SEC23_PHANO
ID SEC23_PHANO Reviewed; 776 AA.
AC Q0US25;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; ORFNames=SNOG_05439;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT87830.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAT87830.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH445331; EAT87830.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001795844.1; XM_001795792.1.
DR AlphaFoldDB; Q0US25; -.
DR SMR; Q0US25; -.
DR STRING; 13684.SNOT_05439; -.
DR PRIDE; Q0US25; -.
DR GeneID; 5972719; -.
DR KEGG; pno:SNOG_05439; -.
DR eggNOG; KOG1986; Eukaryota.
DR InParanoid; Q0US25; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
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..776
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000295468"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 86165 MW; DE0E3A90DA8C51CD CRC64;
MADFEAMKDT WSDVEDRDGV RLSWNTFPSS RMEASRLVVP IGALYTPLKE KTDTPLLQYE
PVVCRAPCKG VLNPYCQVDM RARVWICPFC LNRNQLPPHY KDISQEQIPP ELHPSSTTIE
YRLPKPARCA PIFIFVIDTC QEEDSLKALK DSIIMSLSLL PAYALVGLIT YGTMTQVHEL
GYTECAKSYV FRGNKDYSTK QVQTMIGLGQ MAAPRPGMQA QPGQPGGAPP TAAMRFILPV
GQCEFQLTNV LESLQRDPWP VANDKRALRC TGVALSVASG LLEASNFVNT GARIMLFAGG
PATEGPGMVV GPELREPIRS HHDIDRDNIK YYKKALKFYE TLAKRVSTNG HIVDIFAGCL
DQVGLLEMRG LANTTGGHMI LTDSFTSSMY KQSFARVFNK DADDNLLMGF NAEMEVLTTK
ELKVTGLIGH AVSLNKKSVN VGETECGIGN TCAWKMCGID PEASYGIYFE IAGQGGPSGM
TGGAPQAIMQ FLTYYQHSSG QMHLRVTTVS RPMSGPSGDP ALAQSFDQEA AAVLMSRIAV
FKAEVDDGPD VLRWVDRMLI RLCSRFAEYR KDDPSSFRLE KNFTLYPQFM FHLRRSQFLQ
VFNNSPDETA FYRHVLNHED VGNSLVMIQP TLDSYGFDHE GGQPVLLDSA SIQSETVLLL
DTFFHILIFH GETMAEWRKA GYQDQEGYEN FRTLLEAPKE DAKDLIQDRF PLPRFIVCDA
GGSQARFLLS KLNPSTTHQT STYGGVAQTA QTIFTDDVSL QTFMDHLMKL AVSGTS
