ENV7_YEAST
ID ENV7_YEAST Reviewed; 364 AA.
AC Q12003; D6W3D4; Q7LGU7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase ENV7;
DE EC=2.7.11.1;
DE AltName: Full=Late endosome and vacuole interface protein 7;
GN Name=ENV7; OrderedLocusNames=YPL236C;
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 [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 [2]
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 [3]
RP FUNCTION.
RX PubMed=11062466; DOI=10.1038/81576;
RA Zhu H., Klemic J.F., Chang S., Bertone P., Casamayor A., Klemic K.G.,
RA Smith D., Gerstein M., Reed M.A., Snyder M.;
RT "Analysis of yeast protein kinases using protein chips.";
RL Nat. Genet. 26:283-289(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP PALMITOYLATION AT CYS-13; CYS-14 AND CYS-15.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21912603; DOI=10.1371/journal.pone.0023696;
RA Ricarte F., Menjivar R., Chhun S., Soreta T., Oliveira L., Hsueh T.,
RA Serranilla M., Gharakhanian E.;
RT "A genome-wide immunodetection screen in S. cerevisiae uncovers novel genes
RT involved in lysosomal vacuole function and morphology.";
RL PLoS ONE 6:E23696-E23696(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in vacuolar
CC processing and morphology. {ECO:0000269|PubMed:11062466,
CC ECO:0000269|PubMed:21912603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Peripheral membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to internal accumulation of precursor CPY.
CC {ECO:0000269|PubMed:21912603}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; Z67751; CAA91608.1; -; Genomic_DNA.
DR EMBL; Z73591; CAA97953.1; -; Genomic_DNA.
DR EMBL; Z73592; CAA97954.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11200.1; -; Genomic_DNA.
DR PIR; S61028; S61028.
DR RefSeq; NP_015088.1; NM_001184050.1.
DR AlphaFoldDB; Q12003; -.
DR SMR; Q12003; -.
DR BioGRID; 35926; 78.
DR DIP; DIP-6626N; -.
DR IntAct; Q12003; 5.
DR STRING; 4932.YPL236C; -.
DR iPTMnet; Q12003; -.
DR SwissPalm; Q12003; -.
DR MaxQB; Q12003; -.
DR PaxDb; Q12003; -.
DR PRIDE; Q12003; -.
DR EnsemblFungi; YPL236C_mRNA; YPL236C; YPL236C.
DR GeneID; 855840; -.
DR KEGG; sce:YPL236C; -.
DR SGD; S000006157; ENV7.
DR VEuPathDB; FungiDB:YPL236C; -.
DR eggNOG; KOG2345; Eukaryota.
DR GeneTree; ENSGT00550000075037; -.
DR HOGENOM; CLU_000288_109_1_1; -.
DR InParanoid; Q12003; -.
DR OMA; MHQYKVK; -.
DR BioCyc; YEAST:G3O-34123-MON; -.
DR PRO; PR:Q12003; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12003; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0006624; P:vacuolar protein processing; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Vacuole.
FT CHAIN 1..364
FT /note="Serine/threonine-protein kinase ENV7"
FT /id="PRO_0000255977"
FT DOMAIN 30..364
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 13
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
FT LIPID 14
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
FT LIPID 15
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
SQ SEQUENCE 364 AA; 40749 MW; 3A7439E4077BAD20 CRC64;
MISIVLELFQ NLCCCRGFSD ATIRVNDKRY RIQRLLGEGG MSFVYLVQLS KNSLIIDNGI
ATPELYALKK IICPSVESIS NGMREIENYK RFQSPYVIKS IDSQVMQEKD GSKTIYIVLP
YYSLGSLQDS INRRLLEGTF VSEAECVRIM LGVTRGLLCL HDPASRQDNA TSRVNVDAVS
MTYSDETAML LEDTPLEMDM LSSNSAGSIA YAHRDITPSN ILFSSDGLPV IGDLGSCSQA
DITIENRHQL SELQEWVNDN CTLPYTPPEL LNLKLNQVLS SKVDIWSLGC TFYTLMFGIS
PFEREEQIHG ASLTYAINTG KYSFPRNSRF SEGLLSVIKK CIQVDPIQRP TTSQLLNLLQ
DLDT
