ID   IZH3_ASHGO              Reviewed;         419 AA.
AC   Q75F81;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ADIPOR-like receptor IZH3;
GN   Name=IZH3; OrderedLocusNames=AAL153C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: ADIPOR-like receptor involved in zinc metabolism either by
CC       altering membrane sterol content or by directly altering cellular zinc
CC       levels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50213.1; -; Genomic_DNA.
DR   RefSeq; NP_982389.1; NM_207742.1.
DR   AlphaFoldDB; Q75F81; -.
DR   SMR; Q75F81; -.
DR   STRING; 33169.AAS50213; -.
DR   EnsemblFungi; AAS50213; AAS50213; AGOS_AAL153C.
DR   GeneID; 4618444; -.
DR   KEGG; ago:AGOS_AAL153C; -.
DR   eggNOG; KOG0748; Eukaryota.
DR   HOGENOM; CLU_655480_0_0_1; -.
DR   InParanoid; Q75F81; -.
DR   OMA; SCHPYWR; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR   InterPro; IPR004254; AdipoR/HlyIII-related.
DR   PANTHER; PTHR20855; PTHR20855; 1.
DR   Pfam; PF03006; HlyIII; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..419
FT                   /note="ADIPOR-like receptor IZH3"
FT                   /id="PRO_0000240374"
FT   TOPO_DOM        1..147
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..225
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..283
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..377
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  47153 MW;  845246B8DA874372 CRC64;
     MSHPNTHMPR THAVHGRAAP QRRGCRTSVE KTDQSGHSRS SLAESAMEQA QLRSRGEAGG
     GRSVLCASGE PGSAHKWAGA VTCSGAEEQP LHWAESRARG LARHLHYWEL PYAWRENRYI
     IYGHRFYHSH RKSLLSVLNA YGWHNETINI WSHLVGAAVL AYLLCWGWPR SDVYRAAQVP
     RLAKWAIGAF LACGVKCMAS SVAWHTFNGT CHLKLRSRFV CVDYTGITLL VTASVVTTVA
     VTLYGLSRPL MYAYMVASIG LGTAAGVMNW SPHFDRPEAR PLRIAVYVGL AALGLVSFVH
     VWMQVRWASA HLMAPLVYKS LVWYGIGVVF YATLVPERWR SDVTLDCCSG PVHEAACRQF
     RDLPPVARKD RQFWSLWWVD YFCHSHFLWH VFVVLGVVGH YRAVLQMSRI VWLDAGRAF