SEC23_ASPTN
ID SEC23_ASPTN Reviewed; 771 AA.
AC Q0CUU1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein transport protein sec23;
GN Name=sec23; ORFNames=ATEG_02543;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37505.1; -; Genomic_DNA.
DR RefSeq; XP_001211721.1; XM_001211721.1.
DR AlphaFoldDB; Q0CUU1; -.
DR SMR; Q0CUU1; -.
DR STRING; 341663.Q0CUU1; -.
DR EnsemblFungi; EAU37505; EAU37505; ATEG_02543.
DR GeneID; 4316845; -.
DR VEuPathDB; FungiDB:ATEG_02543; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000007963; 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..771
FT /note="Protein transport protein sec23"
FT /id="PRO_0000295454"
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 771 AA; 85634 MW; C2B459E0D1427E61 CRC64;
MDYEALKDYW TDIEDRDGIR LSWNKFPSSR MEASRLVVPI GAVYTPLKER PDAPLLQYAP
VTCKPPCNGV LNPYANVDDR ARIWICPFCL MRNPLPPQYK DISATVVPPE LHPLNTTIEY
QLPRGPRPAP PPPIFVYVVD TCQEEDSLKA LKDALVVSLS LLPPNALVGL ITFGTMAQVH
EIGYTECAKS YVFRGSKEYA AKQVQEMLGL SQGMRPAMPN QPPQGPLGPA ARFLLPVQQA
EFQITNVLEQ LQRDPWPVAN DKRPLRCTGV ALGVAVGLLE TSFQNAGARI MLFTSGAATE
GPGLVVGHEL KEPIRSHHDI DRDNIKYYKK AVKFYDNMAK RAAHNGHIVD IFAGCLDQVG
LLEMKNLSNY TGGHMLLTDS FTSSQFKQSF IRVFDKDAND NLLMGFNASL EVLTTKELKV
TGLIGHAVSL NKKSSSVGET ECGIGNTCAW KMCGIDPASS YGIYFEVANQ GGPAAVQPGT
QKGVMQFLTY YQHSSGHYHL RVTTVGRELS GPAGDPTLAQ SFDQEAAAVL MARIAVFKAE
VDDGPDVLRW VDRMLIRLCS RFADYRKDDP TSFRLEKNFT LYPQFMFHLR RSQFLQVFNN
SPDETAFYRH VLNHEDVGDS LVMIQPTLDS YSLEHEGSQP VLLDSASIQP THILLLDTFF
HILIFHGETI AEWRKAGYQD QEGYENIKAL LEQPKEDARE LIADRFPLPR FIVCDAGGSQ
ARFLLSKLNP STTHTTGGYG GGVTSQTIFT DDVSLQTFMD HLMKLAVSGT S
