ID A0A1S2ZCZ6_ERIEU Unreviewed; 1256 AA.
AC A0A1S2ZCZ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=ATP13A3 {ECO:0000313|RefSeq:XP_007517481.2};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007517481.2};
RN [1] {ECO:0000313|RefSeq:XP_007517481.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_007517481.2; XM_007517419.2.
DR AlphaFoldDB; A0A1S2ZCZ6; -.
DR CTD; 79572; -.
DR eggNOG; KOG0208; Eukaryota.
DR InParanoid; A0A1S2ZCZ6; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000079721; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-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:SF12; POLYAMINE-TRANSPORTING ATPASE 13A3; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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, ECO:0000256|RuleBase:RU362082};
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:UP000079721};
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}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 936..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 966..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1001..1028
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1074..1092
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1104..1124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1144..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 13..150
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 176..226
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
SQ SEQUENCE 1256 AA; 141769 MW; 384A05AED34C7972 CRC64;
MDKEERKTIN QGQEDEMEVY GYNLSRWKLA IVCLGVLCSG GFLLLILYWL PEWRVKATCI
RAAVKDCEVV LLRTSDEFRM WFCAKIRFLS LGAQPISSLK SVTNKVSNGH AVHLSENLAE
ENKHEMNKYS HTQSQQIRYF THHSIKYFWN DALHNFDFLK GLDEGVSCTS IYEKHSAGLT
KGMHAYRKLL YGVNEITVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVI
MSVVSIVTSL YSIRKQYVML HDMVAAHSTV RVSVCRLNEE IEEIFSTDLV PGDVMVIPLN
GTVMPCDAVL ISGTCIVNES MLTGESVPVT KTNLPNPSVD IKGMGDELYS PEIHKRHTLF
CGTTVIQTRF YTGELVKAVV VRTGFSTSKG QLVRSILYPK PTDFKLYRDA YLFLLCLVAV
AGIGFIYTIV NSVLHQVEAG SIIIESLDII TITVPPALPA AMTAGIVYAQ RRLKKVGIFC
ISPQRINICG QLNLVCFDKT GTLTEDGLDL WGIQRVENAR YLLPEESVCN EMLVKSQFVA
CMATCHSLTK IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPD
STPAGNQEME LFELPAIYEI GIVRQFPFSS ALQRMSVVAR VLGDKKMDAY MKGAPEIIAN
LCKPETVPVD FETVLEDYTK QGFRVIALAH RKLESKLTWH KVQNISRDAI ENNMDFMGLI
IMQNKLKQET PAVLEDLHKA NIRTVMVTGD NMLTAISVAR DCGMILPHDK VIIAEALPPK
DGKVATINWH YADTLTQCSN SSAIGSEAIP IKLADDSLED LQMSRYHFAM NGKSFSVILE
HFQDLVPKLM LHGTVFARMA PDQKTQLVEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL
SELEASVASP FTSKTPSISC VPNLIREGRA ALMTSFCVFK FMALYSIIQY FSVTLLYSIL
SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG LISGALLFSV LSQIVICIGF
QSFGFFWVKQ QPWYEVWHPH SDACNTTGSL YWNSSYLYNE TELDERNIQN YENTTVFFIS
CFQYLIVAIA FSKGKPFRQP CYKNYFFVVS VIILYVFTLF IMLYPVASVD QVLQIVCVPY
QWRITMLIII LVNALVAIMV ENFFLDMVLW KVVFNRDKQG EYRFTTTQPP QESLNWWGKY
CLSWAQGCRK KIPKAKYMYL AQELLVDPEW PPKPQTTTEA KTLVKENGSC QIITIT
//
