AKR1_YEAST
ID AKR1_YEAST Reviewed; 764 AA.
AC P39010; D6VSP8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=YDR264C; ORFNames=D9954.9, YD9230B.03C;
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], AND FUNCTION.
RX PubMed=8524293; DOI=10.1128/mcb.16.1.168;
RA Kao L.-R., Peterson J., Ji R., Bender L., Bender A.;
RT "Interactions between the ankyrin repeat-containing protein Akr1p and the
RT pheromone response pathway in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:168-178(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION.
RX PubMed=9243510; DOI=10.1091/mbc.8.7.1317;
RA Givan S.A., Sprague G.F. Jr.;
RT "The ankyrin repeat-containing protein Akr1p is required for the
RT endocytosis of yeast pheromone receptors.";
RL Mol. Biol. Cell 8:1317-1327(1997).
RN [5]
RP FUNCTION.
RX PubMed=10866691; DOI=10.1128/mcb.20.14.5350-5359.2000;
RA Feng Y., Davis N.G.;
RT "Akr1p and the type I casein kinases act prior to the ubiquitination step
RT of yeast endocytosis: Akr1p is required for kinase localization to the
RT plasma membrane.";
RL Mol. Cell. Biol. 20:5350-5359(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, AND MUTAGENESIS OF
RP 497-ASP--HIS-498 AND CYS-500.
RX PubMed=12370247; DOI=10.1083/jcb.200206120;
RA Roth A.F., Feng Y., Chen L., Davis N.G.;
RT "The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl
RT transferase.";
RL J. Cell Biol. 159:23-28(2002).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=15105419; DOI=10.1074/jbc.m403071200;
RA Babu P., Deschenes R.J., Robinson L.C.;
RT "Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary
RT and sufficient for plasma membrane targeting.";
RL J. Biol. Chem. 279:27138-27147(2004).
RN [10]
RP TOPOLOGY.
RX PubMed=15632165; DOI=10.1074/jbc.m411946200;
RA Politis E.G., Roth A.F., Davis N.G.;
RT "Transmembrane topology of the protein palmitoyl transferase Akr1.";
RL J. Biol. Chem. 280:10156-10163(2005).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, AND
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine
CC residues, which is required for their proper plasma membrane
CC localization. Required for constitutive endocytosis of a-factor
CC receptor STE3 and both constitutive and pheromone-induced endocytosis
CC of alpha-factor receptor STE2. {ECO:0000269|PubMed:10866691,
CC ECO:0000269|PubMed:12370247, ECO:0000269|PubMed:15105419,
CC ECO:0000269|PubMed:8524293, ECO:0000269|PubMed:9243510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225;
CC -!- INTERACTION:
CC P39010; P18851: STE4; NbExp=3; IntAct=EBI-2421, EBI-7390;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane
CC protein. Golgi apparatus membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC -!- MISCELLANEOUS: Present with 4072 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR EMBL; L31407; AAC41676.1; -; Genomic_DNA.
DR EMBL; U51030; AAB64454.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94103.1; -; Genomic_DNA.
DR EMBL; Z68290; CAA92582.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12108.1; -; Genomic_DNA.
DR PIR; S48521; S48521.
DR RefSeq; NP_010550.1; NM_001180572.1.
DR AlphaFoldDB; P39010; -.
DR SMR; P39010; -.
DR BioGRID; 32320; 190.
DR DIP; DIP-1145N; -.
DR IntAct; P39010; 40.
DR MINT; P39010; -.
DR STRING; 4932.YDR264C; -.
DR iPTMnet; P39010; -.
DR SwissPalm; P39010; -.
DR MaxQB; P39010; -.
DR PaxDb; P39010; -.
DR PRIDE; P39010; -.
DR EnsemblFungi; YDR264C_mRNA; YDR264C; YDR264C.
DR GeneID; 851857; -.
DR KEGG; sce:YDR264C; -.
DR SGD; S000002672; AKR1.
DR VEuPathDB; FungiDB:YDR264C; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; P39010; -.
DR OMA; PWMAGIF; -.
DR BioCyc; YEAST:G3O-29834-MON; -.
DR BRENDA; 2.3.1.225; 984.
DR PRO; PR:P39010; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39010; protein.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IPI:SGD.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:SGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..764
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212934"
FT TOPO_DOM 1..321
FT /note="Cytoplasmic"
FT TRANSMEM 322..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..346
FT /note="Lumenal"
FT TRANSMEM 347..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..384
FT /note="Cytoplasmic"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..418
FT /note="Lumenal"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..513
FT /note="Cytoplasmic"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..570
FT /note="Lumenal"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..764
FT /note="Cytoplasmic"
FT REPEAT 72..102
FT /note="ANK 1"
FT REPEAT 108..137
FT /note="ANK 2"
FT REPEAT 142..171
FT /note="ANK 3"
FT REPEAT 175..204
FT /note="ANK 4"
FT REPEAT 213..242
FT /note="ANK 5"
FT REPEAT 246..275
FT /note="ANK 6"
FT DOMAIN 470..520
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 500
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000305|PubMed:12370247"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 497..498
FT /note="DH->AA: Abolishes YCK2 palmitoylation."
FT /evidence="ECO:0000269|PubMed:12370247"
FT MUTAGEN 500
FT /note="C->A: Abolishes YCK2 palmitoylation."
FT /evidence="ECO:0000269|PubMed:12370247"
SQ SEQUENCE 764 AA; 85840 MW; 9C9759F0140CE3F6 CRC64;
MVNELENVPR ASTLTNEEQT VDPSNNDSQE DISLGDSNEI TSLASLKAIR SGNEEESGNE
QVNHNDEAEE DPLLTRYHTA CQRGDLATVK EMIHGKLLEV NNDGDSTEHI TGLHWASINN
RLSVVDFLVS QGADVNARAG ALHATPLHWA ARYGYVYIVD FLLKHGADPT MTDDQGFNLL
HLSVNSSNIM LVLYVLFNVV SKGLLDIDCR DPKGRTSLLW AAYQGDSLTV AELLKFGASI
KIADTEGFTP LHWGTVKGQP HVLKYLIQDG ADFFQKTDTG KDCFAIAQEM NTVYSLREAL
THSGFDYHGY PIKKWFKKSQ HAKLVTFITP FLFLGIAFAL FSHINPLFVI IVLFLLAIAT
NKGLNKFVLP SYGRMGVHNV TLLRSPLLSG VFFGTLLWVT IVWFFKVMPR TFSDEQYTNI
LMLVILVSVF YLFGQLVIMD PGCLPEETDH ENVRQTISNL LEIGKFDTKN FCIETWIRKP
LRSKFSPLNN AVVARFDHYC PWIFNDVGLK NHKAFIFFIT LMESGIFTFL ALCLEYFDEL
EDAHEDTSQK NGKCFILGAS DLCSGLIYDR FVFLILLWAL LQSIWVASLI FVQAFQICKG
MTNTEFNVLM KESKSIGPDG LSFNENFNTT PEGFAPSIDP GEESNDTVLA PVPGSTIRKP
RTCFGVCYAV TGMDQWLAVI KETIGIKDST GHNVYSITSR IPTNYGWKRN VKDFWLTSDI
NAPLWRRILY PPSGSKALLN GIEVDYFKLY KLPNKDVEQG NDMV
