ID A0A3P9NHI1_POERE Unreviewed; 1176 AA.
AC A0A3P9NHI1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ATPase 13A3 {ECO:0000313|Ensembl:ENSPREP00000009036.1};
GN Name=ATP13A3 {ECO:0000313|Ensembl:ENSPREP00000009036.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009036.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009036.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009036.1};
RG Ensembl;
RL Submitted (SEP-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}.
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 AlphaFoldDB; A0A3P9NHI1; -.
DR Ensembl; ENSPRET00000009146.1; ENSPREP00000009036.1; ENSPREG00000006118.1.
DR GeneTree; ENSGT00940000155941; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006118; Expressed in caudal fin and 1 other cell type or tissue.
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; 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; 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: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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000242638};
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 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 935..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 999..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..162
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 131275 MW; 31FFC5661D59768E CRC64;
MLAPGSNPFH SLETQTTSPP SSPSSPSCPF SSPSPSPLAN GHTPHPSDGS PAQELIRRFS
YYQPTQIRYF TFHSTKYYWN DEMQNFKVLI GLEDLEVSCS TIHSEHSAGL TRNQQEYRKL
FFGVNEIAVK VPSVFKLLIK EVLNPFYIFQ LFSIILWSAD EYYYYAVAIL LMSVISIATS
LYTIKKQYVM LHDMVAAHSI VRVSVYRANN DVEETLSTDL VPGDVVVIPS NGTIMPCDAV
LISGTCIVNE SMLTGESVPV TKTNLPNPLP GEREGADSAY NTEEHKRHTL FCGTNVIQTR
FYTGELVKAV VVRTGFSTAK GQLVRSILYP KPTDFKLYRD AYLFLLCLVA VAGIGFIYSI
ILSVMKGEEV KTIIIESLDI ITITVPPALP AAMTAGIVYA QRRLKKIGIF CISPQRINIC
GQINLVCFDK TGTLTEDGLD MWGVQRVEGG RFHLSEESAN KENLVKSQFV ACMATCHSLT
KIEGQLSGDP LDLKMFEATG WILEEATEEE TALHNRIMPT VVRPPPQLLP TQADESAEQD
MELAELSSLY EIGIVRQFPF SSALQRMSVV SRTLGEKCMD AYMKGAPEVV ASLCKSETVP
ENFAEVLEGY TKQGFRVIAL AHRRLGSKLN WHKVQNVNRD YIEANLEFLG LIIMQNKLKA
ETPGVLQDLH RANIRTIMVT GDNMLTAVSV ARDCGMIPPE DMVIIADALP PHDGQAAKIA
WRYADKPSRT TRLEEISISL EDEGHAEEPK TQPLYHFAMN GKSFAIIAEH FPDMLQKLVL
HGTVFARMAP DQKTQLVETL QGVDYFVGMC GDGANDCGAL KRAHSGISLS ELEASVASPF
TSRTPNISCV PSLIREGRAA LITSFCVFKF MALYSIIQYI SVTLLYSVSS NLGDFQFLFI
DIAIILLIVF TMSLNPAWKE LVSRRPPSGL ISGPLLFSVL TQILICLGFQ TITFLWVQKQ
PWFERWTPAT NVCNHSDHLN VSGLNQTDNH NIQNFENTSL FYVSCFQYLI VAIVFSKGKP
FRQPSYKNWP FVLSAVSLYF FLLFIMFYPV KGIDDYLEIV CVPFEWKLNL LLIIAVNAAV
SVMVETFILD IILWKLVLSR DKQATPAAPT PQGAVDMQAY KCLFRLCPRK TTPKARYMHL
AQELSLDPDW PPKPTTTTEA KPRPENGSVY DIISHS
//
