位置:首页 > 蛋白库 > SNF8_YEAST
SNF8_YEAST
ID   SNF8_YEAST              Reviewed;         233 AA.
AC   Q12483; D6W410;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Vacuolar-sorting protein SNF8;
DE   AltName: Full=ESCRT-II complex subunit VPS22;
DE   AltName: Full=Vacuolar protein-sorting-associated protein 22;
GN   Name=SNF8; Synonyms=VPS22; OrderedLocusNames=YPL002C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7785322; DOI=10.1002/yea.320110304;
RA   Yeghiayan P., Tu J., Vallier L.G., Carlson M.;
RT   "Molecular analysis of the SNF8 gene of Saccharomyces cerevisiae.";
RL   Yeast 11:219-224(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12194858; DOI=10.1016/s1534-5807(02)00219-8;
RA   Babst M., Katzmann D.J., Snyder W.B., Wendland B., Emr S.D.;
RT   "Endosome-associated complex, ESCRT-II, recruits transport machinery for
RT   protein sorting at the multivesicular body.";
RL   Dev. Cell 3:283-289(2002).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH VPS25 AND VPS36.
RX   PubMed=15469844; DOI=10.1016/j.devcel.2004.09.003;
RA   Teo H., Perisic O., Gonzalez B., Williams R.L.;
RT   "ESCRT-II, an endosome-associated complex required for protein sorting:
RT   crystal structure and interactions with ESCRT-III and membranes.";
RL   Dev. Cell 7:559-569(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH VPS25 AND VPS36.
RX   PubMed=15329733; DOI=10.1038/nature02914;
RA   Hierro A., Sun J., Rusnak A.S., Kim J., Prag G., Emr S.D., Hurley J.H.;
RT   "Structure of the ESCRT-II endosomal trafficking complex.";
RL   Nature 431:221-225(2004).
CC   -!- FUNCTION: Component of the endosomal sorting complex required for
CC       transport II (ESCRT-II), which is required for multivesicular body
CC       (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC       MVB pathway mediates delivery of transmembrane proteins into the lumen
CC       of the lysosome for degradation. The ESCRT-II complex is probably
CC       involved in the recruitment of the ESCRT-III complex.
CC       {ECO:0000269|PubMed:12194858}.
CC   -!- SUBUNIT: Component of the endosomal sorting complex required for
CC       transport II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of
CC       SNF8, and 1 copy of VPS36. The ESCRT-II complex interacts directly with
CC       the VPS20 subunit of the ESCRT-III complex.
CC       {ECO:0000269|PubMed:12194858, ECO:0000269|PubMed:15329733,
CC       ECO:0000269|PubMed:15469844}.
CC   -!- INTERACTION:
CC       Q12483; P47142: VPS25; NbExp=6; IntAct=EBI-30277, EBI-25595;
CC       Q12483; Q06696: VPS36; NbExp=10; IntAct=EBI-30277, EBI-36540;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12194858}. Endosome
CC       membrane {ECO:0000269|PubMed:12194858}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12194858}.
CC   -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF8 family. {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; U10361; AAA86824.1; -; Genomic_DNA.
DR   EMBL; U33335; AAB68103.1; -; Genomic_DNA.
DR   EMBL; Z71255; CAA95039.1; -; Genomic_DNA.
DR   EMBL; Z48483; CAA88384.1; -; Genomic_DNA.
DR   EMBL; AY692759; AAT92778.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11426.1; -; Genomic_DNA.
DR   PIR; S52529; S52529.
DR   RefSeq; NP_015323.1; NM_001183816.1.
DR   PDB; 1U5T; X-ray; 3.60 A; A=1-233.
DR   PDB; 1W7P; X-ray; 3.60 A; A=1-233.
DR   PDBsum; 1U5T; -.
DR   PDBsum; 1W7P; -.
DR   AlphaFoldDB; Q12483; -.
DR   SMR; Q12483; -.
DR   BioGRID; 36175; 130.
DR   ComplexPortal; CPX-1623; ESCRT-II complex.
DR   DIP; DIP-1745N; -.
DR   IntAct; Q12483; 6.
DR   MINT; Q12483; -.
DR   STRING; 4932.YPL002C; -.
DR   TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   MaxQB; Q12483; -.
DR   PaxDb; Q12483; -.
DR   PRIDE; Q12483; -.
DR   EnsemblFungi; YPL002C_mRNA; YPL002C; YPL002C.
DR   GeneID; 856105; -.
DR   KEGG; sce:YPL002C; -.
DR   SGD; S000005923; SNF8.
DR   VEuPathDB; FungiDB:YPL002C; -.
DR   eggNOG; KOG3341; Eukaryota.
DR   GeneTree; ENSGT00390000007843; -.
DR   HOGENOM; CLU_070147_0_1_1; -.
DR   InParanoid; Q12483; -.
DR   OMA; SNTEQGC; -.
DR   BioCyc; YEAST:G3O-33921-MON; -.
DR   Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   EvolutionaryTrace; Q12483; -.
DR   PRO; PR:Q12483; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12483; protein.
DR   GO; GO:0000814; C:ESCRT II complex; IDA:SGD.
DR   GO; GO:1904669; P:ATP export; IMP:SGD.
DR   GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR   DisProt; DP01604; -.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR016689; ESCRT-2_cplx_Snf8.
DR   InterPro; IPR040608; Snf8/Vps36.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12806; PTHR12806; 1.
DR   Pfam; PF04157; EAP30; 1.
DR   PIRSF; PIRSF017215; ESCRT2_Vps22; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Endosome; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..233
FT                   /note="Vacuolar-sorting protein SNF8"
FT                   /id="PRO_0000215214"
FT   COILED          23..46
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   233 AA;  26954 MW;  212C74F086A0325E CRC64;
     MKQFGLAAFD ELKDGKYNDV NKTILEKQSV ELRDQLMVFQ ERLVEFAKKH NSELQASPEF
     RSKFMHMCSS IGIDPLSLFD RDKHLFTVND FYYEVCLKVI EICRQTKDMN GGVISFQELE
     KVHFRKLNVG LDDLEKSIDM LKSLECFEIF QIRGKKFLRS VPNELTSDQT KILEICSILG
     YSSISLLKAN LGWEAVRSKS ALDEMVANGL LWIDYQGGAE ALYWDPSWIT RQL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024