ID Q22B52_TETTS Unreviewed; 1208 AA.
AC Q22B52;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=TTHERM_01123860 {ECO:0000313|EMBL:EAR82503.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR82503.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; GG662311; EAR82503.2; -; Genomic_DNA.
DR RefSeq; XP_001030166.2; XM_001030166.2.
DR AlphaFoldDB; Q22B52; -.
DR STRING; 312017.Q22B52; -.
DR EnsemblProtists; EAR82503; EAR82503; TTHERM_01123860.
DR GeneID; 7833387; -.
DR KEGG; tet:TTHERM_01123860; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q22B52; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 115..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 936..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 992..1011
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1093..1115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 64..113
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 873..1120
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 742..779
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1208 AA; 139869 MW; 06CDD203483B716E CRC64;
MSNDDTGVQN LDDQDSKRFG YDYQYANVSK DNRSCQFFYY NQNKLKYQSE PRKITTGRPD
ECLPNNNIKT NKYTCLNFFP KNLYLQFSKL ANIYFLFIGI MQSIPQISIS NAIPVIFLPL
AVIVAITGGK DLYEDYKRMK SDRTENDQKI QIFDNKSNSF KEFTWKEIRP GHIVKVMRDH
YFPADVVLLM TSDPQGICYI ETKNLDGETN LESKQADPRI RDKCIKDESK LGQECVIIHY
ESPNKRIYRF DGSFDTKMGE NYQLSYTNVV LRGCCLKNTE YAIGMAVYTG HQSKIMYNLY
QGSAKKSTLE QLIGKLIIQI FLLQLVVCII CASIYIGFYS LVGYELSYLV IKASSDVYEE
ANAINFFVRL GNWILIFTNF VPISLIVTLE TVKFIQGMFM TADEKMGNPT VQASNLNEQL
GQINYIFSDK TGTLTKNVMQ FKQIAIGDTL YGGNEQKSEQ PLTDEEIMFN YPKVENVDFR
DRSFLDKVKD EEDPEHVKIR RVLFMLASCH TVTSTIDHQQ NTIYTASSPD EYAIINFTKF
AGVEFLKVEK VDGNTNILIR FKQKIFSLQL LHVFEFDSNR KRQSVIVKDQ DDKYFLFCKG
ADQVITMNLS ENTDPIMLRN LNEKLKYFGS QGLRTLMLAE RQIDKQAYEI WSEKYLKARS
QAENKDLEIE KLQDEMETDL EILGATAIED KLQDDVSDTI KALKDSGIKI WVLTGDKIET
AINIAYSCKL LDDTLEKAII DVEEENEVNK FLQDTLQNLL DAEATYIQQQ KQNKKAIDED
ALKNHALIIS GFALNHISKT EIKTLIMQIV KYCKCIICCR VSPKQKQEVV TTVREMEKNA
TTLAIGDGAN DVNMITAAHV GIGIKGVEGQ QAARASDYSI NQFKELRRLL FYHGRECYRR
NSNLVLYNFY KNVLLVLPQF WYGWTNWFSG QTLYNSFIYQ LFNIFFASLP IMVYAIWDEE
YSDVVLVKNE KKNYYEQGIK NKLFNQREFW KWNLIASVQA GLIVICSLFP LELNFVTQNG
QTQWFWATGT MVFGLVVVIS NLKILIMSTD HSLGSLMILA LSMLLYLITW VIVSNLNSTE
IYRTLGQMFQ TPNFHLGNIL CIIVTSFFDW AFCLYKKWTY EFDEKQQVTK IDKTPKQVKT
NSTFPIKMRT FNTDVPKKQN GFVKDQTKAN YATQEMKRTY YQDVNTGYAF NQIDRHQYVQ
KQKEQQMF
//
