ID   Q8N4D4_HUMAN            Unreviewed;      1088 AA.
AC   Q8N4D4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   SubName: Full=ATP13A2 protein {ECO:0000313|EMBL:AAH34575.1};
DE   Flags: Fragment;
GN   Name=ATP13A2 {ECO:0000313|EMBL:AAH34575.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAH34575.1};
RN   [1] {ECO:0000313|EMBL:AAH34575.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix {ECO:0000313|EMBL:AAH34575.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   EMBL; BC034575; AAH34575.1; -; mRNA.
DR   RefSeq; NP_001135445.1; NM_001141973.2.
DR   RefSeq; NP_001135446.1; NM_001141974.2.
DR   AlphaFoldDB; Q8N4D4; -.
DR   PeptideAtlas; Q8N4D4; -.
DR   DNASU; 23400; -.
DR   GeneID; 23400; -.
DR   OrthoDB; 6047at2759; -.
DR   BioGRID-ORCS; 23400; 14 hits in 1156 CRISPR screens.
DR   ChiTaRS; ATP13A2; human.
DR   GenomeRNAi; 23400; -.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
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; 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; 2.
DR   NCBIfam; TIGR01657; P-ATPase-V; 1.
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   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   2: Evidence at transcript level;
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   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        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        907..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        957..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        986..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1026..1046
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          18..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAH34575.1"
SQ   SEQUENCE   1088 AA;  118812 MW;  63D6A9E5EFFB2888 CRC64;
     RDKEDSSWQL FTVQVQTEAI GEGSLEPSPQ SQAEDGRSQA AVGAVPEGAW KDTAQLHKSE
     EAVSVGQKRV LRYYLFQGQR YIWIETQQAF YQVSLLDHGR SCDDVHRSRH GLSLQDQMVR
     KAIYGPNVIS IPVKSYPQLL VDEALNPYYG FQAFSIALWL ADHYYWYALC IFLISSISIC
     LSLYKTRKQS QTLRDMVKLS MRVCVCRPGG EEEWVDSSEL VPGDCLVLPQ EGGLMPCDAA
     LVAGECMVNE SSLTGESIPV LKTALPEGLG PYCAETHRRH TLFCGTLILQ ARAYVGPHVL
     AVVTRTGFCT AKGGLVSSIL HPRPINFKFY KHSMKFVAAL SVLALLGTIY SIFILYRNRV
     PLNEIVIRAL DLVTVVVPPA LPAAMTVCTL YAQSRLRRQG IFCIHPLRIN LGGKLQLVCF
     DKTGTLTEDG LDVMGVVPLK GQAFLPLVPE PRRLPVGPLL RALATCHALS RLQDTPVGDP
     MDLKMVESTG WVLEEEPAAD SAFGTQVLAV MRPPLWEPQL QAMEEPPVPV SVLHRFPFSS
     ALQRMSVVVA WPGATQPEAY VKGSPELVAG LCNPETVPTD FAQMLQSYTA AGYRVVALAS
     KPLPTVPSLE AAQQLTRDTV EGDLSLLGLL VMRNLLKPQT TPVIQALRRT RIRAVMVTGD
     NLQTAVTVAR GCGMVAPQEH LIIVHATHPE RGQPASLEFL PMESPTAVNG VKDPDQAASY
     TVEPDPRSRH LALSGPTFGI IVKHFPKLLP KVLVQGTVFA RMAPEQKTEL VCELQKLQYC
     VGMCGDGAND CGALKAADVG ISLSQAEASV VSPFTSSMAS IECVPMVIRE GRCSLDTSFS
     VFKYMALYSL TQFISVLILY TINTNLGDLQ FLAIDLVITT TVAVLMSRTG PALVLGRVRP
     PGALLSVPVL SSLLLQMVLV TGVQLGGYFL TLAQPWFVPL NRTVAAPDNL PNYENTVVFS
     LSSFQYLILA AAVSKGAPFR RPLYTNVPFL VALALLSSVL VGLVLVPGLL QGPLALRNIT
     DTGFKLLLLG LVTLNFVGAF MLESVLDQCL PACLRRLRPK RASKKRFKQL ERELAEQPWP
     PLPAGPLR
//