SEC24_MAGO7
ID SEC24_MAGO7 Reviewed; 959 AA.
AC A4QUL1; G4N0Z2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; ORFNames=MGG_09564;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001233; EHA52370.1; -; Genomic_DNA.
DR RefSeq; XP_003712177.1; XM_003712129.1.
DR AlphaFoldDB; A4QUL1; -.
DR SMR; A4QUL1; -.
DR STRING; 318829.MGG_09564T0; -.
DR EnsemblFungi; MGG_09564T0; MGG_09564T0; MGG_09564.
DR GeneID; 2680462; -.
DR KEGG; mgr:MGG_09564; -.
DR VEuPathDB; FungiDB:MGG_09564; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; A4QUL1; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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..959
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295491"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..308
FT /note="Zinc finger-like"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 959 AA; 104630 MW; B35FC5065FF56654 CRC64;
MSAPDQGYGQ YPPAGQQYDQ QQQPYPDQQG FEAQPGAPPQ AGAPPTADGR KKKRNYAAGA
FDVGTGANVA PGAGPPMPGQ TPQYGMPPAG QPAYGGFAQQ PDPQAPVYGD PSQQQPQQYG
APMASPGQPG VGGYQAPDPY YTSGVGAPGA PAGPGGVAGL TSNLAGMQLG PGQPAQAPAQ
QQARPTPLNQ LYPTDLLNQP FNVSELDLPP PPVILPLNSS VTSSPMANCP PKYVRSTLNA
VPTTHSLLKK SKLPFALVIQ PYAALHDHED NVPLVQDQVI SRCRRCRSYI NPYVVFLDQG
HRWRCNMCNL TNDVPQAFDW DAAEQRAVDR WQRHELNHAV VEFVAPQEYM VRPPQPLVYL
FLFDVSYAAV SSGLLATSAR TILDSLNRIP NADRRTRLGF IAVDSSLHYF AVPKDGDENA
ETSMLVVSDL DEPFLPVPQE LLVPLTDSRQ RIENFLTKLP EMFQNTTNNG SCMGSALRAG
HKLISPLGGK IVVLSASLPN VGYGKLDMRE DKKVLGTSKE NSLLQTANSF YKSFAVDSSK
NQVSIDMFLF SSQYQDVASL SNLPRYTGGQ TWFYPGWNAG RPEDAIKFAS EFSDYLSSEI
GLEAVLRVRA TTGLRMSSFY GNFFNRSSDL CAFPAFPRDQ CYVVEVAIDE TLGKNVVCMQ
TAVLHTTCNG ERRIRVITLA LPTTTNLADV YASADQCAIT TYFSHKAVEK ALSSGLEAAR
DSLQSKLTEL LQTFRKELAG GSMGGGLQFP ANLRGLPALF LGLIKNVGLR KSAQIPSDLR
SAALCLLSTL PLPLLVQYIY PRLYSLHDMP DNAGIPDPET SQIVLPPPLN LSSERFQPFG
LYLIDDGQTQ FLWVGRDAVP QLLIDVFGVQ DRTQLRVGKG SVPELDNDFN ERVRAVISKS
RDYKSRGVGS ITVPHLYIVR EDGEPALKLW AQTLLVEDRA DQGMSYQQWM GTLREKVVQ
