVPHLYV VKEDGEPGLR LWAQTMLVED
     RADQSVSLVQ WMGSLREKV
 
 
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