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Protein

Calcium-transporting ATPase

Gene

ATP2B3

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.UniRule annotation

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).UniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-transporting ATPase activity Source: UniProtKB-EC
  3. metal ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Calcium transportUniRule annotation, Ion transport, Transport

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Calcium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPaseUniRule annotation (EC:3.6.3.8UniRule annotation)
Gene namesi
Name:ATP2B3Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei376 – 39722HelicalUniRule annotationAdd
BLAST
Transmembranei417 – 44327HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Proteomic databases

PRIDEiA1L3B5.

Expressioni

Gene expression databases

BgeeiA1L3B5.
ExpressionAtlasiA1L3B5. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliA1L3B5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Phylogenomic databases

HOGENOMiHOG000265623.
HOVERGENiHBG061286.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.50.1000. 1 hit.
InterProiIPR030325. ATP2B3.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF265. PTHR24093:SF265. 1 hit.
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1L3B5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDMANSSIE FHPKPQQQRD VPQAGGFGCT LAELRTLMEL RGAEALQKIE
60 70 80 90 100
EAYGDVSGLC RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ
110 120 130 140 150
LVWEALQDVT LIILEVAAIV SLGLSFYAPP GEESEACGNV SGGAEDEGEA
160 170 180 190 200
EAGWIEGAAI LLSVICVVLV TAFNDWSKEK QFRGLQSRIE QEQKFTVIRN
210 220 230 240 250
GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQANDLKID ESSLTGESDH
260 270 280 290 300
VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
310 320 330 340 350
KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA
360 370 380 390 400
NAPKKEKSVL QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVEGR
410 420 430 440 450
TWLAECTPVY VQYFVKFFII GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK
460 470 480 490 500
DNNLVRHLDA CETMGNATAI CSDKTGTLTT NRMTVVQSYL GDTHYKEIPA
510 520 530 540 550
PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG NKTECALLGF
560 570 580 590 600
VLDLKRDFQP VREQIPEDKL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
610 620 630 640 650
ASEILLKKCT NILNSNGELR GFRPRDRDDM VRKIIEPMAC DGLRTICIAY
660 670 680 690 700
RDFSAGQEPD WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT
710 720 730 740 750
VRMVTGDNIN TARAIAAKCG IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE
760 770 780 790 800
RLDKVWPKLR VLARSSPTDK HTLVKGIIDS TTGEQRQVVA VTGDGTNDGP
810 820 830 840 850
ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM WGRNVYDSIS
860 870
KFLQFQLTVN VVAVIVAFTG ACIT
Length:874
Mass (Da):95,426
Last modified:February 6, 2007 - v1
Checksum:iD62D8158B93431D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC130009 mRNA. Translation: AAI30010.1.
UniGeneiHs.533956.
Hs.658008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC130009 mRNA. Translation: AAI30010.1.
UniGeneiHs.533956.
Hs.658008.

3D structure databases

ProteinModelPortaliA1L3B5.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA1L3B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000265623.
HOVERGENiHBG061286.

Miscellaneous databases

ChiTaRSiATP2B3. human.
NextBioi35460530.

Gene expression databases

BgeeiA1L3B5.
ExpressionAtlasiA1L3B5. baseline and differential.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.50.1000. 1 hit.
InterProiIPR030325. ATP2B3.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF265. PTHR24093:SF265. 1 hit.
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiA1L3B5_HUMAN
AccessioniPrimary (citable) accession number: A1L3B5
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: February 4, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.