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AATP3_ARATH
ID   AATP3_ARATH             Reviewed;         495 AA.
AC   Q8GW96; Q683K1; Q9SI12;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=AAA-ATPase At2g18193;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN   OrderedLocusNames=At2g18193 {ECO:0000312|EMBL:AEC06737.1};
GN   ORFNames=F8D23 {ECO:0000305};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:BAC43568.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD31347.1; Type=Erroneous gene model prediction; Note=The predicted gene At2g18190 has been split into 2 genes: At2g18190 and At2g18193.; Evidence={ECO:0000305};
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DR   EMBL; AC007212; AAD31347.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06737.1; -; Genomic_DNA.
DR   EMBL; AK118992; BAC43568.1; -; mRNA.
DR   EMBL; AK175116; BAD42879.1; -; mRNA.
DR   EMBL; AK175187; BAD42950.1; -; mRNA.
DR   EMBL; AK175325; BAD43088.1; -; mRNA.
DR   EMBL; AK176580; BAD44343.1; -; mRNA.
DR   EMBL; BT026385; ABH04492.1; -; mRNA.
DR   PIR; D84561; D84561.
DR   RefSeq; NP_849972.1; NM_179641.2.
DR   AlphaFoldDB; Q8GW96; -.
DR   SMR; Q8GW96; -.
DR   STRING; 3702.AT2G18193.1; -.
DR   SwissPalm; Q8GW96; -.
DR   PaxDb; Q8GW96; -.
DR   PRIDE; Q8GW96; -.
DR   ProteomicsDB; 244584; -.
DR   EnsemblPlants; AT2G18193.1; AT2G18193.1; AT2G18193.
DR   GeneID; 816333; -.
DR   Gramene; AT2G18193.1; AT2G18193.1; AT2G18193.
DR   KEGG; ath:AT2G18193; -.
DR   Araport; AT2G18193; -.
DR   TAIR; locus:1005716649; AT2G18193.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_010189_0_1_1; -.
DR   InParanoid; Q8GW96; -.
DR   OMA; RNVNART; -.
DR   OrthoDB; 532729at2759; -.
DR   PhylomeDB; Q8GW96; -.
DR   PRO; PR:Q8GW96; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8GW96; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025753; AAA_N_dom.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF14363; AAA_assoc; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="AAA-ATPase At2g18193"
FT                   /id="PRO_0000434705"
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          451..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..488
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         250..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        219
FT                   /note="K -> R (in Ref. 4; BAD42879)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  56469 MW;  0C2D721D84E14A57 CRC64;
     MFPSSDFSFS PSSLFSAYAS LTGFLMLFRS MLHDFVPEKL RSYFSSLLDR FFTPKSKYLT
     VIIDENFGLN RNQVFDAAEM YLRSKIGPET ERLRVGKIPK QKHFTISIER GEEILDTFEE
     SEVKWSYVQS ENEKGDKVKR YYELTFEKKL RDKVLNSYLT HVVAESEEIK RNLRVVKLYS
     RDVYASDDDD GMAGGNWGCI NLEHPSTFDT LAMDPNAKKK IIDDLERFLK RKEFYKRVGK
     AWKRGYLLYG PPGTGKSSLI AAMANYLKFD VFDLELSSIY DNGELKRVLL STTNRSILVI
     EDIDCNAEVR DREAENQEDE QIKGKVTLSG ILNFIDGLWS SFGDERIIVF TTNHKERLDP
     ALLRPGRMDV HINMSYCTGL GFRTLVSNYL GLDGLNHPLC EEIEALVDST EVTPAELAEE
     LMQDDDTDVV LRGVISFVEK RKVERSKTKK EVSICKATDD DEKQNGSLGC VKKKKKGGKQ
     KGKGKGKGKA KTYLI
 
 
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