ALA11_ARATH
ID ALA11_ARATH Reviewed; 1203 AA.
AC Q9SAF5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Probable phospholipid-transporting ATPase 11 {ECO:0000303|PubMed:11402198};
DE Short=AtALA11 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 11 {ECO:0000303|PubMed:11402198};
GN Name=ALA11 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g13210 {ECO:0000312|Araport:AT1G13210};
GN ORFNames=F3F19.24 {ECO:0000312|EMBL:AAD31074.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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; AC007357; AAD31074.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28985.1; -; Genomic_DNA.
DR EMBL; AY099862; AAM20713.1; -; mRNA.
DR PIR; F86266; F86266.
DR RefSeq; NP_172780.1; NM_101192.3.
DR AlphaFoldDB; Q9SAF5; -.
DR SMR; Q9SAF5; -.
DR BioGRID; 23121; 2.
DR STRING; 3702.AT1G13210.1; -.
DR iPTMnet; Q9SAF5; -.
DR PaxDb; Q9SAF5; -.
DR PRIDE; Q9SAF5; -.
DR ProteomicsDB; 245044; -.
DR EnsemblPlants; AT1G13210.1; AT1G13210.1; AT1G13210.
DR GeneID; 837881; -.
DR Gramene; AT1G13210.1; AT1G13210.1; AT1G13210.
DR KEGG; ath:AT1G13210; -.
DR Araport; AT1G13210; -.
DR TAIR; locus:2031860; AT1G13210.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9SAF5; -.
DR OMA; CVKENER; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9SAF5; -.
DR BioCyc; ARA:AT1G13210-MON; -.
DR PRO; PR:Q9SAF5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAF5; baseline and differential.
DR Genevisible; Q9SAF5; 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 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1203
FT /note="Probable phospholipid-transporting ATPase 11"
FT /id="PRO_0000046395"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..955
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1041
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1064
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1065..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1092..1108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1134..1203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 429
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 866
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 870
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1203 AA; 136584 MW; D06ED2FBA046FC6E CRC64;
MTKCRRRRLH LSNIYAFKGR KSNFQEDHSH IGGPGFSRVV YCNEPNSPAA ERRNYVGNYV
RSTKYTLASF IPKSLFEQFR RVANFYFLVT GVLSLTALSP YSPISALLPL TFVIAASMVK
EAIEDWGRKK QDIEMNNRKV KVHDGNGIFR REGWRDLKVG NIVRVEKDEF FPADLLLLSS
SYEDSICYVE TMNLDGETNL KVKQGLEATS SALHEDSDFK ELKAVVKCED PNADLYTFVG
TLHFEEQRLP LSITQLLLRD SKLRNTEYIY GVVVFTGHDT KVIQNSTDPP SKRSRIERKM
DKIIYLMFGV VFLMSFIGSI VFGIETREDR VRNGGRTERW YLRPDNADIF FDPDRAPMAA
VYHFFTAVML YSYFIPISLY VSIEIVKVLQ SLFINNDILM YYEENDKPAH ARTSNLNEEL
GMVDTILSDK TGTLTCNSME FIKCSIAGTA YGRGITEVER SMAMRSNGSS LVGDDLDVVV
DQSGPKIKGF NFLDERVMKG NWVKQRDAAV LQKFFRLLAV CHTAIPETDE ATGSVSYEAE
SPDEAAFVVA AREFGFEFFS RTQNGISFRE LDLASGKTVE RVYRLLNVLE FNSARKRMSV
IVRDEDGRLL LLSKGADNVM FERLAKNGRK FEEKTREHVN EYADAGLRTL ILAYREVDEN
EYIEFSKNFN EAKNSVTADR ESLIDEITEQ MERDLILLGA TAVEDKLQNG VPDCIDKLAQ
AGIKIWVLTG DKMETAINIG FACSLLRQEM KQIIINLETP HIKALEKAGE KDAIEHASRE
SVVNQMEEGK ALLTASSSAS SHEAFALIID GKSLTYALED DFKKKFLDLA TGCASVICCR
SSPKQKALVT RLVKSGTGKT TLAIGDGAND VGMLQEADIG VGISGVEGMQ AVMSSDIAIA
QFRYLERLLL VHGHWCYSRI SSMICYFFYK NITFGVTVFL YEAYTSFSAQ PAYNDWFLSL
FNVFFSSLPV IALGVFDQDV SARYCYKFPL LYQEGVQNLL FSWKRIIGWM FNGVFTALAI
FFLCKESLKH QLYNPNGKTA GREILGGTMY TCVVWVVNLQ MALAISYFTW LQHIVIWGSV
AFWYIFLMIY GAITPSFSTD AYKVFIEALA PAPSYWLTTL FVMFFALIPF FVFKSVQMRF
FPGYHQMIQW IRYEGHSNDP EFVEMVRQRS IRPTTVGFTA RRAASVRRSG RFHDQLNKNF
IAF
