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ETR1_SOLLC
ID   ETR1_SOLLC              Reviewed;         754 AA.
AC   Q41342; O49186;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Ethylene receptor 1;
DE            Short=LeETR1;
DE            EC=2.7.13.3;
GN   Name=ETR1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rutgers; TISSUE=Abscission zone, and Fruit;
RX   PubMed=8704141; DOI=10.1007/bf00019564;
RA   Zhou D., Kalaitzis P., Mattoo A.K., Tucker M.L.;
RT   "The mRNA for an ETR1 homologue in tomato is constitutively expressed in
RT   vegetative and reproductive tissues.";
RL   Plant Mol. Biol. 30:1331-1338(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rutgers; TISSUE=Root;
RX   PubMed=9721682; DOI=10.1046/j.1365-313x.1998.00202.x;
RA   Lashbrook C.C., Tieman D.M., Klee H.J.;
RT   "Differential regulation of the tomato ETR gene family throughout plant
RT   development.";
RL   Plant J. 15:243-252(1998).
CC   -!- FUNCTION: May act early in the ethylene signal transduction pathway,
CC       possibly as an ethylene receptor, or as a regulator of the pathway.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per dimer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q41342; B6GVA2: int106; NbExp=2; IntAct=EBI-2407792, EBI-2407896;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Leaves, flowers and fruits.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages.
CC   -!- INDUCTION: Constitutively expressed and accumulation not affected by
CC       ethylene, silver ions or auxin.
CC   -!- PTM: Activation probably requires a transfer of a phosphate group
CC       between a His in the transmitter domain and an Asp of the receiver
CC       domain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR   EMBL; U41103; AAA85479.1; -; mRNA.
DR   EMBL; AF043084; AAC02213.1; -; mRNA.
DR   PIR; S71783; S71783.
DR   PIR; T52288; T52288.
DR   RefSeq; NP_001234149.1; NM_001247220.2.
DR   AlphaFoldDB; Q41342; -.
DR   SMR; Q41342; -.
DR   BioGRID; 2310725; 1.
DR   IntAct; Q41342; 2.
DR   STRING; 4081.Solyc12g011330.2.1; -.
DR   PaxDb; Q41342; -.
DR   GeneID; 606298; -.
DR   KEGG; sly:606298; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   InParanoid; Q41342; -.
DR   OrthoDB; 199912at2759; -.
DR   BRENDA; 2.7.13.3; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q41342; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051740; F:ethylene binding; IEA:InterPro.
DR   GO; GO:0038199; F:ethylene receptor activity; IEA:InterPro.
DR   GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR014525; ETR.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Copper; Disulfide bond; Endoplasmic reticulum;
KW   Ethylene signaling pathway; Kinase; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..754
FT                   /note="Ethylene receptor 1"
FT                   /id="PRO_0000081416"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          173..321
FT                   /note="GAF"
FT   DOMAIN          364..601
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          629..746
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         80
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         367
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         677
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DISULFID        18
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        20
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        105
FT                   /note="P -> A (in Ref. 2; AAC02213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   754 AA;  84202 MW;  D7443B6517781D0A CRC64;
     MGSLLRMNRL LSSIVESCNC IIDPQLPADD LLMKYQYISD FFIALAYFSI PVELIYFVKK
     SAVFPYRWVL VQFGAFIVLC GATHLINLWT FNMHTRNVAI VMTTPKALTA LVSCITALML
     VHIIPDLLSV KTRELFLKKK AAQLDREMGI IRTQEETGRH VRMLTHEIRS TLDRHTILKT
     TLVELGRTLA LEECALWMPT RTGLELQLSY TLRHQNPVGL TVPIQLPVIN QVFGTNHVVK
     ISPNSPVARL RPAGKYMPGE VVAVRVPLLH LSNFQINDWP ELSTKRYALM VLMLPSDSAR
     QWHVHELELV EVVADQVAVA LSHAAILEES MRARDLLMEQ NVALDLARRE AEMAVRARND
     FLAVMNHEMR TPMHAIIALS SLLQETDLTP EQRLMVETIL KSSNLLATLI NDVLDLSRLE
     DGSLQLDIGT FNLHALFREV HSLIKPIASV KKLFVTLSLS SDLPEYVIGD EKRLMQILLN
     VVGNAVKFSK EGNVSISAFV AKSDSLRDPR APEFFAVPSE NHFYLRVQIK DTGIGITPQD
     IPNLFSKFTQ SQALATTNSG GTGLGLAICK RFVNLMEGHI WIESEGLGKG STAIFIIKLG
     IPGRANESKL PFVTKLPANH TQMSFQGLKV LVMDENGVSR MVTKGLLTHL GCDVTTVGSR
     DECLRVVTHE HKVVIMDVSM QGIDCYEVAV VIHERFGKRH GRPLIVALTG NTDRVTKENC
     MRVGMDGVIL KPVSVYKMRS VLSELLEHGV VLES
 
 
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