ID   A0A5F5XWB1_FELCA        Unreviewed;      1157 AA.
AC   A0A5F5XWB1;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2B4 {ECO:0000313|Ensembl:ENSFCAP00000058542.1,
GN   ECO:0000313|VGNC:VGNC:68639};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000058542.1, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000058542.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000058542.1,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000058542.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000058542.1,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000058542.1}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000058542.1};
RG   Ensembl;
RL   Submitted (JAN-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC         Evidence={ECO:0000256|RuleBase:RU361146};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; AANG04001043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A5F5XWB1; -.
DR   Ensembl; ENSFCAT00000077321.1; ENSFCAP00000058542.1; ENSFCAG00000000870.6.
DR   VGNC; VGNC:68639; ATP2B4.
DR   GeneTree; ENSGT00940000154527; -.
DR   Proteomes; UP000011712; Chromosome F1.
DR   Bgee; ENSFCAG00000000870; Expressed in brain and 10 other tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 3.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093:SF435; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 4; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 2.
DR   Pfam; PF00702; Hydrolase; 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   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Ion transport {ECO:0000256|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        409..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        843..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        916..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        957..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        995..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1028..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          45..121
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          294..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  128649 MW;  37BC986C95E56CFA CRC64;
     MTNPTERTLP ANSMVESHER EFGCTVMDLR KLMELRSTDA INQINVHYGG VTNLCSRLKT
     NPVEGLSGNP ADLEKRKHVF GQNFIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
     FYRPPGEENE QCGLPVSSPE DEGEAEAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL
     QNRIEKEQKF SVIRNGHIIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT
     GESDHVKKSV ERDPMLLSGT HVMEGSGRMV VTAVGINSQT GIIFTLLGAS EGEEEEKKKK
     GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GTDNEEKEKK AAKLPRKEKS VLQGKLTRLA
     VQIGKAGLIM SAITVLILIL YFVIDNFVIH RRAWLPECTP IYIQYFVKFF IIGITVLVVA
     VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA
     YIGDTHYHQI PSPDVLLPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGSKTECALL
     GFVTDLKQDY HAVRNEVPEE KLYKVYTFNS VRKSMSTVIE KPSGGYRMYS KGASEIILRK
     CNRILDKKGE VVPFKNKDRD EIVRTVIEPM ACEGLRTICI AYRDFNDGEP PWDNESEILT
     ELTCVAVVGI EDPVRPEVPD AIAKCKQAGI TVRMVTGDNI NTARAIATKC GIVTPGDDFL
     CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGEQRQVV
     AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
     SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTESLL
     KRRPYGRNKP LISRTMMKNI LGHAVYQLTV IFFLVFAGEK FFDIDSGRKA PLHSPPSQHY
     TIIFNTFVLM QLFNEINSRK IHGERNVFAG IFRNLIFCCV VLGTFISQIL IVEFGGKPFS
     CTKLTLSQWF WCLFIGIGEL LWGQIISSIP TQSLKFLKEA GHGTTKEEIT KDAEGLDEID
     HAEMELRRGQ ILWFRGLNRI QTQIKVVKAF HSSLHESIQK PKNQNSIHNF MTHPEFAIDE
     KVQTGPQSGC LLLFHWN
//