Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type - Drosophila pseudoobscura pseudoobscura (Fruit fly)

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Reviewed, UniProtKB/Swiss-Prot Q292Q0 (ATC1_DROPS)

Last modified June 16, 2009. Version 26. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
      Short name=Calcium pump
    EC=3.6.3.8

Gene names

Name:	Ca-P60A
ORF Names:	GA17643

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Complete proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length	1002 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic activity	ATP + H₂O + Ca²⁺(Cis) = ADP + phosphate + Ca²⁺(Trans).
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family.

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Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW sarcoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1002

1002

Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type

PRO_0000233306

Regions

Topological domain

1 – 48

Cytoplasmic By similarity UniProtKB P04191

Transmembrane

49 – 69

1 By similarity UniProtKB P04191

Topological domain

70 – 89

Lumenal By similarity UniProtKB P04191

Transmembrane

90 – 110

2 By similarity UniProtKB P04191

Topological domain

111 – 253

143

Cytoplasmic By similarity UniProtKB P04191

Transmembrane

254 – 273

3 By similarity UniProtKB P04191

Topological domain

274 – 295

Lumenal By similarity UniProtKB P04191

Transmembrane

296 – 313

4 By similarity UniProtKB P04191

Topological domain

314 – 757

444

Cytoplasmic By similarity UniProtKB P04191

Transmembrane

758 – 777

5 By similarity UniProtKB P04191

Topological domain

778 – 787

Lumenal By similarity UniProtKB P04191

Transmembrane

788 – 808

6 By similarity UniProtKB P04191

Topological domain

809 – 828

Cytoplasmic By similarity UniProtKB P04191

Transmembrane

829 – 851

7 By similarity UniProtKB P04191

Topological domain

852 – 897

Lumenal By similarity UniProtKB P04191

Transmembrane

898 – 917

8 By similarity UniProtKB P04191

Topological domain

918 – 930

Cytoplasmic By similarity UniProtKB P04191

Transmembrane

931 – 949

9 By similarity UniProtKB P04191

Topological domain

950 – 964

Lumenal By similarity UniProtKB P04191

Transmembrane

965 – 985

10 By similarity UniProtKB P04191

Topological domain

986 – 1002

Cytoplasmic By similarity

Sites

Active site

351

4-aspartylphosphate intermediate By similarity UniProtKB P04191

Metal binding

304

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

305

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

307

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

309

Calcium 2 By similarity UniProtKB P04191

Metal binding

703

Magnesium By similarity UniProtKB P04191

Metal binding

707

Magnesium By similarity UniProtKB P04191

Metal binding

768

Calcium 1 By similarity UniProtKB P04191

Metal binding

771

Calcium 1 By similarity UniProtKB P04191

Metal binding

796

Calcium 2 By similarity UniProtKB P04191

Metal binding

799

Calcium 1 By similarity UniProtKB P04191

Metal binding

800

Calcium 1 By similarity UniProtKB P04191

Metal binding

800

Calcium 2 By similarity UniProtKB P04191

Metal binding

908

Calcium 1 By similarity UniProtKB P04191

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Sequences

Sequence

Length

Mass (Da)

Tools

Q292Q0-1 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: CC68BABBEBD7BB77
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FASTA

1,002

109,168

        10         20         30         40         50         60 
MEDGHSKTVE QSLNFFGTDG ERGLTLDQIK TNQAKYGPNE LPTEEGKSIW QLVLEQFDDL 

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

       130        140        150        160        170        180 
EYEPEMGKVI RQDKSGIQKV RAKEIVPGDL VEVSVGDKIP ADIRLTHIYS TTIRIDQSIL 

       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 
MSVSRMLIFE KVEGNDSSFL EFELTGSTYE PIGELFLGGQ RVKASDYEAL QELATVCIMC 

       430        440        450        460        470        480 
NDSAIDYNEF KAAFEKVGEA TETALIVLAE KLNAFSVNKS GLDRRSNAIA ARGEIETKWK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSSYCTP LKASRLGTGP KLFVKGAPEG VLDRCTHARV GTSKVPLTSA 

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

       610        620        630        640        650        660 
DPPRKEVFDA IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFTEEEDTTG KSYSGREFDD 

       670        680        690        700        710        720 
LSIAEQKAAV ARSRLFSRVE PQHKSKIVEY LQGMNEISAM TGDGVNDAPA LKKAEIGIAM 

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

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

       850        860        870        880        890        900 
GFYVGAATVG AAAWWFIASS EGPGLTYWQL THHLSCLGGG DEFKGVDCKI FSDPKAMTMA 

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

       970        980        990       1000 
PLSAEEWITV MKFSIPVVLL DETLKFVARK IADVPDAVVD KW

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References

[1]

"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L.

Gibbs R.A.
Genome Res. 15:1-18(2005) [PubMed: 15632085] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MV2-25.

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Cross-references

Sequence databases
	CM000071 Genomic DNA. Translation: EAL24811.2.
RefSeq	XP_001360237.2.
3D structure databases
SMR	Q292Q0. Positions 1-994.
ModBase	Search...
Genome annotation databases
GeneID	4803524.
KEGG	dpo:Dpse_GA17643.
Organism-specific databases
FlyBase	FBgn0077654. Dpse\GA17643.
Enzyme and pathway databases
BRENDA	3.6.3.8. 190795.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ATC1_DROPS

Accession

Primary (citable) accession number: Q292Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 20, 2009
Last modified:	June 16, 2009
This is version 26 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project

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Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents