SEC23_COCIM
ID SEC23_COCIM Reviewed; 772 AA.
AC Q1DY01; J3KET6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; ORFNames=CIMG_04812;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; EAS33788.3; -; Genomic_DNA.
DR RefSeq; XP_001245371.1; XM_001245370.2.
DR AlphaFoldDB; Q1DY01; -.
DR SMR; Q1DY01; -.
DR STRING; 246410.Q1DY01; -.
DR EnsemblFungi; EAS33788; EAS33788; CIMG_04812.
DR GeneID; 4563551; -.
DR KEGG; cim:CIMG_04812; -.
DR VEuPathDB; FungiDB:CIMG_04812; -.
DR InParanoid; Q1DY01; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000001261; 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..772
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000295459"
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 772 AA; 85989 MW; 99F78579272F772A CRC64;
MDYEALKDQW SEIEDRDGIR LSWNTFPSTR MEASRLVVPI GAIYTPLKER PDAPLLQYEP
VTCKQPCRAV LNPYANVDIR ARIWICPFCL QRNPLPPHYK DITENTIPPE LHPQSTTIEY
QLARPAPAPP IFLFVVDTCQ EEDGLKAVKD SLVMSLSLLP PNALVGLITF GTMAQVHELG
YTECAKSYVF KGSKDYTPKQ IQEMLGLLAP GLRAPAPQQQ PGRPAPAVAP AARFLLPVQQ
ADFQITNVLE QLQQDPWPVA NDRRPLRCTG VALSVAIGLM ETSFQNAGGR IMLFTSGPAT
EGPGLVVGPQ LREPIRSHHD IDRDNIKYYK KAVKFYDNLA KRVSHNGHIV DIFIGSLDQV
GLLEMKGLVN STGGHMVLTD AFTSSQFKQS FVRVFDRDAN DNLVMGFNAA LEVLTTKELK
VTGLIGHAVS LNKKSSSVGE TECGIGNTCS WKMCGIDPAA SYGIYFEIAN QGGPAPMQQG
PHKAMMQFLT YYQHSSGQYH LRVTTVARPL SSPAGDSALA QSFDQEAAAV LMARIAVFKA
DVDDGPDVLR WVDRMLIRLC SRFADYRKDD PTSFRLEKNF TLYPQFMFHL RRSQFLQVFN
NSPDETTFYR HVLNHEFVGD SLIMIQPTLD SYSLDHEGAQ PVLLDSASIQ PTHILLLDTF
FHILIFHGET MAAWRKAGYQ DKEGYDNFRA ILEQPKEDAK ELIQDRFPLP RFIICDAGGS
QARFLLSKLN PSTTHSSGGY GGTQSGQTIF TDDVSLHTFM EHLMKLAVSG TN
