ID A0A1V4K392_PATFA Unreviewed; 1249 AA.
AC A0A1V4K392;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=ATP13A4 {ECO:0000313|EMBL:OPJ78932.1};
GN ORFNames=AV530_004906 {ECO:0000313|EMBL:OPJ78932.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ78932.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ78932.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ78932.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ78932.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ78932.1}.
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DR EMBL; LSYS01004732; OPJ78932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4K392; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; 2.
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; 4.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF1; CATION-TRANSPORTING ATPASE 13A4-RELATED; 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; PF12409; P5-ATPase; 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, 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:UP000190648};
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 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 223..242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 396..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 905..923
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 929..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 969..991
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1045..1063
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1115..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 147..220
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1249 AA; 139639 MW; AC8A8F7B786D4EB3 CRC64;
MVWMSLDSSL ETRNHQPTLD KEIFGYKTQS CRKALCIAGY ILSCGALLLL FYWKPEWDVW
ANCIRCSLEE ADVVLLRTTD EYQIYSRKTV TWISVSALIK SRSDYPTTAE EDSLFSKAIT
KPSLQVRSIQ VQKIRYVWNI CAKQFQKVGA LEDHHTCSAI HAKFGSGLTC DEQNVRRVIC
GPNTIDVPVI PIWKLLVKEV LNPFYVFQLF SVCLWFAEEY MEYAIAIIIM SLLSIFLTVY
DLRQQSIKLH RLVESHNNMM VTVCRNKEGF QELESHHLVP GDVLVLKEGK TLLPCDAILI
SGQCVVNESM LTGESIPVTK THLPQADNCK PWRMHCAEDY KKHVLFCGTE VIQTKADDRG
AVKAVVLRTG FNTAKGDLVR SILYPKPMNF KLYRDALRFL MCLIAFAAIG MIYAVCVFVL
NGEETGEVVK KALDVITIAV PPALPAALTT GIIYTQRRLK KKGIFCISPQ RINMCGQLNL
ICFDKTGTLT EDGLDLWGLL PSERNCFQDV HSFPADHSLP WGPVFRAMAV CHSLIVWEGK
IQGDPLDVKM FEATNWVIDD SSGHQIDGHG STHAMVVRPG PKASSAPVEG VTILHQFPFS
SALQRMSVIA QEIGGEQQVF TKGAPETVAM LCRAETVPSN FESKLRLYTA QGFRVIGLAC
KSLQSGKQST DLTREEIESD LTFLGLLIME NRLKRETKPV LEELSAARIR SVMVTGDNIQ
TAVTVAKNAG MISPMNRVIL VEANEIPGSF SAYVTWKPLE EEKTGDYRTL ENDSQTERKI
RPALESGQYH FATSGKSYQI IAQHFRHLLP KLLLNGTVFA RMSPGQKSSL VEEFQKLDYF
VGMCGDGAND CGALKVAHAG ISLSEQEASV ASPFTSRTPS IACVPELIRE GRAALVTSFC
MFKYMALYST IQYLGVLLLY WQLNSFGNYQ FLFQDLAITT VIGVTMSFTG AYPKLVPYRP
PSQLVSPPLL LSVVLNILFS LSMQIFGFVV VQEQPWYSKT DIHSACLSMN NHMENSSSIS
SLGHGGLRDV TLEQMDNGYK SYENTTVWLL STINCIIVAL VFSKGKPFRQ PVYTNYVFIL
VLIGQLGICL FLLFADIDDL YSKMDLVCTP TMWRISMVMM LAVTFAVSFI VEPSLEISSK
TGVVAATSPL LSFLKVPHLN DQIQGSARPN HLFCPLEAVI ENRALWLLMK KTFWYQSKSH
YKRLQRALEQ DPAWPPLNET FFSDSVAISV EGNMGGHSNP TFDSNEDAL
//
