SEC23_NEOFI
ID SEC23_NEOFI Reviewed; 780 AA.
AC A1D4S4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein transport protein sec23;
GN Name=sec23; ORFNames=NFIA_021250;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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.
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; DS027688; EAW23417.1; -; Genomic_DNA.
DR RefSeq; XP_001265314.1; XM_001265313.1.
DR AlphaFoldDB; A1D4S4; -.
DR SMR; A1D4S4; -.
DR STRING; 36630.CADNFIAP00001928; -.
DR EnsemblFungi; EAW23417; EAW23417; NFIA_021250.
DR GeneID; 4591624; -.
DR KEGG; nfi:NFIA_021250; -.
DR VEuPathDB; FungiDB:NFIA_021250; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000006702; 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; 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..780
FT /note="Protein transport protein sec23"
FT /id="PRO_0000295466"
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 780 AA; 86789 MW; E4346FB738569AC7 CRC64;
MDYEALKDQW SDVEDRDGIR LSWNTFPSTR MEASRLVVPI AAVYTPLKEK PDSPLLQYEP
VTCKAPCRAV LNPYANVDVR ARIWICPFCL MRNPLPPHYK DITENAIPPE LHPQSTTIEY
QLARPAPAPP IFVYVVDTCQ EEDSLKALKD TLILSLSLLP PNALVGLITY GTMAQVHELG
YTECAKSYVF RGSKEYAAKQ VQEMLGLLAA GPRPNMPQQP ARPPVGPAAR FLLPVQQAEF
QITNVLEQLQ RDPWPVANDK RPLRCTGVAL SVAVGLLETS FQNAGGRIMV FTSGPATEGP
GHVVGPELKE PMRSHHDIDR DNIKYYKKAV KFYDALAKRA ANNGHVVDIF AGCLDQVGLL
EMKNLANFTG GHMLLTDSFT SSQFKQSFVR VFDKDANDNL LMGFNASLEV LTTKELKVTG
LIGHAVSLNK KSSSVGETEC GIGNTCAWKM CGIDPSSSYG VYFEIANQGG PAAVQPGPQR
GMMQFLTYYQ HASGHYHLRV TTVARPLSGP TGDPTLAQSF DQEAAAVLMA RIAVYKADVD
DGPDVIRWVD RMLIRLCSRF ADYRKDDPTS FRLEKNFTLY PQFMFHLRRS QFLQVFNNSP
DETAFYRHVL NHEDVGDALV MIQPTLDSYS LEHEGSQPVL LDSASIQPTH ILLLDTFFHI
LIFHGETIAE WRKAGYQDQE GYENLKALLE QPKEDARELI ADRFPLPRFI VCDAGGSQAR
FLLSKLNPST THTTGGYGGG VTSQTIFTDD VSLQTFMDHL MKYAIPTCFT IVMNDANPPI
