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P22700 (ATC1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type

EC=3.6.3.8
Alternative name(s):
Calcium ATPase at 60A
Calcium pump
Gene names
Name:Ca-P60A
ORF Names:CG3725
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Interacts with SclA and SclB. Ref.7

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Note: Colocalizes with SclA and SclB at the sarcoplasmic reticulum (SR) and the dyad, a structure in which the SR membrane lies closest to both the plasma membrane and the sarcomeres. Ref.7

Sequence similarities

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

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from sequence or structural similarity Ref.1. Source: GOC

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 16899722. Source: FlyBase

flight behavior

Inferred from genetic interaction PubMed 16899722. Source: FlyBase

heart contraction

Inferred from mutant phenotype PubMed 24098595. Source: FlyBase

intestinal stem cell homeostasis

Inferred from mutant phenotype PubMed 23434461. Source: FlyBase

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 15520268. Source: FlyBase

positive regulation of calcium-transporting ATPase activity

Inferred from genetic interaction PubMed 24098595. Source: FlyBase

regulation of sequestering of calcium ion

Inferred from mutant phenotype PubMed 15520268. Source: FlyBase

stabilization of membrane potential

Inferred from genetic interaction PubMed 16899722. Source: FlyBase

stem cell differentiation

Inferred from mutant phenotype PubMed 23434461. Source: FlyBase

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from direct assay PubMed 16979555. Source: FlyBase

nuclear envelope

Inferred from direct assay PubMed 15520268. Source: FlyBase

sarcoplasmic reticulum

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-transporting ATPase activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17362353. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P22700-1)

Also known as: C; D; E; F; G; H;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform A (identifier: P22700-2)

The sequence of this isoform differs from the canonical sequence as follows:
     994-1020: GESPIYKMHGIVLMWAVFFGLLYAMML → VPDVVVDRM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10201020Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
PRO_0000046208

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 6921Helical; Name=1; By similarity
Topological domain70 – 8920Lumenal By similarity
Transmembrane90 – 11021Helical; Name=2; By similarity
Topological domain111 – 253143Cytoplasmic By similarity
Transmembrane254 – 27320Helical; Name=3; By similarity
Topological domain274 – 29522Lumenal By similarity
Transmembrane296 – 31318Helical; Name=4; By similarity
Topological domain314 – 757444Cytoplasmic By similarity
Transmembrane758 – 77720Helical; Name=5; By similarity
Topological domain778 – 78710Lumenal By similarity
Transmembrane788 – 80821Helical; Name=6; By similarity
Topological domain809 – 82820Cytoplasmic By similarity
Transmembrane829 – 85123Helical; Name=7; By similarity
Topological domain852 – 89746Lumenal By similarity
Transmembrane898 – 91720Helical; Name=8; By similarity
Topological domain918 – 93013Cytoplasmic By similarity
Transmembrane931 – 94919Helical; Name=9; By similarity
Topological domain950 – 96415Lumenal By similarity
Transmembrane965 – 98521Helical; Name=10; By similarity
Topological domain986 – 102035Cytoplasmic By similarity

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2; via carbonyl oxygen By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3091Calcium 2 By similarity
Metal binding7031Magnesium By similarity
Metal binding7071Magnesium By similarity
Metal binding7681Calcium 1 By similarity
Metal binding7711Calcium 1 By similarity
Metal binding7961Calcium 2 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding8001Calcium 1 By similarity
Metal binding8001Calcium 2 By similarity
Metal binding9081Calcium 1 By similarity

Amino acid modifications

Modified residue2401Phosphoserine Ref.6

Natural variations

Alternative sequence994 – 102027GESPI…YAMML → VPDVVVDRM in isoform A.
VSP_010297

Experimental info

Sequence conflict1581K → R in AAL13694. Ref.4
Sequence conflict3021L → V in AAB00735. Ref.1
Sequence conflict3571T → L in CAA35505. Ref.5
Sequence conflict4951S → P in AAL13694. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform B (C) (D) (E) (F) (G) (H) [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 6A62D350BF316984

FASTA1,020111,701
        10         20         30         40         50         60 
MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW QLVLEQFDDL 

        70         80         90        100        110        120 
LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA NAVVGVWQER NAESAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL VEVSVGDKIP ADIRITHIYS TTLRIDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TDAIPDPRAV NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS 

       250        260        270        280        290        300 
ETEEIKTPLQ QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV 

       310        320        330        340        350        360 
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 

       370        380        390        400        410        420 
MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ RIKAADYDTL QELSTICIMC 

