SEC23_CHAGB
ID SEC23_CHAGB Reviewed; 773 AA.
AC Q2HB00;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; ORFNames=CHGG_02604;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ90669.1; -; Genomic_DNA.
DR RefSeq; XP_001229120.1; XM_001229119.1.
DR AlphaFoldDB; Q2HB00; -.
DR SMR; Q2HB00; -.
DR STRING; 38033.XP_001229120.1; -.
DR PRIDE; Q2HB00; -.
DR EnsemblFungi; EAQ90669; EAQ90669; CHGG_02604.
DR GeneID; 4389933; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q2HB00; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000001056; 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..773
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000295458"
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 773 AA; 86249 MW; CCC504E3AA9F2F0B CRC64;
MDYDSMKEQW GEVEDRDGVR LSWNVFPSTR MEASRLVVPI GALYTPLKEK PDTPLLQFEP
VTCKQPCRSV LNPFCQVDVR ARLWICPFCL SRNPLPPHYK DITAQAIPPE LHPSNTTIEY
RLSRPAPSPP IFLYVVDTCQ EEDSLAALKE SLIMSLSLLP ENALVGLITY GTMAQVHEIG
YTECAKSYVF RGSKEYAAKQ VQEMLGLIQP AMRPGMPAHQ PGRPMPMGPA SRFLLPVTQA
EFQLTKALEQ LQQDPWPISS DRRNLRCTGV ALSVAVGLLE TSFQNAGGRI MLFAGGPATE
GPGMVVGPEL REPIRSHHDI DRDNVKYYKK ALKFYDNLAK RTAHNGHTID IFAGCLDQVG
LLEMKGLCNS TGGHMILTDS FTSSMFKQSF IRVFEKDGDD NLLMGFNAVL EVLTTKELKV
TGLIGHAVSL NKKSTSVGET ECGIGNTCSW KMCGIDPKAS YGVYFEIAQG GPSQHQQNQK
GMIQFLTYYQ HSSGQFHLRV TTIARDLSGP AGDPAIAHSF DQEAAAVLMS RIAVFKAEVD
DGPDVLRWVD RMLIRLCSRF ADYRKDDPSS FRLEKNFTLY PQFMFHLRRS QFLQVFNNSP
DETAFYRHVL DHEDVSNSLV MIQPTLDSYT FDQEGGQPVL LDSSSIQPTH ILLLDTFFHI
LIFHGETVAE WRKAGYQDQE GYENFASLLE QPKEDARDLI TDRFPLPRFI VCDHGGSQAR
FLLSKLNPST THTSGAGAYG GVGAQSAQTI FTDDVSLQTF MEHLMKLAVS GTN
