Reviewed, UniProtKB/Swiss-Prot O46674 (AT2A2_CANFA)

Names and origin

Protein names

Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
      Short name=SR Ca(2+)-ATPase 2
      Short name=SERCA2
    EC=3.6.3.8
Alternative name(s):
    Calcium pump 2
    Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
    Endoplasmic reticulum class 1/2 Ca(2+) ATPase

Gene names

Name:

ATP2A2

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	997 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle By similarity.
Catalytic activity	ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).
Enzyme regulation	Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN.
Subunit structure	Associated with phospholamban (PLN). Isoform SERCA2B interacts with TRAM2 (via C-terminus). Interacts with HAX1 By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Isoform SERCA2A is highly expressed in heart and slow twitch skeletal muscle. Isoform SERCA2B is widely expressed.
Post-translational modification	Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Isopeptide bond Nitration Phosphoprotein Ubl conjugation
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-SubCell sarcoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Isoform SERCA2A (identifier: O46674-1)

Also known as: ATP2A2A;

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.

Isoform SERCA2B (identifier: O46674-2)

Also known as: ATP2A2B;

The sequence of this isoform is not available.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 997	997	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2		PRO_0000046194
Regions
	Topological domain	1 – 48	48	Cytoplasmic By similarity
	Transmembrane	49 – 69	21	1 By similarity
	Topological domain	70 – 89	20	Lumenal By similarity
	Transmembrane	90 – 110	21	2 By similarity
	Topological domain	111 – 253	143	Cytoplasmic By similarity
	Transmembrane	254 – 273	20	3 By similarity
	Topological domain	274 – 295	22	Lumenal By similarity
	Transmembrane	296 – 313	18	4 By similarity
	Topological domain	314 – 756	443	Cytoplasmic By similarity
	Transmembrane	757 – 776	20	5 By similarity
	Topological domain	777 – 786	10	Lumenal By similarity
	Transmembrane	787 – 807	21	6 By similarity
	Topological domain	808 – 827	20	Cytoplasmic By similarity
	Transmembrane	828 – 850	23	7 By similarity
	Topological domain	851 – 896	46	Lumenal By similarity
	Transmembrane	897 – 916	20	8 By similarity
	Topological domain	917 – 929	13	Cytoplasmic By similarity
	Transmembrane	930 – 948	19	9 By similarity
	Topological domain	949 – 963	15	Lumenal By similarity
	Transmembrane	964 – 984	21	10 By similarity
	Topological domain	985 – 997	13	Cytoplasmic By similarity
	Region	370 – 400	31	Interacts with phospholamban 1 By similarity
	Region	575 – 594	20	Interacts with HAX1 By similarity
	Region	787 – 807	21	Interacts with phospholamban 2 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	702	1	Magnesium By similarity
	Metal binding	706	1	Magnesium By similarity
	Metal binding	767	1	Calcium 1 By similarity
	Metal binding	770	1	Calcium 1 By similarity
	Metal binding	795	1	Calcium 2 By similarity
	Metal binding	798	1	Calcium 1 By similarity
	Metal binding	799	1	Calcium 1 By similarity
	Metal binding	799	1	Calcium 2 By similarity
	Metal binding	907	1	Calcium 1 By similarity
Amino acid modifications
	Modified residue	294	1	Nitrated tyrosine By similarity
	Modified residue	295	1	Nitrated tyrosine By similarity
	Modified residue	464	1	N6-acetyllysine By similarity
	Modified residue	537	1	Phosphothreonine By similarity
	Modified residue	663	1	Phosphoserine By similarity
	Cross-link	143		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform SERCA2A (ATP2A2A) [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 266770F599A9E3D3	FASTA	997	109,653
	10 20 30 40 50 60 MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 70 80 90 100 110 120 LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 130 140 150 160 170 180 EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 190 200 210 220 230 240 TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 250 260 270 280 290 300 ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 310 320 330 340 350 360 ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 370 380 390 400 410 420 MSVCRMFILD RVEGDSCSLN EFTITGSTYA PIGEVHKDDK PVKCHQYDGL VELATICALC 430 440 450 460 470 480 NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 490 500 510 520 530 540 KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV 550 560 570 580 590 600 KQKVMSVIRE WGSGSDTLRC LALATHDNPL RREEMNLEDS ANFIKYETNL TFVGCVGMLD 610 620 630 640 650 660 PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 670 680 690 700 710 720 SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG 730 740 750 760 770 780 SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 790 800 810 820 830 840 GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 850 860 870 880 890 900 CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKDDNP DFEGVDCAIF ESPYPMTMAL 910 920 930 940 950 960 SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 970 980 990 LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPAILE
	Isoform SERCA2B (ATP2A2B) (Sequence not available).	FASTA	–	–

References

[1]

"Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation." Autry J.M., Jones L.R. J. Biol. Chem. 272:15872-15880(1997) [PubMed: 9188486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U94345 mRNA. Translation: AAC02263.1.
PIR	A24345.
RefSeq	NP_001003214.1.
UniGene	Cfa.97
3D structure databases
SMR	O46674. Positions 1-992.
ModBase	Search...
Protein-protein interaction databases
STRING	O46674.
Genome annotation databases
Ensembl	ENSCAFT00000027396; ENSCAFP00000025477; ENSCAFG00000008434; Canis familiaris. [Genome view]
GeneID	403878.
KEGG	cfa:403878.
Organism-specific databases
CTD	403878.
Phylogenomic databases
eggNOG	maNOG06423.
HOVERGEN	O46674.
Enzyme and pathway databases
BRENDA	3.6.3.8. 463.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_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. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AT2A2_CANFA

Accession

Primary (citable) accession number: O46674

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)