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Database: UniProt
Entry: A0A452RA50_URSAM
LinkDB: A0A452RA50_URSAM
Original site: A0A452RA50_URSAM 
ID   A0A452RA50_URSAM        Unreviewed;      1208 AA.
AC   A0A452RA50;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ATPase 13A3 {ECO:0000313|Ensembl:ENSUAMP00000015509.1};
GN   Name=ATP13A3 {ECO:0000313|Ensembl:ENSUAMP00000015509.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000015509.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000015509.1}
RP   IDENTIFICATION.
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}.
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DR   AlphaFoldDB; A0A452RA50; -.
DR   Ensembl; ENSUAMT00000017381.1; ENSUAMP00000015509.1; ENSUAMG00000011019.1.
DR   GeneTree; ENSGT00940000155941; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
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; 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; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
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        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        432..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        918..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        948..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        983..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1056..1074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1086..1110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1122..1142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..104
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   DOMAIN          158..208
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
SQ   SEQUENCE   1208 AA;  136015 MW;  0D0963532F69A7DC CRC64;
     MDKEERKTIN QGQEDEMEIY GYNLCRWKLA VVSLGVVCTG GFLLLLLYWM PEWRVKATCI
     RAAIRDCEVV LLRTTDEFRM WFCAKIRFLS LETHPFLSPK SMTNKVANGH AVHLSENLAE
     ETRHEMSKYS QTQPQQEYRK MRGLDEGVSC TSIYEKHSAG LTKGMHAYRK LLYGVNEITV
     KVPSVFKLLI KEVLNPFYIF QLFSVILWST DEYYYYALAI VIMSIVSIVS SLYSIRKQYI
     MLHDMVAAHS TVRVSVCRVN EEIEEIFSTD LVPGDVMVIP LNGTVMPCDA VLINGTCIVN
     ESMLTGESVP VTKTNLPNPS VDIKGMGDEF YSPEIHKRHT LFCGTTVIQT RFYTGELVKA
     VVVRTGFSTS KGQLVRSILY PKPTDFKLYR DAYLFLLCLV AVAGIGFIYT IINSILNKVE
     IGVIIIESLD IITITVPPAL PAAMTAGIVY AQRRLKKIGI FCISPQRINI CGQLNLVCFD
     KTGTLTEDGL DLWGIQRVEN TRFLLPEENV CNEILVKSQF VACMATCHSL TKIEGVLSGD
     PLDLKMFEAI GWILEEATEE ETALHNRIMP TVVRPAKQLL PESTPAGNQE MELFELPAIY
     EIGIVRQFPF SSALQRMSVV ARVLGDKKMD AYMKGAPEVI ASLCKPETVP VDFEKVLEDY
     TKQGFRVIAL AHRKLESKLT WHKVQNISRD VIENNMDFMG LIVMQNKLKQ ETPAVLEDLH
     KANIRTVMVT GDNMLTAVSV ARDCGMILPQ DKVIIAEALP PKDGKVAKIN WHYADTLTQC
     SNSSAIDSEA IPIKLVHDSL EDLQVTRYHF AMNGKSFSVI LEHFQDLAPK LMLHGTVFAR
     MAPDQKTQLI EALQNVDYFV GMCGDGANDC GALKRAHGGI SLSELEASVA SPFTSKTPSI
     SCVPNLIREG RAALMTSFCV FKFMALYSII QYFSVTLLYS ILSNLGDFQF LFIDLAIILV
     VVFTMSLNPA WKELVAQRPP SGLISGALLF SVLSQIIICI GFQSLGFFWV KQQPWYEVWH
     PQSDACNTTG SLYWNSSHLY NETDLDTHNI QNYENTTVFF ISSFQYLIVA IAFSKGKPFR
     QPCYKNYFFV VSVIILYVFI LLIMLHPVAS IDQVLQIVCV PYQWRITMLM IVLVNALVSI
     MVEESVDRWG KCCLSWALGC RKKIPKAKYM YLAQELLVDP EWPPKPQTTT EAKALVKENG
     SCQIITIT
//
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