ID   AT2B1_CHICK             Reviewed;        1205 AA.
AC   Q98SH2; A0A1D5PSV8; Q9PSK0;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Plasma membrane calcium-transporting ATPase 1 {ECO:0000250|UniProtKB:P20020};
DE            EC=7.2.2.10 {ECO:0000250|UniProtKB:G5E829};
DE   AltName: Full=Plasma membrane calcium ATPase isoform 1 {ECO:0000250|UniProtKB:P20020};
DE            Short=PMCA1 {ECO:0000250|UniProtKB:P20020};
DE   AltName: Full=Plasma membrane calcium pump isoform 1;
GN   Name=ATP2B1 {ECO:0000250|UniProtKB:P20020}; Synonyms=PMCA1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000312|EMBL:AAK14839.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 992-1205, AND INDUCTION.
RC   STRAIN=White leghorn; TISSUE=Intestine;
RX   PubMed=7679502; DOI=10.1073/pnas.90.4.1345;
RA   Cai Q., Chandler J.S., Wasserman R.H., Kumar R., Penniston J.T.;
RT   "Vitamin D and adaptation to dietary calcium and phosphate deficiencies
RT   increase intestinal plasma membrane calcium pump gene expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1345-1349(1993).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium from the cytoplasm to the extracellular space thereby
CC       maintaining intracellular calcium homeostasis.
CC       {ECO:0000250|UniProtKB:G5E829}.
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:0000250|UniProtKB:G5E829};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20020};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- INDUCTION: By vitamin D and 1,25-dihydroxyvitamin D3, and by calcium
CC       and phosphorous deficiency. {ECO:0000269|PubMed:7679502}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
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DR   EMBL; AADN04000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L08769; AAK14839.1; -; mRNA.
DR   PIR; A47276; A47276.
DR   RefSeq; NP_001161474.1; NM_001168002.3.
DR   AlphaFoldDB; Q98SH2; -.
DR   SMR; Q98SH2; -.
DR   STRING; 9031.ENSGALP00000057692; -.
DR   PaxDb; 9031-ENSGALP00000018350; -.
DR   Ensembl; ENSGALT00000080355; ENSGALP00000055998; ENSGALG00000030550.
DR   Ensembl; ENSGALT00015018064; ENSGALP00015009914; ENSGALG00015007592.
DR   GeneID; 374244; -.
DR   KEGG; gga:374244; -.
DR   CTD; 490; -.
DR   VEuPathDB; HostDB:geneid_374244; -.
DR   InParanoid; Q98SH2; -.
DR   PhylomeDB; Q98SH2; -.
DR   Reactome; R-GGA-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-GGA-5578775; Ion homeostasis.
DR   Reactome; R-GGA-936837; Ion transport by P-type ATPases.
DR   PRO; PR:Q98SH2; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000030550; Expressed in brain and 13 other cell types or tissues.
DR   ExpressionAtlas; Q98SH2; baseline and differential.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
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   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093:SF245; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 1; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   CHAIN           2..1205
FT                   /note="Plasma membrane calcium-transporting ATPase 1"
FT                   /id="PRO_0000046213"
FT   TOPO_DOM        2..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        126..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        175..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        352..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        372..403
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425..840
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        841..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        862..868
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        869..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        890..912
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        913..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        934..956
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        957..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        977..990
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        991..1012
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        1013..1024
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1025..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   TOPO_DOM        1046..1205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          94..111
FT                   /note="Calmodulin-binding subdomain A"
FT                   /evidence="ECO:0000250"
FT   REGION          296..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        460
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         782
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   MOD_RES         1101
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1022
FT                   /note="S -> L (in Ref. 2; AAK14839)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1050
FT                   /note="R -> H (in Ref. 2; AAK14839)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1205 AA;  133019 MW;  81904969719EC111 CRC64;
     MGDMANNSVA YSGVKNAVKE ANHGEFGVTL AELRSLMELR ATDALHKIQE CYGDVQGICT
     KLKTSPNEGL SGNPADIERR EAVFGKNFIP PKKPKTFLQL VWEALQDVTL IILEIAAVVS
     LGLSFYQPPG GNEALCGSVN VGEEEEESEA GWIEGAAILL SVVCVVLVTA FNDWSKEKQF
     RGLQSRIEQE QKFTVIRGGQ VIQIPVADII VGDIAQVKYG DLLPADGILI QGNDLKIDES
     SLTGESDHVK KSLDRDPMLL SGTHVMEGSG RMVVTAVGVN SQTGIIFTLL GAGGDEEEKE
     KEKKDKKTKA QDGAAMEMQP LKSEDGVDGD EKDKKRSNLP KKEKSVLQGK LTKLAVQIGK
     AGLLMSAITV IILVLYFVID TSWVQKRPWL AECTPIYIQY FVKFFIIGVT VLVVAVPEGL
     PLAVTISLAY SVKKMMRDNN LVRHLDACET MGNATAICSD KTGTLTMNRM TVVQAYISEK
     HYKKIPAPEA IPENIMAYLV TGISVNCAYT SKILPPEKEG GLPRHVGNKT ECALLGFLLD
     LKRDYQDVRN EIPEEKLHKV YTFNSVRKSM STVLKNSDGS FRIFSKGASE IVLKKCFKIL
     SADGEPKVFR PRDRDDIVKT VIEPMASEGL RTICLAFRDF PAGEPEPEWD NENDIVTGLT
     CIAVVGIEDP VRPEVPDAIK KCQRAGITVR MVTGDNINTA RAIALKCGIL NPGEDFLCLE
     GKDFNRRIRN EKGEIEQERI DKIWPKLRVL ARSSPTDKHT LVKGIIDSTI FDQRQVVAVT
     GDGTNDGPAL KKADVGFAMG IAGTDVAKEA SDIILTDDNF TSIVKAVMWG RNVYDSISKF
     LQFQLTVNVV AVIVAFTGAC ITQDSPLKAV QMLWVNLIMD TLASLALATE PPTEALLLRK
     PYGRNKPLIS RTMMKNILGH AFYQLVVVFT LLFAGEKIFD IDSGRNAPLH APPSEHYTIV
     FNTFVMMQLF NEINARKIHG ERNVFEGIFN NAIFCTIVLG TFVVQIIIVQ FGGKPFSCSK
     LSIEQWLWSV FLGMGTLLWG QLISTIPTSR LKFLKEAGHG TQKEEIPEEE LAEDVEEIDH
     AERELRRGQI LWFRGLNRIQ TQIRVVNAFR SSLYEGLEKP ETRSSIHNFM THPEFRIEDS
     EPHIPLIDDT DAEDDAPTKR NSTPPPSPNK NNNAVDSGIH LTTDMNKSAT SSSPGSPLHS
     LETSL
//