SEC23_ASPCL
ID SEC23_ASPCL Reviewed; 762 AA.
AC A1CRW7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein transport protein sec23;
GN Name=sec23; ORFNames=ACLA_031210;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW08388.1; -; Genomic_DNA.
DR RefSeq; XP_001269814.1; XM_001269813.1.
DR AlphaFoldDB; A1CRW7; -.
DR SMR; A1CRW7; -.
DR STRING; 5057.CADACLAP00002848; -.
DR PRIDE; A1CRW7; -.
DR EnsemblFungi; EAW08388; EAW08388; ACLA_031210.
DR GeneID; 4700609; -.
DR KEGG; act:ACLA_031210; -.
DR VEuPathDB; FungiDB:ACLA_031210; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000006701; 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..762
FT /note="Protein transport protein sec23"
FT /id="PRO_0000295450"
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 762 AA; 84789 MW; E79DF9F5806BA0C9 CRC64;
MDYEALKDQW SDVEERDGIR LSWNTFPSTR MEASRLVVPI AAVYTPLKEK PESPLLQYEP
VTCKAPCRAV LNPYANVDVR ARIWICPFCL MRNPLPPHYK DITENAIPPE LHPQSTTIEY
QLARPAPAPP IFVYVVDTCQ EEDSLKALKD TLILSLSLLP PNALVGLITF GTMAQVHELG
YTECAKSYVF RGSKDYAAKQ VQEMLGLLAP GPRPNVPQQP ARPPVGPAAR FLLPVQQAEF
QITNVLEQLQ RDPWPVANDK RPLRCTGVAL SVAVGLLETS FQNAGGRVMV FTSGPATEGP
GHVVGPELKE PIRSHHDIDR DNIKYYKKAV KFYDALAKRA ANNGHVVDIF AGCLDQVGLL
EMKNLSNFTG GHMLLTDSFT SSQFKQSFVR VFDKDANDNL LMGFNASLEV LTTKELKVTG
LIGHAVSLNK KSSSVGETEC GIGNTCAWKM CGIDPASSYG VYFEIANQGG PAAVQPGPQR
GMMQFLTYYQ HSSGHYHLRV TTVARPLSGP TGDPALAQSF DQEAAAVLMA RIAVYKADVD
DGPDVIRWVD RMLIRLCSRF ADYRKDDPTS FRLEKNFTLY PQFMFHLRRS QFLQVFNNSP
DETAFYRHVL NHEDVGDSLV MIQPTLDSYS LEHEGSQPVL LDSASIQPTH ILLLDTFFHI
LIFHGETIAE WRKAGYQDQE GYENLKALLE QPKEDARELI ADRFPLPRFI VCDAGGSQAR
FLLSKLNPST THTTGGYGGG VTSQTIFTDD VSLQTFMDHL MK
