ID A0A090LP99_STRRB Unreviewed; 1976 AA.
AC A0A090LP99;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=SRAE_X000091000 {ECO:0000313|EMBL:CEF71586.1,
GN ECO:0000313|WBParaSite:SRAE_X000091000.1,
GN ECO:0000313|WormBase:SRAE_X000091000};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF71586.1};
RN [1] {ECO:0000313|EMBL:CEF71586.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_X000091000.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF71586.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_X000091000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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 Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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DR EMBL; LN609530; CEF71586.1; -; Genomic_DNA.
DR STRING; 34506.A0A090LP99; -.
DR EnsemblMetazoa; SRAE_X000091000.1; SRAE_X000091000.1; WBGene00266472.
DR WBParaSite; SRAE_X000091000.1; SRAE_X000091000.1; WBGene00266472.
DR WormBase; SRAE_X000091000; SRP02974; WBGene00266472; -.
DR eggNOG; KOG0208; Eukaryota.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd18987; LGIC_ECD_anion; 1.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF12409; P5-ATPase; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362082};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 389..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 915..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 943..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 979..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1033..1052
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1064..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1104..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1831..1849
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1887..1909
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1947..1966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 30..132
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 159..210
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 940..1121
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT DOMAIN 1621..1795
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT COILED 1909..1936
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1976 AA; 227221 MW; BB023825AE8A9739 CRC64;
MVKIKNSDLN SGVPYPDNHS ANFANGESLL TFYGYKIDKK RKFIYYIFSI ITLGFLPLFC
YWYPQIKTYL ISKKCKISNA DQILIEENKN YSVKNVKIIQ SDIPFEIPFK DTILKVKELQ
TFSYRKINFI WHEKEKTYVS VASLCDNVYI KKFHNILELN SGLDDSTVES IEKLYGKNVI
EVKVTPLFLI AFKEFLSPFY IFQVFSVAIW FSDEYVLYAS IIVFISIISI FTESWSIQKE
QKKLADMVHN ETTVEVIRNN GKIITLNSSD LVPGDLFVVP KYDYTLQCDA ILISGSCIIN
ESMLTGESVP ETKVPLPEDD DENNPIKYNG DIHGKHSLYC GTTIIQTRYN ANSPAKAIVL
RTGFTTLKGN LVRSIMYPKP IDYTFTKDLL KFVCFLLCVA LLGFTYTIIL MILRGSTPSK
IIIRSLDIIT VVVPPALPAA MTIGMISAAQ RLKKSKIHCI SQETINTCGM ITCCCFDKTG
TLTEDGLAFN GVRPVFIDHI KNNKPYFGEK TTEYVKGKIP INSRLIRAVA TCHSITKING
EYVGDPVDVL NFNVTGFDFK ETFDDNTVKE KTRFDMLQPN TYSGILETKN GPKNVTLAVL
RTLPFSSALQ RMGVIVHDDE DEETEIHFYT KGSPEIISSL CIPESIPNDF TDIVKEYTKK
GYRLIAVAYK DLSHVNFTKA LKISRNEIEN NLKMLGIIVM ENKIKPQSLP VIDELNKAGI
RTLMITGDNI LTAISVAREC HILNKEKICF TVDIIPNEKT INGKTKIVLN QNSFDEKMLI
SEERLSQHLK DIYNKKKSSP ISYQLAISGP VFNVICNEYP ELLPKIICTC NVFARMTPDQ
KQFLIHSLID QSYYVMMCGD GANDCGALKA AHAGISLSTA EASIAAPFTS NINNISCVPR
TIREGRAALV TSFGIFKYMA GYSLTQFVSI MLLYWINTNL TDFQFIFIDL GLITFCAIVF
GYTPASLTID KKPPPNRLLS LASIMSVVGQ LTIVGIFQFI AFIWVSKQSW FIPFTKPVTH
DDDEDKRSMQ GTAIFNVSVF QYIALAICYS KGAPYRQSIV KNKFLCILLI IQIGIGLFLG
LQGIPEFSNL IDIEIIPYIA DRLFIFGIAF ISVTCMFLYE KFIVEHLILN IRDRKIKKNQ
VKNGTSKKSY EKILSKIGNN IEWFENDMYN NKNSSIDMTS ISEYDINSLA SSHGKQIYVH
SMTKNDLNYV KKDEQLSQIL TEYSNRNIVN NLETSNKDNI LIKNKKKDYM IISEYHQSPI
EGNFDSTTTI EPLTIFYKQA SSKKEHKYNV ENNFDKLDVS SKSSINEINN GKVILTNDYF
TFTTEKTITT ISKPFIKNNL QPNKILLFKK NENNNLNKNR IKLLTNNKDI QFPTWNFKKI
SAKIEKTSKS NFYNNNNIVL EKNYESYVKN DLNSNKNVYN NLSYNKNFNK KDNNFFRYLN
VKIENMRNDI KNYSNEDSSK EINIKNEEKK INNKNIEDVN NSNNIKDIEK DNENNLKTNA
IEIVFDDEEE DDVLTKLFNS KEEKNLSYSM ENASIGEHIT IEEVQYDEND IQKDIQSEDE
YDNDFLKEGE HFDYNETMLT EFINDNLKRD DNTLRTILVD KMLLEKDIPD NTGDYSGSHI
YPTLISQNYN NNSLPIMFSD IPVYVMVSLD IFDISSFNMQ SMDYSVDLLI NMRWYDMRLI
HKMNKPITVC EERILEKIWR PDPYIVNAKK SYLHKITFPN IKMRIFPDGL VLYTIHITIQ
STCNMKFCMF PHDQQECYLD LSSLSYSDRQ LKFIWSDEPY FLVNPSTLPE FKIINITVNE
CLSHDKLITS SCLRLAFKLR RDSAKYIVEK YIPSTLAMMF AWVAPYVPYN YEDVRIVTPI
TILLALVQMQ KGEVETRTSY LTSLDKWFAV MKVFSVISLM ESLVVLSLVR KFRELKKKEN
KAINEFEKEM IKLQQRQVKK LYNTIDLYAR IISPVVFILY LIYYLLFMVT GNEENC
//