       430        440        450        460        470        480 
NDSAIDYNEF KQAFEKVGEA TETALIVLAE KLNSFSVNKS GLDRRSAAIA CRGEIETKWK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSSYCTP LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA 

       550        560        570        580        590        600 
LKAKILALTG QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML 

       610        620        630        640        650        660 
DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG KSYSGREFDD 

       670        680        690        700        710        720 
LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM TGDGVNDAPA LKKAEIGIAM 

       730        740        750        760        770        780 
GSGTAVAKSA AEMVLADDNF SSIVSAVEEG RAIYNNMKQF IRYLISSNIG EVVSIFLTAA 

       790        800        810        820        830        840 
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI 

       850        860        870        880        890        900 
GFYVGAATVG AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA 

       910        920        930        940        950        960 
LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV DVLSTVFQVT 

       970        980        990       1000       1010       1020 
PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK MHGIVLMWAV FFGLLYAMML 

« Hide

Isoform A [UniParc].

Checksum: 463400C1967BD7D7
Show »

FASTA1,002109,611

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal localization of a sarco/endoplasmic reticulum-type Ca2(+)-ATPase of Drosophila melanogaster."
Magyar A., Varadi A.
Biochem. Biophys. Res. Commun. 173:872-877(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Head.
[5]"Amplification of the phosphorylation site-ATP-binding site cDNA fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by polymerase chain reaction."
Varadi A., Gilmore-Heber M., Benz E.J. Jr.
FEBS Lett. 258:203-207(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 357-513.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[7]"Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames."
Magny E.G., Pueyo J.I., Pearl F.M., Cespedes M.A., Niven J.E., Bishop S.A., Couso J.P.
Science 341:1116-1120(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCLA AND SCLB, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62892 mRNA. Translation: AAB00735.1.
AE013599 Genomic DNA. Translation: AAF47101.1.
AE013599 Genomic DNA. Translation: AAF47102.1.
AE013599 Genomic DNA. Translation: AAF47103.1.
AE013599 Genomic DNA. Translation: AAM68278.1.
AE013599 Genomic DNA. Translation: AAM68279.1.
AE013599 Genomic DNA. Translation: AAM68280.1.
AE013599 Genomic DNA. Translation: AAM68281.1.
AY058465 mRNA. Translation: AAL13694.1.
X17472 mRNA. Translation: CAA35505.1.
PIRA36691.
RefSeqNP_476832.1. NM_057484.2. [P22700-2]
NP_726381.1. NM_166633.1. [P22700-1]
NP_726382.1. NM_166634.1. [P22700-1]
NP_726383.1. NM_166635.1. [P22700-1]
NP_726384.1. NM_166636.1. [P22700-1]
NP_726385.1. NM_166637.1. [P22700-1]
NP_726386.1. NM_166638.1. [P22700-1]
NP_726387.1. NM_166639.1. [P22700-1]
UniGeneDm.3812.

3D structure databases

ProteinModelPortalP22700.
SMRP22700. Positions 1-989.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid72161. 103 interactions.
DIPDIP-20129N.
IntActP22700. 2 interactions.
MINTMINT-1567799.

Proteomic databases

PaxDbP22700.
PRIDEP22700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072211; FBpp0072120; FBgn0263006. [P22700-1]
FBtr0072212; FBpp0072121; FBgn0263006. [P22700-1]
FBtr0072213; FBpp0072122; FBgn0263006. [P22700-1]
FBtr0072214; FBpp0072123; FBgn0263006. [P22700-1]
FBtr0072216; FBpp0072125; FBgn0263006. [P22700-1]
FBtr0072217; FBpp0072126; FBgn0263006. [P22700-1]
FBtr0072218; FBpp0072127; FBgn0263006. [P22700-1]
GeneID49297.
KEGGdme:Dmel_CG3725.

Organism-specific databases

CTD49297.
FlyBaseFBgn0263006. Ca-P60A.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076887.
InParanoidP22700.
OMAPKMEDMI.
OrthoDBEOG73Z2SF.
PhylomeDBP22700.

Gene expression databases

BgeeP22700.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR005782. ATPase_P-typ_Ca-transp_IIA.
IPR006068. ATPase_P-typ_cation-transptr_C.
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.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi49297.
NextBio839728.
PROP22700.

Entry information

Entry nameATC1_DROME
AccessionPrimary (citable) accession number: P22700
Secondary accession number(s): A4UZU0 expand/collapse secondary AC list , Q2MGN2, Q95TX1, Q9W1G2, Q9W1G3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase