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ALA9_ARATH
ID   ALA9_ARATH              Reviewed;        1200 AA.
AC   Q9SX33;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Putative phospholipid-transporting ATPase 9 {ECO:0000303|PubMed:11402198};
DE            Short=AtALA9 {ECO:0000303|PubMed:11402198};
DE            EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE   AltName: Full=Aminophospholipid flippase 9 {ECO:0000303|PubMed:11402198};
GN   Name=ALA9 {ECO:0000303|PubMed:11402198};
GN   OrderedLocusNames=At1g68710 {ECO:0000312|Araport:AT1G68710};
GN   ORFNames=F24J5.6 {ECO:0000312|EMBL:AAD49973.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11402198; DOI=10.1104/pp.126.2.696;
RA   Axelsen K.B., Palmgren M.G.;
RT   "Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
RL   Plant Physiol. 126:696-706(2001).
CC   -!- FUNCTION: Involved in transport of phospholipids.
CC       {ECO:0000305|PubMed:11402198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000305|PubMed:11402198};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000305}.
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DR   EMBL; AC008075; AAD49973.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34830.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58269.1; -; Genomic_DNA.
DR   PIR; F96711; F96711.
DR   RefSeq; NP_001320717.1; NM_001334377.1.
DR   RefSeq; NP_177038.1; NM_105543.6.
DR   AlphaFoldDB; Q9SX33; -.
DR   SMR; Q9SX33; -.
DR   STRING; 3702.AT1G68710.1; -.
DR   iPTMnet; Q9SX33; -.
DR   PaxDb; Q9SX33; -.
DR   PRIDE; Q9SX33; -.
DR   ProteomicsDB; 244982; -.
DR   EnsemblPlants; AT1G68710.1; AT1G68710.1; AT1G68710.
DR   EnsemblPlants; AT1G68710.2; AT1G68710.2; AT1G68710.
DR   GeneID; 843201; -.
DR   Gramene; AT1G68710.1; AT1G68710.1; AT1G68710.
DR   Gramene; AT1G68710.2; AT1G68710.2; AT1G68710.
DR   KEGG; ath:AT1G68710; -.
DR   Araport; AT1G68710; -.
DR   TAIR; locus:2026900; AT1G68710.
DR   eggNOG; KOG0206; Eukaryota.
DR   HOGENOM; CLU_000846_3_1_1; -.
DR   InParanoid; Q9SX33; -.
DR   OMA; YWEIGVQ; -.
DR   PhylomeDB; Q9SX33; -.
DR   PRO; PR:Q9SX33; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX33; baseline and differential.
DR   Genevisible; Q9SX33; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   GO; GO:1901703; P:protein localization involved in auxin polar transport; IGI:TAIR.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1200
FT                   /note="Putative phospholipid-transporting ATPase 9"
FT                   /id="PRO_0000046393"
FT   TOPO_DOM        1..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..364
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..925
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        926..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        946..959
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        960..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        980..1009
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1010..1032
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1033..1045
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1046..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1069..1074
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1075..1095
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1096..1112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1113..1137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1138..1200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        430
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         870
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         874
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1200 AA;  136045 MW;  E8CAB216E2D2B261 CRC64;
     MVGGGTKRRR RRLQLSKLYT LTCAQACFKQ DHSQIGGPGF SRVVYCNEPD SPEADSRNYS
     DNYVRTTKYT LATFLPKSLF EQFRRVANFY FLVTGVLAFT PLAPYTASSA IVPLLFVIGA
     TMVKEGVEDW RRQKQDNEVN NRKVKVHRGD GSFDAKEWKT LSIGDIVKVE KNEFFPADLV
     LLSSSYEDAI CYVETMNLDG ETNLKVKQGL EVTSSLRDEF NFKGFEAFVK CEDPNANLYS
     FVGTMELKGA KYPLSPQQLL LRDSKLRNTD FIFGAVIFTG HDTKVIQNST DPPSKRSMIE
     KKMDKIIYLM FFMVITMAFI GSVIFGVTTR DDLKDGVMKR WYLRPDSSSI FFDPKRAPVA
     AIYHFLTAVM LYSYFIPISL YVSIEIVKVL QSIFINQDIH MYYEEADKPA RARTSNLNEE
     LGQVDTILSD KTGTLTCNSM EFIKCSVAGT AYGRGVTEVE MAMGRRKGGP LVFQSDENDI
     DMEYSKEAIT EESTVKGFNF RDERIMNGNW VTETHADVIQ KFFRLLAVCH TVIPEVDEDT
     EKISYEAESP DEAAFVIAAR ELGFEFFNRT QTTISVRELD LVSGKRVERL YKVLNVLEFN
     STRKRMSVIV QEEDGKLLLL CKGADNVMFE RLSKNGREFE EETRDHVNEY ADAGLRTLIL
     AYRELDEKEY KVFNERISEA KSSVSADRES LIEEVTEKIE KDLILLGATA VEDKLQNGVP
     DCIDKLAQAG IKIWVLTGDK METAINIGFA CSLLRQDMKQ IIINLETPEI QSLEKTGEKD
     VIAKASKENV LSQIINGKTQ LKYSGGNAFA LIIDGKSLAY ALDDDIKHIF LELAVSCASV
     ICCRSSPKQK ALVTRLVKSG NGKTTLAIGD GANDVGMLQE ADIGVGISGV EGMQAVMSSD
     IAIAQFRYLE RLLLVHGHWC YRRISTMICY FFYKNITFGF TLFLYETYTT FSSTPAYNDW
     FLSLYNVFFS SLPVIALGVF DQDVSARYCL KFPLLYQEGV QNVLFSWRRI LGWMFNGFYS
     AVIIFFLCKS SLQSQAFNHD GKTPGREILG GTMYTCIVWV VNLQMALAIS YFTLIQHIVI
     WSSIVVWYFF ITVYGELPSR ISTGAYKVFV EALAPSLSYW LITLFVVVAT LMPYFIYSAL
     QMSFFPMYHG MIQWLRYEGQ CNDPEYCDIV RQRSIRPTTV GFTARLEAKK RSVRISEPAS
 
 
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