PMA1_DICDI
ID PMA1_DICDI Reviewed; 1058 AA.
AC P54679; Q54RX4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable plasma membrane ATPase;
DE Short=PAT2 {ECO:0000303|PubMed:9421912};
DE EC=7.1.2.1 {ECO:0000269|PubMed:9421912};
DE AltName: Full=P-type H(+)-ATPase {ECO:0000303|PubMed:9421912};
DE AltName: Full=Proton pump;
GN Name=patB; ORFNames=DDB_G0282817;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=9421912; DOI=10.1099/00221287-143-12-3877;
RA Coukell M.B., Moniakis J., Cameron A.M.;
RT "The patB gene of Dictyostelium discoideum encodes a P-type H(+)-ATPase
RT isoform essential for growth and development under acidic conditions.";
RL Microbiology 143:3877-3888(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: P-type plasma membrane H+-ATPase (proton pump)
CC (PubMed:9421912). The proton gradient it generates drives the active
CC transport of nutrients by H(+) symport (PubMed:9421912). The resulting
CC external acidification and/or internal alkinization may mediate growth
CC responses (PubMed:9421912). {ECO:0000269|PubMed:9421912,
CC ECO:0000303|PubMed:9421912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC Evidence={ECO:0000269|PubMed:9421912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853;
CC Evidence={ECO:0000269|PubMed:9421912};
CC -!- ACTIVITY REGULATION: Acid pH levels increase its ATPase activity.
CC {ECO:0000269|PubMed:9421912}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9421912}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66931.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X98286; CAA66931.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000047; EAL65988.1; -; Genomic_DNA.
DR PIR; T30580; T30580.
DR RefSeq; XP_639363.1; XM_634271.1.
DR AlphaFoldDB; P54679; -.
DR SMR; P54679; -.
DR STRING; 44689.DDB0214946; -.
DR PaxDb; P54679; -.
DR EnsemblProtists; EAL65988; EAL65988; DDB_G0282817.
DR GeneID; 8623803; -.
DR KEGG; ddi:DDB_G0282817; -.
DR dictyBase; DDB_G0282817; patB.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; P54679; -.
DR OMA; GVDINWM; -.
DR PhylomeDB; P54679; -.
DR PRO; PR:P54679; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IDA:dictyBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1058
FT /note="Probable plasma membrane ATPase"
FT /id="PRO_0000046295"
FT TOPO_DOM 1..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..810
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..889
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..967
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1058
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 480
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 728
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 732
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1058 AA; 117268 MW; 12D39896E92F3A9F CRC64;
MDNNQIPKNS PESSAINSAE SSPKSNVSSD VLHENHHKEQ QQLQQQLQQE QQQQQLPTTP
QSEPTQRVNN NEEGIEMDRI AENSNINVPS DVGESSLKTI SGYPSSKNTE AGSSSSGKKE
EDYNYRSTWV PKLHQELFEN PEVLESRRTK QRASNYRKTL EREKEGIKPL DNILEELKAN
ANGLTKAEAQ KRLEEVGPNA IPDVKRYPIL EFLYFMWNPL SWTMEVAAIV SIALLDWVDF
ILICALLLLN ATIGFIEENT AGNAVEALKN SLVSQIRCMR DGEWVMLPSP DLVPGDVVML
KIGAIIPADC RVIEAEQVKI DQSSLTGESL PVTKKIGDEV YSGSAMKQGE AKCVVTATGV
NTFFGRAANL VQETEGHGHL QVILRNIGLF CISFIAIWVL VELLVDFLGY DGYCHGVGGG
RCLPLNNALV LLVGGIPIAM PTVLSVTMAI GATQLSKKKA IVSRLASIEE LAAMDILCSD
KTGTLTLNIL TVDEPLPVGD TPKEDIVFHA FLACSEGEDQ DAIDKAISNY CRDTYPNVDY
SGNEIVKHYP FNPEDKKAMG LVNANGKQFK TAKGAPQIIL READNYKQVG EAVEKEIENL
ADRGYRALGV SVSYDAPDFK VWHFEGLIPL FDPPRHDTED TIKRALEMGV SVKMITGDQL
AIAKETARRL GMGGNLFTIP YLENNDLGIS EGEVIEMADG FAEMWPEHKY KVVDQLQKRK
HVVGMTGDGV NDAPALKKAQ IGIAVAGATD AARSVSDIVL TSSGLSVIID AIISSRKIFQ
RMRNYVIYSV AATVRICTTF GILTVAWNFK FPTIATVIIA ILNDGTMLTI SKDRVRARNE
PDQWNLFEVF TMALCYGFYL VGSTIVFFAI IHDGTWFHDA INLRILTDNE LRGLIYLQVS
ISGLATIFVS RSQGFSYFER PGNLVIFAFV MSQIVATFIG VYGFRGYPHD SFSDNPDYPV
HGTNFQGCGW GWAVCAWIWC FLWYIPMDFI KLGVTYILRG KIEPINKDAL RKIYGWFGKE
IPKEATQVSH KVAEQQAKRD ALHAQETHHK SVVTDNKV
