ID H2V5N9_TAKRU Unreviewed; 1265 AA.
AC H2V5N9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=ATPase 13A3 {ECO:0000313|Ensembl:ENSTRUP00000044523.3};
GN Name=ATP13A3 {ECO:0000313|Ensembl:ENSTRUP00000044523.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000044523.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000044523.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000044523.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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; H2V5N9; -.
DR Ensembl; ENSTRUT00000044673.3; ENSTRUP00000044523.3; ENSTRUG00000017383.3.
DR GeneTree; ENSGT00940000155941; -.
DR Proteomes; UP000005226; Chromosome 20.
DR GO; GO:0016020; C: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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
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; 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; 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 SMART; SM00831; Cation_ATPase_N; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1031
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1043..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1185..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..274
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 142470 MW; 5C4E697954252C74 CRC64;
MEKEDLKILN KGGEEEMVYY FGLLLQCLNL SFFSIQNKPF DLSVCLQELQ GYHLCRWRLV
LVGLGVLCTG GFLLLLLYWM PEWCVKCTCT RTSVRDADVI LLRSTDDFRH WFLARVRVML
APGSNPFYSL DTQTTSPPSP KCPFSSLPSP ANRNTSHPST GSPAQELISK FVDYQPTQIR
YFTFHSAKYY WNDAMQNFEV LTGMEDLQVT CSTLHSEHSA GLTRNQQEYR KLFFGVNEIA
VKVPSLFKLL IKEVLNPFYI FQLFSVILWS ADEYYYYAVA IVIMSVISIA TSLYTIKKQY
VMLHDMVATH SIVRVSVCRS NDEIEEILST DLVPGDLMVI PSNGTIMPCD AVLVSGTCIV
NESMLTGESV PVTKTNLPNP FHGDGGDEAD CPYNTEEHKR HTLFCGTNVI QTRFYTGELV
KAVVVRTGFS TAKGQLVRSI LYPKPTDFKL YHDAYIFLFC LVGVAAIGFI YSIALSIIHE
VPAKTIIIES LDIVTITVPP ALPAAMTAGI VYAQRRLKNL RIFCISPQRI NICGQINLVC
FDKTGTLTED GLDLWGVQRV DNGSFFLSEE NAYKENLVKS QFVACMATCH SLTKIDGQLS
GDPLDLKMFE ATGWILEEAT EEETSLHNRI MPTVVRPPKQ LLPPEPVTSP EQDMELYELS
STYEIGIVRQ FPFSSTLQRM SVVARLLGEK CMDAYMKGAP EVVASLCKKE TVPENFAEVL
EGYTKQGFRV IALAHRRLES KLTWHKVQNV NRDHLEAKMD FLGLIIMQNK LKAETAGVLH
DLHKARIRTV MVTGDNMLTA ISVARDCGMI PPQDTVIIAD ALPPHNGQTA KITWRYADKP
ALTTRLGEVN ISLEDVCHED ALKRKEQYHF AMNGKSFAVI AEHFPDMLHK LMLHGTVFAR
MAPDQKTQLI EILQDVDYYV GMCGDGANDC GALKRAHGGI SLSELEASVA SPFTSKTPNI
SCVPSLIREG RAALITSFCV FKFMALYSII QYISVTLLYS ILSNLGDFQF LFIDIAIILL
IVFTMSLNAA WKELVSCRPP SGLISAPLLL SVITQILICL GFQIFTFLLV KQQPWYTVWE
PITDVCNQSS YINKSDLNDT EADDHNIQNF ENTSIFYVSC FQYLIVAIVF SKGKPFRQPS
YKNWPFVLSV ASLYAFLLFI MFHPVETIDD FLDIVCVPVE WRVKLFIIIL VNATVSVLVE
VGFDYSRCKC LPWFCCRRKM APKARYKRLA QELSVDPDWP PKPTTTTEAM PRPENGSSYQ
IMVDC
//
