AT2B1_CHICK
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 03-AUG-2022, entry version 114.
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.ENSGALP00000018350; -.
DR Ensembl; ENSGALT00000080355; ENSGALP00000055998; ENSGALG00000030550.
DR GeneID; 374244; -.
DR KEGG; gga:374244; -.
DR CTD; 490; -.
DR VEuPathDB; HostDB:geneid_374244; -.
DR GeneTree; ENSGT00940000158686; -.
DR InParanoid; Q98SH2; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q98SH2; -.
DR PRO; PR:Q98SH2; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000030550; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q98SH2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030320; ATP2B1.
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:SF245; PTHR24093:SF245; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
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
