ID A0A3Q0GIH9_ALLSI Unreviewed; 1212 AA.
AC A0A3Q0GIH9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=ATP13A2 {ECO:0000313|RefSeq:XP_025059474.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025059474.1};
RN [1] {ECO:0000313|RefSeq:XP_025059474.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025059474.1; XM_025203689.1.
DR AlphaFoldDB; A0A3Q0GIH9; -.
DR Proteomes; UP000189705; 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; 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; 3.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF2; POLYAMINE-TRANSPORTING ATPASE 13A2; 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; 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, 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:UP000189705};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 249..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 478..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 956..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 981..998
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1019..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1068..1089
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1101..1120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1140..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 47..188
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 213..264
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
SQ SEQUENCE 1212 AA; 134011 MW; A7B5C6AB9F22EE61 CRC64;
MDGSSQATEG EGNCLGVIII ALVFYSSRLM RNQQPGYGAL LQVPDKSCME VSGYQSRTWK
VVLCHLFSVL TAGLLLIVFH WKPSLEVRAK CRPCPLSQAD WVIIQDGFGQ CFTTRVQTEE
IGDGREAGLL RYGQSLEQHP GTRPDDGRAS VAVGVTDEDD GRDTIQLHKK EEKNILRYYL
FEGSRYVWLE RQQAYCKVSI LDEGWTCADI RLSQAGLTQQ DHNTKRKIYG PNLIDVPVKS
YLRLLVDEVL NPFYIFQIFS IVLWICDTYY YYAACIFVIS AISIGLSLYE TRKQSKTLQN
MVKMAISVRV RRPSGGEAMV SSEDLVPGDC ISLPCDGLLV PCDAALLTGE CMVNESMLTG
ESVPVMKTPL PDGPQAINLI YSPEEHKRHT LFCGTQVLQA KSYVGQDVLA VVTRTGFCTA
KGDLISSILY PKPLSFKFYK DAMKFVLFLA VLALIGTIYS ILILIRNKVA LGQIIIRALD
LITVIVPPAL PAAMTVGTIY AQNRLKKHGI FCVSPPRINL CGKIHLVCFD KTGTLTEDGL
DVWGVVPLEN SCFLPLIQEP RCLPDGPLLY SLSTCHTVSL LREQPIGDPV DLKMMESTGW
ILEKAEGEEA DLHAIQQFGT KVLAVMKPPP VEEQPHGTKH QVPVGILRRF PFSSSLQRMS
VVVKLPGDAP AEAYAKGAPE MVASLCNKET VPGDFSQMLR HYTTDGFRVL ALAYKPLAPV
KTFEDAQQLT RDAVESGLTL LGFLVMKNVL KAETAPVIHL LRKASLRPVM VTGDNMLTAV
NVAKSCRMVE PKERVVFVNG SPPDHDRPAA LKFSLAEQAP GQELAEGPYQ QEGCLLRQLP
SHLALNGKSF AVVCEHFPDL LPKILVQATI FARMSPDQKT RLVRCLQDLN YCVGMCGDGA
NDCGALKAAD VGISLSEAEA SVASPFTSRI PNIECVPLVI REGRCSLVTS FGVFKYMALY
SLVQFVSVLL LYTINTNLSD LQFLFFDLII TTTVAVLMGK TGPAQELGTQ RPQGALISVL
VLGSLLLQTA LLIIVQVASY FITVSQTWYV PLNSTVTAPQ NLPNYENTVV FCISGFQYLT
LAVAMSKGYP FRKPLYTNVP FLLALVILFG LMIGVTVYPL GFVKSLLMLK DTSDMNFKLL
LVGMATLNFF VAFTLETALD HGMLDWVRKL RRKKTSKKLF KRVEEELRRQ QPPWPPLDQP
LLATPRMSIA VR
//
