ID A0A2Y9N0W6_DELLE Unreviewed; 1215 AA.
AC A0A2Y9N0W6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_022425012.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022425012.1};
RN [1] {ECO:0000313|RefSeq:XP_022425012.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022425012.1};
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|RuleBase:RU362082}.
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DR RefSeq; XP_022425012.1; XM_022569304.2.
DR AlphaFoldDB; A0A2Y9N0W6; -.
DR Proteomes; UP000248483; 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; 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; 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:UP000248483};
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 27..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 406..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 892..916
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 922..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 957..984
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1033..1051
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1063..1083
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1103..1128
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 1215 AA; 137544 MW; 42C5BCAAA3A53B7B CRC64;
MDKEERKTIN QGQEDEMEIY GYNLCRWKLA IVSLGVVCTG GFLLLLLYWM PEWRVKATCI
RAAVKDCEVV LLRTTDEFRM WFCAKIRFLS LETPPFSSSK SMANKVSNGH AVHLTENLAE
ENRLEMNKYS QSQSQQIRYF THHSVKYFWN DTLHNFVFLK GLDEGVSCTS IYEKHSAGLT
KGMHAYRKLL YGVNEIAVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYAIAIVI
MSVVSIISSL YAIRKQYIML HDMVAAHSTV RVSVCRVNEG ESVPVTKTNL PNPSVDVKGM
GDELYSPETH RRHTLFCGTT VIQTRFYTGE LVKAIVVRTG FSTSKGQLVR SILYPKPTDF
KLYRDAYLFL LCLVAVAGIG FIYTIINSIL NEVEVGDIII ESLDIITITV PPALPAAMTA
GIVYAQRRLK KVGIFCISPQ RINICGQLNL VCFDKTGTLT EDGLDLWGIQ RVENTRFLLP
EEKVCNEMLV KSQFVACMAT CHSLTKIEGV LSGDPLDLKM FEAIGWILEE ATEEETALHN
RIMPTVVRPP KQLLPESTPA GNQEMELFEL PAIYEIGIVR QFPFSSALQR MSVVARVLGD
RKMDAYVKGA PEVIAGLCKP ETVPVDFEKV LENYTKQGFR VIALAHRKLE SKLTWHKVQN
ISRDAIENNM DFMGLIIMQN KLKRETPAVL EDLHKANIRT VMVTGDNMLT AVSVARDCGM
ILPQDKVIIA EALPPKDGKV AKINWHYADT LTQSSDSSAV DSEAIPIKLV HDNLEDLQVT
RYHFAMNGKS FSVILEHFQD LVPKLMLHGT VFARMAPDQK TQLVEALQNV DYFVGMCGDG
ANDCGALKRA HGGISLSELE ASVASPFTSK TPSISCVPNL IREGRAALMT SFCVFKFMAL
YSIIQYFSVT LLYSILSNLG DFQFLFIDLA IILVVVFTMS LNPAWKELVA QRPPSGLISG
ALLFSVLSQI IICIGFQSLG FFWVKQQTWY KESHPHSDTQ EAFNTTGSLY GNSSHLYNET
NPDRHNIENY ENTTVFFISS FQYLIVAIAF SKGKPFRQPC YKNYFFVVSL IILYVFILFI
MLHPVASIDQ ILQIVCVPYQ WRVTMLIIVL VNAFVSIMVE NFFLDMVLWK VVFNRDKQGE
YRFTTTQPPQ ESVDWWGKCC LSWALNCRKK MPKAKYMYLA QELLVDPEWP PKPQTTTEAK
ALVKENGSCQ IITIT
//
