ATX9_TETTH
ID ATX9_TETTH Reviewed; 1133 AA.
AC Q95050;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable cation-transporting ATPase 9;
DE EC=7.2.2.-;
GN Name=TPA9;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CU428;
RX PubMed=9405804; DOI=10.1111/j.1749-6632.1997.tb52247.x;
RA Wang S., Gao D., Penny J., Krishna S., Takeyasu K.;
RT "P-type ATPases in Tetrahymena.";
RL Ann. N. Y. Acad. Sci. 834:158-160(1997).
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 -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; U41063; AAB08071.1; -; mRNA.
DR PIR; T30302; T30302.
DR AlphaFoldDB; Q95050; -.
DR SMR; Q95050; -.
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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1133
FT /note="Probable cation-transporting ATPase 9"
FT /id="PRO_0000046355"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 907..915
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..994
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1019..1030
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1031..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1102..1124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1125..1133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 451
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 827
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 831
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1133 AA; 129669 MW; 6875FFBD651BAD27 CRC64;
MRVSSIEAEM ENPIDVDKTD VEGELKIKQV TLLRENIVKK IVFFLVAIFC SDRPSVLKKV
FYEEVSKQEE ATHVYVLASD LTDYIEEASL KENPEEGGEK SIYFVNRLQK YIYHKKQNKF
RAIEYFIQGK SYSEIANNKP LATGRVDQLL AYYGKSEIEI NVPSFLTLMW REFKKPINFL
LYFGIIVWGI EQMYVSTAIT VVFTTTINSL ICIYIRGVMQ KLKDACLNNT SVIVQRHNGQ
GYQEITVASN MIAPGDIVLF KREVTLPFDC VILEGSCQVT EANITGENVA IGKCQIPTDH
HNDIFKYESS KSHTLFQGTQ LMKIEDDILK VIVVRTGFGS YKGQIIRALL YPKPFNKKFQ
QQAVKLTILM ATLLLIGFLS TLSRLLDIEL PPLFIAFRFL DILIYSAPPG MPMLIAITNF
VGLKRLKNNQ ILGQDPNSAS QAGRIQTLCF DKTGTLTEDK VDLIGYQLKG QNQTFDKIQC
QDPNNISIEH KLFSICHEVT KINNKLLGDL MDVKMAEFST LDIDYDHEAK QHYSKSGNKR
FYCIQVNQFH SEYQSMSVVC KEVDMITKEF KHYFFIKGSP EKIQSLSHVQ SSEKAQLSTL
INEGYRILGF GYKEIPQSEI DAFLDLSREQ QEANVQSLGF LIYKNNLKPD TQEVIKEFKE
ACYNIKVISG DNPITTLKIS QELEIVNRKN PTVIINFEET ENVKSHLIIT EIQPDNSTQV
IDFSSAQNEQ DYINKQMSYC CDAFLNNKSF CFSGKAHYYF QLKAKTDHIS FKPEWVKMQD
KSVQKIISFY QMLIINTNVF ARTQPEQKQT IVRLLKESDQ IVCMVGDGAN DCSAIREADV
GISFAEADGQ FSSSYVSLST SLSCVKRVLL EGRVNLSNSV EIFKGYLQVA LLRYLGFLTL
AYFYSSYSSG QMDWQALASG YFLVYLILGC NTPLKKLEKS VFDDNLFSIY NVTSVLFGFT
LHILSIVGCV ESLHASPIYK EVNSLDAENN FQFETQHNTV LNFNILINFF YVIISNHIGK
PMKDRYYKNT IAIYYDLGLI YTCKCMILQV LLILEHTHHG LIFLILLLDQ EFSSSLTVQV
YFSLPMNLFL PEEFSLNFTQ EVKKEKELLI CNSSSTILEV DYNLRLNYFQ QNF
