IZH2_YEAST
ID IZH2_YEAST Reviewed; 317 AA.
AC Q12442; D6W265;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ADIPOR-like receptor IZH2;
DE AltName: Full=Phosphate metabolism protein 36;
GN Name=IZH2; Synonyms=PHO36; OrderedLocusNames=YOL002C; ORFNames=UND327;
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].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
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 [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 INDUCTION.
RX PubMed=9774671; DOI=10.1128/mcb.18.11.6560;
RA Karpichev I.V., Small G.M.;
RT "Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription
RT factors that regulate genes encoding peroxisomal proteins in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 18:6560-6570(1998).
RN [5]
RP FUNCTION, AND IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=11916977; DOI=10.1074/jbc.m202045200;
RA Karpichev I.V., Cornivelli L., Small G.M.;
RT "Multiple regulatory roles of a novel Saccharomyces cerevisiae protein,
RT encoded by YOL002c, in lipid and phosphate metabolism.";
RL J. Biol. Chem. 277:19609-19617(2002).
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: Probable receptor, which is involved in metabolic pathways
CC that regulate lipid metabolism such as fatty acid oxidation.
CC {ECO:0000269|PubMed:11916977}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Regulated by OAF1 and PIP2. Highly expressed in presence of
CC glucose. Expressed at lower level in presence of glycerol or glycerol
CC and oleate. Highly expressed in the presence of saturated fatty-acids
CC such as myristate. {ECO:0000269|PubMed:9774671}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99001.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U43491; AAC49478.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74744; CAA99001.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10781.1; -; Genomic_DNA.
DR PIR; S61982; S61982.
DR RefSeq; NP_014641.2; NM_001183256.1.
DR AlphaFoldDB; Q12442; -.
DR SMR; Q12442; -.
DR BioGRID; 34402; 308.
DR DIP; DIP-5616N; -.
DR IntAct; Q12442; 1.
DR STRING; 4932.YOL002C; -.
DR iPTMnet; Q12442; -.
DR MaxQB; Q12442; -.
DR PaxDb; Q12442; -.
DR PRIDE; Q12442; -.
DR EnsemblFungi; YOL002C_mRNA; YOL002C; YOL002C.
DR GeneID; 854160; -.
DR KEGG; sce:YOL002C; -.
DR SGD; S000005362; IZH2.
DR VEuPathDB; FungiDB:YOL002C; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000170813; -.
DR HOGENOM; CLU_023075_2_0_1; -.
DR InParanoid; Q12442; -.
DR OMA; DYCGIAM; -.
DR BioCyc; YEAST:G3O-33419-MON; -.
DR PRO; PR:Q12442; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12442; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0009636; P:response to toxic substance; IMP:SGD.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="ADIPOR-like receptor IZH2"
FT /id="PRO_0000218834"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 36279 MW; 2782FD18751249B0 CRC64;
MSTLLERTKS VQELKKRAAG KTSANPAEVA KAKKVLRRLY SWDEIPEWQR DNDFILHGYV
KETSSFIETF KSLFYLHNES VNIYSHLIPA LGFFTVLLLD KSTIKVFATT TWLDHMVIDL
FYSGAFACLI LSSSFHCLKS HSLRIATLGN KLDYLGICIL IVTSMVSILY YGYFEKFSLF
CLFALITVSF GIACSIVSLK DKFRKREWRP YRAGLFVCFG LSSIIPIFSG LYCYSFSEIW
TQIQLFWVLL GGVLYIIGAV LYGMRFPEKI CPGKFDIWGH SHQLFHFLVV IAALCHLRGL
LNSYELVHIK MENGIVS
