ID A0A8I5ZTP8_RAT Unreviewed; 1133 AA. AC A0A8I5ZTP8; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 03-MAY-2023, entry version 6. DE SubName: Full=ATPase cation transporting 13A2 {ECO:0000313|Ensembl:ENSRNOP00000082003.1}; GN Name=Atp13a2 {ECO:0000313|Ensembl:ENSRNOP00000082003.1, GN ECO:0000313|RGD:1307977}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000082003.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000082003.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000082003.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000082003.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000082003.1}; RG Ensembl; RL Submitted (JAN-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 Ensembl; ENSRNOT00000114069.1; ENSRNOP00000082003.1; ENSRNOG00000008052.8. DR AGR; RGD:1307977; -. DR RGD; 1307977; Atp13a2. DR GeneTree; ENSGT00940000159714; -. DR Proteomes; UP000002494; Chromosome 5. DR GO; GO:0005776; C:autophagosome; ISO:RGD. DR GO; GO:0005770; C:late endosome; ISO:RGD. DR GO; GO:0031902; C:late endosome membrane; ISO:RGD. DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD. DR GO; GO:0005764; C:lysosome; ISO:RGD. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005771; C:multivesicular body; ISO:RGD. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; ISO:RGD. DR GO; GO:0030133; C:transport vesicle; ISO:RGD. DR GO; GO:0031982; C:vesicle; ISO:RGD. DR GO; GO:0012506; C:vesicle membrane; ISO:RGD. DR GO; GO:0015417; F:ABC-type polyamine transporter activity; ISO:RGD. 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; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro. DR GO; GO:0070300; F:phosphatidic acid binding; ISO:RGD. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:RGD. DR GO; GO:0015203; F:polyamine transmembrane transporter activity; ISO:RGD. DR GO; GO:1905037; P:autophagosome organization; ISO:RGD. DR GO; GO:0061909; P:autophagosome-lysosome fusion; ISO:RGD. DR GO; GO:0006914; P:autophagy; ISO:RGD. DR GO; GO:0071287; P:cellular response to manganese ion; ISO:RGD. DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD. DR GO; GO:0097734; P:extracellular exosome biogenesis; ISO:RGD. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:RGD. DR GO; GO:0006879; P:intracellular iron ion homeostasis; ISO:RGD. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; ISO:RGD. DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD. DR GO; GO:0007041; P:lysosomal transport; ISO:RGD. DR GO; GO:1990938; P:peptidyl-aspartic acid autophosphorylation; ISO:RGD. DR GO; GO:1902047; P:polyamine transmembrane transport; ISO:RGD. DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD. DR GO; GO:0061462; P:protein localization to lysosome; ISO:RGD. DR GO; GO:0016243; P:regulation of autophagosome size; IMP:RGD. DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:RGD. DR GO; GO:1905123; P:regulation of glucosylceramidase activity; ISO:RGD. DR GO; GO:1905165; P:regulation of lysosomal protein catabolic process; ISO:RGD. DR GO; GO:0016241; P:regulation of macroautophagy; ISO:RGD. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:RGD. DR GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:RGD. DR GO; GO:2000152; P:regulation of ubiquitin-specific protease activity; ISO:RGD. DR GO; GO:1903710; P:spermine transmembrane transport; ISO:RGD. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. 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; 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; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1. DR PANTHER; PTHR45630:SF2; POLYAMINE-TRANSPORTING ATPASE 13A2; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR Pfam; PF12409; P5-ATPase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00120; HATPASE. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 TIGRFAMs; TIGR01494; ATPase_P-type; 2. DR TIGRFAMs; TIGR01657; P-ATPase-V; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; 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 251..271 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 423..444 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 456..479 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 917..936 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 980..1010 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1030..1050 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1071..1091 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 659..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 670..689 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1133 AA; 123325 MW; 81C54C86B462E874 CRC64; LSTDSSPLLG STPPSYGTLM TGTSIDPLSS SVSSVRLSGY CGSPWRAIGY HAAVWMLAGI PWLLFRWKPL WGVRLRLRPC SLARAETLVI EIRDKEGSSR QLFTVQVQTE AVVDGSLELP SQAKAEDGRS LAAVGVAPES MWQDTTQLHR QKEAKQVLRY YILQGQRYVW METQQAFCQV SLLDHGRACD DIHCSSSGLS LQDQAVRKTI YGPNVIGIPV KSYLQLLVDE ALNPYYGFQA FSIALWLADH YYWYAVCIFL ISAISICLSL YKTRKQSMTL RDMVKLSVRV QVCRPGGEEE WVDSSELVPG DCLVLPQEGG MMPCDAALVA GECVVNESSL TGESIPVLKT ALPEGPQPYC PETHRRHTLF CGTLVLQARA YLGPRVLAVV TRTGFCTAKG GLVSSILHPR PISFKFYRHS MKFVAALSVL ALLGTIYSII ILYRNRVPVK EIVIRALDLV TVVVPPALPA AMTVCTLYAQ SRLRTQGIFC IHPLRINLGG KLRLVCFDKT GTLTEDGLDI MGVVPLKGQM LLPLVPEPCH LPPGPLLRAL VTCHALSQLH DTLVGDPMDL KMVESTGWVL EEGSAAGSAP ETQVLVVMRP PPRGPQQQEE SPEPVSVLRR FPFSSALQRM DVVVTWPGAT QPEAYVKGSP ELVASLCSPE TGEGGSGGGL RSVTHTSLPT SPDDTCQPSR DTVEQELSLL GLLVMRNLLK PQTTPVIQTL RKTGIRTVMV TGDNLQTAVT VAKACGMVGT QEHLAIIHAT HPEQGQPAAL EFLPTEPSAA MNGAKDPVQA TDYPVEPESQ SRHLALSGST FAVLQKHFPK LLPKVLVQAT VFARMAPEQK TQLVCELQRL QYCVGMCGDG ANDCGALKAA DVGISLSQAE ASVVSPFTSS MASIECVPTV IREGRCSLDT SFSVFKYMAL YSLTQFISVL ILYTINTNLG DLQFLAIDLF ITTTVAVLMS RTGPALTLVR ARPPGALLSV PVLGSLLLQV ALVAGIQLGG YFLVIAQPWF VPLNRTVPAP DNLPNYENTV IFSLSGFQYL ILAAAVSKGA PFRQPLYTNG LRNIADSSFK LLLLGLVAFN FVGAFMLESV LDQCLPACLQ WLRPKRASKK QFKQLQRELA ERPWPTLPVG SVR //