P22700 (ATC1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1020 AA.
Sequence status	Complete.
Protein existence	Evidence 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).
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular calcium ion homeostasis Inferred from mutant phenotype PubMed 16899722. Source: FlyBase flight behavior Inferred from genetic interaction PubMed 16899722. Source: FlyBase neuromuscular synaptic transmission Inferred from mutant phenotype PubMed 15520268. 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
Cellular_component	integral to 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_function	ATP 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
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1020	1020	Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type		PRO_0000046208
Regions
	Topological domain	1 – 48	48	Cytoplasmic By similarity
	Transmembrane	49 – 69	21	Helical; Name=1; By similarity
	Topological domain	70 – 89	20	Lumenal By similarity
	Transmembrane	90 – 110	21	Helical; Name=2; By similarity
	Topological domain	111 – 253	143	Cytoplasmic By similarity
	Transmembrane	254 – 273	20	Helical; Name=3; By similarity
	Topological domain	274 – 295	22	Lumenal By similarity
	Transmembrane	296 – 313	18	Helical; Name=4; By similarity
	Topological domain	314 – 757	444	Cytoplasmic By similarity
	Transmembrane	758 – 777	20	Helical; Name=5; By similarity
	Topological domain	778 – 787	10	Lumenal By similarity
	Transmembrane	788 – 808	21	Helical; Name=6; By similarity
	Topological domain	809 – 828	20	Cytoplasmic By similarity
	Transmembrane	829 – 851	23	Helical; Name=7; By similarity
	Topological domain	852 – 897	46	Lumenal By similarity
	Transmembrane	898 – 917	20	Helical; Name=8; By similarity
	Topological domain	918 – 930	13	Cytoplasmic By similarity
	Transmembrane	931 – 949	19	Helical; Name=9; By similarity
	Topological domain	950 – 964	15	Lumenal By similarity
	Transmembrane	965 – 985	21	Helical; Name=10; By similarity
	Topological domain	986 – 1020	35	Cytoplasmic By similarity
Sites
	Active site	351	1	4-aspartylphosphate intermediate By similarity
	Metal binding	304	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	305	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	307	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	309	1	Calcium 2 By similarity
	Metal binding	703	1	Magnesium By similarity
	Metal binding	707	1	Magnesium By similarity
	Metal binding	768	1	Calcium 1 By similarity
	Metal binding	771	1	Calcium 1 By similarity
	Metal binding	796	1	Calcium 2 By similarity
	Metal binding	799	1	Calcium 1 By similarity
	Metal binding	800	1	Calcium 1 By similarity
	Metal binding	800	1	Calcium 2 By similarity
	Metal binding	908	1	Calcium 1 By similarity
Amino acid modifications
	Modified residue	240	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	994 – 1020	27	GESPI…YAMML → VPDVVVDRM in isoform A.		VSP_010297
Experimental info
	Sequence conflict	158	1	K → R in AAL13694. Ref.4
	Sequence conflict	302	1	L → V in AAB00735. Ref.1
	Sequence conflict	357	1	T → L in CAA35505. Ref.5
	Sequence conflict	495	1	S → P in AAL13694. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform B (C) (D) (E) (F) (G) (H) [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 6A62D350BF316984	FASTA	1,020	111,701
	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
	Isoform A [UniParc]. Checksum: 463400C1967BD7D7	FASTA	1,002	109,611
	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 PLSAEEWITV MKFSIPVVLL DETLKFVARK IADVPDVVVD RM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Embryo.
+	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.
PIR	A36691.
RefSeq	NP_476832.1. NM_057484.2. NP_726381.1. NM_166633.1. NP_726382.1. NM_166634.1. NP_726383.1. NM_166635.1. NP_726384.1. NM_166636.1. NP_726385.1. NM_166637.1. NP_726386.1. NM_166638.1. NP_726387.1. NM_166639.1.
UniGene	Dm.3812.
3D structure databases
ProteinModelPortal	P22700.
SMR	P22700. Positions 1-989.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20129N.
IntAct	P22700. 2 interactions.
MINT	MINT-1567799.
Proteomic databases
PaxDb	P22700.
PRIDE	P22700.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0072211; FBpp0072120; FBgn0263006. FBtr0072212; FBpp0072121; FBgn0263006. FBtr0072213; FBpp0072122; FBgn0263006. FBtr0072214; FBpp0072123; FBgn0263006. FBtr0072216; FBpp0072125; FBgn0263006. FBtr0072217; FBpp0072126; FBgn0263006. FBtr0072218; FBpp0072127; FBgn0263006.
GeneID	49297.
KEGG	dme:Dmel_CG3725.
Organism-specific databases
CTD	49297.
FlyBase	FBgn0263006. Ca-P60A.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076887.
InParanoid	P22700.
OMA	TEARTMG.
OrthoDB	EOG4XD25Z.
PhylomeDB	P22700.
Gene expression databases
Bgee	P22700.
GermOnline	CG3725. Drosophila melanogaster.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR005782. 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]
PANTHER	PTHR24093. PTHR24093. 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.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	49297.
NextBio	839728.

Entry information

Entry name

ATC1_DROME

Accession

Primary (citable) accession number: P22700
Secondary accession number(s): A4UZU0 , Q2MGN2, Q95TX1, Q9W1G2, Q9W1G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project