SEC24_ASPNC
ID SEC24_ASPNC Reviewed; 919 AA.
AC A2QSG6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein transport protein sec24;
GN Name=sec24; ORFNames=An08g10650;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270183; CAK45738.1; -; Genomic_DNA.
DR RefSeq; XP_001393169.1; XM_001393132.2.
DR AlphaFoldDB; A2QSG6; -.
DR SMR; A2QSG6; -.
DR PaxDb; A2QSG6; -.
DR EnsemblFungi; CAK45738; CAK45738; An08g10650.
DR GeneID; 4983379; -.
DR KEGG; ang:ANI_1_1430074; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
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_0000295478"
FT REGION 1..43
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; 100343 MW; EE044C57AA45FF4C CRC64;
MAAPQGGYPP QEGYGQPAGY GSPVQQPAGL AAGAPAQGQA GGRKKRVYAG EAFDFGSGAN
AALGGQLPAG GSYGAYPPQP QAAGYQQPMY GADPTQVQAA APGYAAPVSP QVAQMTQQFG
AMGMTDPHLL PPQPVAPAPQ AQAPRAVPLN QLYPTDLLTQ PFNVAELDYP PPPIVLPPGT
SVYPSPYANC PPKYVRSTLN AVPTTSSLLK KSKLPFALVI QPYAALHDSE DPVPVVPDQV
ISRCRRCRSY INPFVTFLDH GHRWRCNMCN LTNDVPQAFD WDTALQKPAD RSLRPDLNHS
VVEFVAPQEY MVRPPQPLVY LFLIDVSYAS VTNGLLATTA RCIRESLDRI PNADRRTRLG
FIAVDSSLHY FSIPRDGSEN SEPRMLVISD LDEPFLPIPG DLLVTLSECR ENIEIFLDKL
QEMFQNTQSN ACAMGSALRA GYKLISPVGG KMTVLSSSLP NIGHGSLTMR EDKKVLGTSK
ESSLLQTANS FYKSFAVECS KAQVSVDMFL FSSQYQDVAS LSNLPRYTGG QTYFYPGWNA
ARGEDAIKFA REFSDYLSSE IGLEAVLRVR ATTGLRMNTF YGNFFNRSSD LCAFPAFPRD
QAYVVEVAID ETVTKPVVCL QTAVLHTTCN GERRIRVLTL ALPTTQNLAD VYASADQQAV
ATYFSHKAVE RALSSGLEPA REALQTKAVE LLSTYRKELA GGSVSGGGLQ FPANLRGLPV
LFLAMIKNLG LRKSAQIPTD MRSAALCLLS TLPLPLLMQY IYPKMYSLHD MPDTAGLPDE
QTGEILLPPP INLSSERIVP YGLYLIDDGQ TQFLWVGRDA VPQLIEDVFG LQDKSQLRVG
KQNLPDVDNE FNQRVRAVVE KSRDHRSKGV GSIVVPHLYV VKEDGEPGLR LWAQTMLVED
RADQSVSLVQ WMGSLREKV
