ID A0A2Y9F413_PHYMC Unreviewed; 1174 AA.
AC A0A2Y9F413;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=ATP13A2 {ECO:0000313|RefSeq:XP_007114610.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007114610.2};
RN [1] {ECO:0000313|RefSeq:XP_007114610.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007114610.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR RefSeq; XP_007114610.2; XM_007114548.4.
DR AlphaFoldDB; A0A2Y9F413; -.
DR STRING; 9755.ENSPCTP00005000491; -.
DR KEGG; pcad:102986477; -.
DR InParanoid; A0A2Y9F413; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000248484; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; 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: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 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, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 253..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 931..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 956..973
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 994..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1043..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1076..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 34..170
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 790..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 128179 MW; 2F143AD92B84A599 CRC64;
MSADSSPLMG NTPAGYGTLT IETSLDALSS SVSSVRLSGY CGSPWRAIGY HVVVWMMAGI
PLLLFRWKPV WRVRLRLQPC SLACAETLVI EIRDKEDSSW QLYTVQVQTE AISKDSLELP
PRTQAEDGRS QAALGTLPEG TWKDTAELHR TEEAQQTLRY YLFRGQRYVW IETQQAFCRV
SLLDHGRTCD DLHCSSTGLS LQDQTVRKTI YGPNVISVPV KSYPQLLVDE ALNPYYGFQA
FSIGLWLADY YYWYALCIFL ISVVSICVSI YKTRKQSQTL RDMVQLSVRV CVCRPGGEEE
WVDSSELVPG DCLVLPQEGG LMPCDAALVA GECMVNESSL TGESVPVLKT ALPEGPVPYF
PETHQRHTLF CGTLILQARA FVGPHVLAVV TQTGFCTAKG ALVSSILHPR PINFKFYKHS
VKFVAALSVL ALLGTIYSIF ILQRNQVPLD EIVIRALDLV TVAVPPALPA AMTVCTLYAQ
SRLRSQGVFC VHPMRINLGG KLRLVCFDKT GTLTEDGLDV MGVVPLKGQE FLPLVPEPRR
LPMGPLLRAL ATCHTLSRLR DTPVGDPLDL KMVESTGWVL EEGPAADSTF GTQVLAVMRP
PLQELHLQGV EEPLVPVGIL SHFPFSSALQ RMSVVVAWPG AARPEACVKG SPELVAGLCD
PRTVPADFAQ MLQSYTAAGY RVVALASKPL PIAPNMEAAQ QLTRDTVEWK LSLLGLLVMQ
NLLKPQTTPV IQALRRTHIR TVMVTGDNLQ TAVTVAQGCG MVGPQERLVI IHANPPERGQ
PASLELQPVE SSAAVNGAQD PDQAASYTME PDPRSSHLAL SGSTFGVLMK HFPKLLPKVL
VQGTVFARMA PEQKTELVCE LQKLQYCVGM CGDGANDCGA LKAADVGISL SQAEASVVSP
FTSSVANIEC VPMVIREGRC SLDTSFSVFK YMALYSLTQF ISVLLLYTVN TNLGDVQFLV
IDLAITTAVA VLMSRTGPAL ALGQARPPGA LLSVPVLSSL LLQVALVASV QLGGYFLTVA
QPWFVPLNRT VPAPDNLPNY ENTVVFCLSS FQYLILAVAV SKGAPFRRPL YTNVPFLVAL
VLLGSVLVGL LLAPGLLQGL LKLRRFADTY FKLLLLGLVA FNFVGAFMLE SVLDQCLPGC
LRWLRPKRAS KKRFKQLEQE LAEQPWPPPT RPVR
//
