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SEC24_PICGU
ID   SEC24_PICGU             Reviewed;         918 AA.
AC   A5DPC0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24; ORFNames=PGUG_05121;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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. Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
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. SEC24 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH408160; EDK41023.2; -; Genomic_DNA.
DR   RefSeq; XP_001483166.1; XM_001483116.1.
DR   AlphaFoldDB; A5DPC0; -.
DR   SMR; A5DPC0; -.
DR   STRING; 4929.XP_001483166.1; -.
DR   PRIDE; A5DPC0; -.
DR   EnsemblFungi; EDK41023; EDK41023; PGUG_05121.
DR   GeneID; 5124693; -.
DR   KEGG; pgu:PGUG_05121; -.
DR   VEuPathDB; FungiDB:PGUG_05121; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   InParanoid; A5DPC0; -.
DR   OMA; TFPRDQS; -.
DR   OrthoDB; 330236at2759; -.
DR   Proteomes; UP000001997; 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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd01479; Sec24-like; 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; IPR036180; Gelsolin-like_dom_sf.
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; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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..918
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295494"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..244
FT                   /note="Zinc finger-like"
FT   COMPBIAS        62..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   918 AA;  101431 MW;  2539B6088ACD4A25 CRC64;
     MSKRRAYPQP QYAISQDQAP ATPPVGASAA YGVPQVAQQF QQMNINPQPG AQPGAAVPQG
     YGYNQYGQQP QPGQAYDPYQ QPPQANTGFG GQQQTPSQQP YQQQGGYFGA GAGGQAAPAL
     PLNQLYTTDL SRELPPPISD LSLPPPPLVI PSNTAIVPTS EDSNASPDYF RSTLNVIPNN
     GTLLKRSKLP LALVVRPYTT LRVDQENIPA ASDTIISRCR RCRCYINPFV TLTEQGRRWR
     CNLCNLQNDI PAAFEYDETR GVPRNKFDRV ELNHSVVEFV APKEYMARAP QPIVFVFVID
     VSADAVNSGL TSTVTRTILE SLDRIPNQNK TARVAFLGVD SNLHYFRFDE GLEGSELLIA
     SDLDEPFLPS PSGLLINLEE NRPAIEKLLI DFPTYFENTA NTQFALGPAL KAGHKMIANI
     GGKLITFAAS LPNIGEGKLS VRDEASHSGQ PKESQMLLGA ADKFYKSFAV ECNSAQVTVD
     LFLTSARYQD VATLSNLPRF TAGQTHFYPA WSCVKPEDVT KLSKEISEHL SMDIALEAVL
     RVRSSTGMRS SAFYGNFFNR SSDLCSFPSF PRDQSYVIEM SIEETITKPV VYFQAASLHS
     TSYGERRIRV MNLAIPTSSK LDDIYASADQ LAIANYFTHK AVEKALASSL PDARNYIVKS
     IVDILNVYKK ELVAGNVSGS SPLQISTNLR MLPLLLFSLT KHLGLRGERV PSDHRAAALN
     RLSSLPIPHL IKYIYPTVYS LHNMGDECGL PEQTVTVNEE TGEEETTSGG ILLPEPINDT
     KASWENYGLY LIDNSSEVFL WVSGDVVPDL VYDLFGTDNL YSIPTGKTEL PELQPDESEF
     NYRVRNILGK IREQKDQITW KNLYVVIGGS SNEPIEISQQ RDLMALRMWA LSCLVEDKTA
     NEQGYREFLT SLKGKVAQ
 
 
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