SEC23_MAGO7
ID SEC23_MAGO7 Reviewed; 770 AA.
AC A4R1J7; G4MN10;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; ORFNames=MGG_06910;
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.
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. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; CM001231; EHA57032.1; -; Genomic_DNA.
DR RefSeq; XP_003709644.1; XM_003709596.1.
DR AlphaFoldDB; A4R1J7; -.
DR SMR; A4R1J7; -.
DR STRING; 318829.MGG_06910T0; -.
DR PRIDE; A4R1J7; -.
DR EnsemblFungi; MGG_06910T0; MGG_06910T0; MGG_06910.
DR GeneID; 2685083; -.
DR KEGG; mgr:MGG_06910; -.
DR VEuPathDB; FungiDB:MGG_06910; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; A4R1J7; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
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:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11287; Sec23_C; 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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PTHR11141; 1.
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..770
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000295465"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 770 AA; 85918 MW; 54884E993D159350 CRC64;
MDYENLKEQW SEVEDRDGVR LSWNVFPSTR MEASRLVVPI GALYTPLKEK PDTPLLQFEP
VTCKQPCRSV LNPFCQVDVR ARLWICPFCL SRNPLPPHYK DITANAIPPE LHPSNTTIEY
RLSRPAPSPP IFLYVVDTCQ EDDSLNALKE SLVMSLSLLP ENALVGLITY GTMTQVHEIG
YTECAKSYVF RGSKDYAPKQ VQEMLGLGQM PVRPGMQPQP GRPMPMGPAS RFLMPVSQCE
FQLTKALEQL QKDPWPVAND RRPLRCTGVA LSVAVGLLES SFQNSGGRIM LFAAGPATEG
PGMVVSSELR EPMRSHHDID RDNIKYYKKA LKFYDTLAKR TAHNGHIIDI FAGCLDQVGL
LEMKGLSNST GGHMILVDSF TSSMFKQSFV RVFEKDGDDN LLMGFNGILE VLTTKELKVT
GLIGHAVSMN KKSTSVGETE CGIGNTCSWK MCGIDPTSSY GIYFEVAQGG PSHAQPAQKG
MMQFLTYYQH SSGQFHLRVT TIARNIGGPA GDPAIAQSFD QEAAAVLMSR IAVFKAEVDD
GPDVLRWVDR MLISLCSRFA DYRKDDPSSF RLEKNFTLYP QFMFHLRRSQ FLQVFNNSPD
ETAFYRHVLN HEDVSNSLIM IQPTLDTYTF DQEGGQPVLL DSASIQPTHI LLLDTFFHIL
IFHGETIAQW KKAGYQDQEG YENFAQLLQQ PKEDAMELIT DRFPLPRFIV CDAGGSQARF
LLSKLNPSTT HTTGAYGGVG AQTAQTIFTD DVSLQTFMDH LMKLAVSGTN
