ID G7XP74_ASPKW Unreviewed; 768 AA.
AC G7XP74;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212, ECO:0000256|RuleBase:RU365030};
GN ORFNames=AKAW_06734 {ECO:0000313|EMBL:GAA88620.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88620.1};
RN [1] {ECO:0000313|EMBL:GAA88620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88620.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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. {ECO:0000256|ARBA:ARBA00025471,
CC ECO:0000256|RuleBase:RU365030}.
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:0000256|ARBA:ARBA00011845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299,
CC ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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DR EMBL; DF126464; GAA88620.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XP74; -.
DR STRING; 1033177.G7XP74; -.
DR VEuPathDB; FungiDB:AKAW_06734; -.
DR eggNOG; KOG1986; Eukaryota.
DR InParanoid; G7XP74; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
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; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU365030};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365030};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 60..99
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 127..391
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 402..506
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 520..618
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 635..721
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 768 AA; 85388 MW; 3BCA3B9980A0ECB6 CRC64;
MDYEALKDQW SDVEDRDGIR LSWNTFPSSR MEASRLVVPI GAVYTPLKEK PDSPLLQYEP
VTCKAPCRAV LNPYANVDVR ARIWICPFCL MRNPLPPHYK DITESTIPPE LHPMSTTIEY
QLARPAPAPP IFVYVVDTCQ DDDSLKALKD SLIMSLSLLP VNALVGLITY GTMAQVHELG
YTECAKSYVF RGSKEYAAKQ VQEMLGLASG VRPNMPQQPA RPPLGPAARF LLPVQQAEFQ
ITNVLEQLQR DPWPVANDKR PLRCTGVALS VAVGLLETSF QNAGGRIMVF TSGPATEGPG
HVVGPELKEP IRSHHDIDRD NIKYYKKAVK FYDNMAKRAA NNGHIVDVFA GCLDQVGMLE
MKNLANYTGG HILLTDSFTS SQFKQSFVRI FDKDANDNLL MGFNASLEVL TTKELKVTGL
IGHAVSLNKK SSSVGETECG IGNTCAWKMC GIDPASSYGV YFEIANQGGP AAVQPGPQRG
MMQFLTYYQH SSGHYHLRVT TVARPLSGPA GDPTLAQSFD QEAAAVLMAR IAVFKAEVDD
GPDVLRWVDR MLIRLCSRFA DYRKDDPTSF RLEKNFTLYP QFMFHLRRSQ FLQVFNNSPD
ETAFYRHVLN HEDVGDSLVM IQPTLDSYSL EHEGSQPVLL DSASIQPAHI LLLDTFFHIL
IFHGETIAEW RKAGYQDQEG YENLKVLLEQ PKEDARELIS DRFPLPRFIV CDAGGSQARF
LLSKLNPSTT HTTGGYGGGV TSQTIFTDDV SLQTFMDHLM KLAVSGTS
//
