SEC23_ENCCU
ID SEC23_ENCCU Reviewed; 707 AA.
AC Q8SQX2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; OrderedLocusNames=ECU11_0790;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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: Component of the COPII coat. {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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590450; CAD25989.1; -; Genomic_DNA.
DR RefSeq; NP_586385.1; NM_001042218.1.
DR AlphaFoldDB; Q8SQX2; -.
DR SMR; Q8SQX2; -.
DR STRING; 284813.Q8SQX2; -.
DR PRIDE; Q8SQX2; -.
DR GeneID; 860038; -.
DR KEGG; ecu:ECU11_0790; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_0790; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q8SQX2; -.
DR OMA; HVFMHED; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000000819; Chromosome XI.
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 1: Evidence at protein level;
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..707
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000383109"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 707 AA; 80575 MW; BC6E7F6AAACCB4DE CRC64;
MEEEIRNIEE NDGIRLTWNV WPAKGDATTK IPLACLYNIH QTADVLECEP IYCMSCNSVL
NPHCNIDFGR QSWNCVICNN NTTLPSHARG ITPDNLLPEL LPQNSTVEYV LSRESVFPVV
FFLIVDICTF DGERHTLLKD TLKVVLEKIP EDALVGFVKY GTNIELLELN AEQPRRTHLF
SGRKEYTAEI LKSLGGASKS ESQIVGRFLR RKDECQELLY NMVESLERDP FPVLPAYKPV
RCTGSAVSLA ISLLETSFPD MAVKYLLFTQ GPCTFGPGTV TPIKFKEKGR NEHLEENDPM
YAGPARKFYT GLAERMNSVG HSLDILAATI VDVGICHMER LTGMTGGMLI MAQDFDRDIY
ISSCSKILDR SSEGCLVQGF NAKMHVKTSK NLEYKGVIGQ GRSFGGSWRM GSMFPSTNIS
LLFDKKPDAK HGEFGYVQLI TQYQRSDKRL LVKVTTFARM FTDSREDVIY GFDQEAVAVF
QARFLLLKKY EEIKDCERMI DKNLIRFTKT FARYDKGEPS SLALPDSMAY YPNYMFFFRR
SLLVQTGNNS PDETTYYSTL LYNQRVSDAL KLIKPTLISY HYQGGVEAVE VDSKSLEPDV
ILVLDTFHNV VVWRGEYVAQ WVREGYHEQA EYEFLKDILK SSEERARLLC NERLPTPQFC
ITEQNKSQQR ILHHYVNPSG GGSIITENIN YEKFEEALRR VVVFNSE
