ID A0A1I8IS23_9PLAT Unreviewed; 1003 AA.
AC A0A1I8IS23;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cation-transporting ATPase {ECO:0000313|WBParaSite:maker-uti_cns_0016207-snap-gene-0.3-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0016207-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0016207-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR AlphaFoldDB; A0A1I8IS23; -.
DR WBParaSite; maker-uti_cns_0016207-snap-gene-0.3-mRNA-1; maker-uti_cns_0016207-snap-gene-0.3-mRNA-1; maker-uti_cns_0016207-snap-gene-0.3.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis 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 CDD; cd07543; P-type_ATPase_cation; 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; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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; 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|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 693..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 111191 MW; 7CE86F732C3BCEF3 CRC64;
METESELQQA VHQFGTNNME MVPPKFSELF IERATAPFFV FQVFCVGLWC LDDYWYYSLF
TLGMLVVFEC TLVQQQLRNM AEIRQMGNKP YPIYTLRNKK WNLLDSTGTR DLVSLGRSEK
ERLIPCDLLL LRGQCIVDES MLTGESVPVT KEPAESILDD RSLCLDTDAK HHVLSGGTKV
VQHTPPQKVG AGTKSPDNGC ICYVLRNGFQ TSQGRLLKTI LFGVKRVTAN NLETFLFISF
LLVFALAASA YVWLEGTKDP KRSRYKLFLE CTLIITSVVP PELPIELSLA VQNSLVALHR
LFIYCTEPFR IPFAGKVDIC CFDKTGTLTR DEMVVDGVAG LDSDNPNEIQ TVQNCGQATV
QVMAACHSLV IMDKTNDLLG DPLEKAILKA TGWTLTKGEA VIPPSASRAQ HHPLKVFVRF
HFSSSLQRMA TVAGHTPLGS TDTHYMVCAK GAPERLKEML IDPPPFYDKV SNQLAKDGFR
VLALAYRQLG TLNHQDLRAL KRADVERDLT FCGFLAVSCP LRSTSKSVVR ELLSSSHHVC
MITGDNPYTA CHVAKQLKIA RQPLLSLSQT GQDWSWTGID NDSDCLELDL KLAANKPKRI
VAELLKQHSI CLTGEALDYL RLSTPKLLPL LLPAVSVFAR MKPKQKELIV TVLKDRGYAT
LMCGDGTNDV GALKHAHVGV AIFANAPETL PSSAAAKTEP APAAAPARRQ PEPQPAPRDR
AEAQRQRLEK AQRDLNEMLK EADAPLVRPG DATIAAPFSY KLASVTCVCN IVKQGRCTLV
TTLQMFKILA INALIYAYSQ SVLYLDGVKF SDGQATLQGL VLAACFLFIS RSKPLTTLSA
RRPLPNIFNA YTLLTVFLQF VIHFASLIFL TREAKALMPQ LKEGEFVDLE AEFKPNILNS
VVYLISISMQ INAFAVNYKG HPFMESLMEN KPLLYSITTA TGLVFSLASG YMPELCEQFS
LVEIDNNLRN TIVQVLAADF VGCFVVDRLC DLIFGRGRAK RLV
//
