AKR2_YEAST
ID AKR2_YEAST Reviewed; 749 AA.
AC Q12013; D6W2A0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable palmitoyltransferase AKR2;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR2;
GN Name=AKR2; OrderedLocusNames=YOR034C; ORFNames=OR26.25;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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=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 [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
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 [6]
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).
CC -!- FUNCTION: May be involved in constitutive endocytosis of a-factor
CC receptor STE3. {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 -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 815 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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X87331; CAA60751.1; -; Genomic_DNA.
DR EMBL; Z74942; CAA99224.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10816.1; -; Genomic_DNA.
DR PIR; S62171; S62171.
DR RefSeq; NP_014677.1; NM_001183453.1.
DR AlphaFoldDB; Q12013; -.
DR SMR; Q12013; -.
DR BioGRID; 34436; 74.
DR DIP; DIP-1882N; -.
DR IntAct; Q12013; 5.
DR MINT; Q12013; -.
DR STRING; 4932.YOR034C; -.
DR iPTMnet; Q12013; -.
DR MaxQB; Q12013; -.
DR PaxDb; Q12013; -.
DR PRIDE; Q12013; -.
DR EnsemblFungi; YOR034C_mRNA; YOR034C; YOR034C.
DR GeneID; 854199; -.
DR KEGG; sce:YOR034C; -.
DR SGD; S000005560; AKR2.
DR VEuPathDB; FungiDB:YOR034C; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q12013; -.
DR OMA; GITHILH; -.
DR BioCyc; YEAST:G3O-33580-MON; -.
DR PRO; PR:Q12013; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12013; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
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:0016409; F:palmitoyltransferase activity; ISS:SGD.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; ISS: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; Glycoprotein; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..749
FT /note="Probable palmitoyltransferase AKR2"
FT /id="PRO_0000212936"
FT TOPO_DOM 1..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 49..79
FT /note="ANK 1"
FT REPEAT 83..112
FT /note="ANK 2"
FT REPEAT 117..146
FT /note="ANK 3"
FT REPEAT 150..183
FT /note="ANK 4"
FT REPEAT 189..218
FT /note="ANK 5"
FT REPEAT 222..251
FT /note="ANK 6"
FT DOMAIN 446..496
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 476
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 749 AA; 85236 MW; 887F5A02B9EE030A CRC64;
MTSMSIIDDE NVKKTSNGAA VVTDVAQHAV SDSDNNKAQL LGDGSNTEYV VDIFIEAAKD
GDLKVVKDVV ESGAVDINND RIDELSGLHW ACINNRFSVA KFLLLRGANP NQAAGPGGAT
ALHWAARYGN IYIVDLLLKH GADPTLKDEQ GLNIMHFSVY SSNILLVVYV LYFVVNNNDN
VDIDSKDNNN RTPLLWAAYQ GDFLTVELLL KFGSTVAWTD NRGFNALHCA LVGGDQRVIC
DLILSGANFY ERNNQKQDCF DLAEGMGTKS LFEQALQHHG YDRLGNQKDK LFKKSSHAQF
TIFLSPFLLM VYIYLISLVL SPVLAIMLSL LVTVVMVNTL KKFVLPCLPR KNTYKVSLTR
TPFFSGLFLS TFCFLIYIWT KKLYPYSVSD YTMKNVQFLV TSFLTVVLFL RLVRSDPGCL
KTDDSLTSIQ ETIKQLIDLG KFDRENFCVE TLERKPLRSK YSFFSGALVA RYDHYCPWIY
NDVGLKNHKL FVFFAVTVQY HMFLFMWLCL AYFKKTNYIY EQVEEYARCA LLKNETLCKG
SNYDPSTFFL FIWISVNFIW LGAMLIVQFF QILKGITTPE LFILIKEEHK AKFINLIPFE
NSIYTSESKG VEDSDMIPEG PSATTITHTI SIDGLEPRNR RRAILSACFS MMGINQWLVT
IKEIVGITHI LHGQVPQQHH SSLLRSFLVT NHWKTNLTDF WLNSDVTAPL WQRFFYSSDT
SKAMLGGTEV DYYELYEYPA REGEVLRPN
