ID F2YMF5_MANIN Unreviewed; 629 AA.
AC F2YMF5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=ERS1 {ECO:0000313|EMBL:ADZ76430.1};
OS Mangifera indica (Mango).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Anacardiaceae; Mangifera.
OX NCBI_TaxID=29780 {ECO:0000313|EMBL:ADZ76430.1};
RN [1] {ECO:0000313|EMBL:ADZ76430.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fruit {ECO:0000313|EMBL:ADZ76430.1};
RX PubMed=21676621; DOI=10.1016/j.plaphy.2011.05.010;
RA Ish-Shalom M., Dahan Y., Maayan I., Irihimovitch V.;
RT "Cloning and molecular characterization of an ethylene receptor gene,
RT MiERS1, expressed during mango fruitlet abscission and fruit ripening.";
RL Plant Physiol. Biochem. 49:931-936(2011).
RN [2] {ECO:0000313|EMBL:ADZ76430.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fruit {ECO:0000313|EMBL:ADZ76430.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family.
CC {ECO:0000256|ARBA:ARBA00009842}.
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DR EMBL; JF323582; ADZ76430.1; -; mRNA.
DR AlphaFoldDB; F2YMF5; -.
DR SMR; F2YMF5; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051740; F:ethylene binding; IEA:UniProt.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR24423:SF625; ETHYLENE RESPONSE SENSOR 1; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 2: Evidence at transcript level;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Ethylene signaling pathway {ECO:0000256|ARBA:ARBA00022745};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..586
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 629 AA; 70590 MW; 86A34A81F47821F0 CRC64;
MISCDCIDTQ LAQDELLVKY QYISDVLIAL AYFSIPLELI YFVKKSAFFP YRWVLMQFGA
FIILCGATHF ISLWTFSLHS KAVAVVMTVA KSSCALVSCL TALLLVYIIP DLLSVRTREL
FLKNRAEELD REMGLILTQE ETGRHVRMLT HEIRSTLDRD TILRTTLVEL GRTLGLEECA
LWMPSRTGIT LELSHTLNHQ IQVGSTVPRN LPIINDIFGT ARATFLPYNC PLAGTRPVVG
RHRPYEGVAV RVPLLHYSNF QISDWPEFSA KSYAVMVLIL PTDSGRKWRD HELELVEVVA
DQVAVALSHA AILEQSMRAR DQLLQQNVAL DLARQEAEKA IHARNDFRAV MNHEMRTQMH
AVIALSSLLL ETELSPDQRA MIETVLKSSN LLTTLVDDVL DLSRLEDGSL ELEIGPFNLH
EVFREVINLI KPIASIKKLS MNINMAPDLP TYLIGDKKRL MQTILNIVGN AVKFTKEGYV
LIKASVANPE SSRDWRPEFH PASCNGHFYL RVQVTDSGCG ILPQDIPFVF TRFVQSRSGS
NRSTGGAGLR LAISRRFVNL MGGHIWIESE GLDKGSTVTF LVQLGICTTH QAVPKGRVNH
GSADLSGHKQ VFRDTDEVAL SKTRYQRSL
//
