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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Acts as a regulator of TNFSF11-mediated Ca2+ signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation.By similarity

Catalytic activityi

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

Enzyme regulationi

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (By similarity). Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi304Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi305Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi307Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi309Calcium 2By similarity1
Active sitei3514-aspartylphosphate intermediateBy similarity1
Metal bindingi702MagnesiumBy similarity1
Metal bindingi706MagnesiumBy similarity1
Metal bindingi767Calcium 1By similarity1
Metal bindingi770Calcium 1By similarity1
Metal bindingi795Calcium 2By similarity1
Metal bindingi798Calcium 1By similarity1
Metal bindingi799Calcium 1By similarity1
Metal bindingi799Calcium 2By similarity1
Metal bindingi907Calcium 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SSC-418359. Reduction of cytosolic Ca++ levels.
R-SSC-5578775. Ion homeostasis.
R-SSC-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:3.6.3.8)
Short name:
SERCA2
Short name:
SR Ca(2+)-ATPase 2
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 namesi
Name:ATP2A2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 14

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 48CytoplasmicBy similarityAdd BLAST48
Transmembranei49 – 69Helical; Name=1By similarityAdd BLAST21
Topological domaini70 – 89LumenalBy similarityAdd BLAST20
Transmembranei90 – 110Helical; Name=2By similarityAdd BLAST21
Topological domaini111 – 253CytoplasmicBy similarityAdd BLAST143
Transmembranei254 – 273Helical; Name=3By similarityAdd BLAST20
Topological domaini274 – 295LumenalBy similarityAdd BLAST22
Transmembranei296 – 313Helical; Name=4By similarityAdd BLAST18
Topological domaini314 – 756CytoplasmicBy similarityAdd BLAST443
Transmembranei757 – 776Helical; Name=5By similarityAdd BLAST20
Topological domaini777 – 786LumenalBy similarity10
Transmembranei787 – 807Helical; Name=6By similarityAdd BLAST21
Topological domaini808 – 827CytoplasmicBy similarityAdd BLAST20
Transmembranei828 – 850Helical; Name=7By similarityAdd BLAST23
Topological domaini851 – 896LumenalBy similarityAdd BLAST46
Transmembranei897 – 916Helical; Name=8By similarityAdd BLAST20
Topological domaini917 – 929CytoplasmicBy similarityAdd BLAST13
Transmembranei930 – 948Helical; Name=9By similarityAdd BLAST19
Topological domaini949 – 963LumenalBy similarityAdd BLAST15
Transmembranei964 – 984Helical; Name=10By similarityAdd BLAST21
Topological domaini985 – 1042CytoplasmicBy similarityAdd BLAST58

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000461981 – 1042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2Add BLAST1042

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphoserineBy similarity1
Modified residuei294Nitrated tyrosineBy similarity1
Modified residuei295Nitrated tyrosineBy similarity1
Modified residuei441PhosphothreonineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei580PhosphoserineBy similarity1
Modified residuei663PhosphoserineBy similarity1

Post-translational modificationi

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.By similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

PeptideAtlasiP11607.
PRIDEiP11607.

Expressioni

Tissue specificityi

Isoform 2 is highly expressed in heart and slow twitch skeletal muscle. Isoform 1 is widely expressed.1 Publication

Interactioni

Subunit structurei

Interacts with sarcolipin (SLN) (By similarity). Interacts with phospholamban (PLN) (By similarity). Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF (By similarity). Isoform 1 interacts with TRAM2 (via C-terminus). Interacts with HAX1. Interacts with S100A8 and S100A9 (By similarity). Interacts with SLC35G1 and STIM1. Interacts with TMEM203. Interacts with TMEM64 and PDIA3 (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

IntActiP11607. 2 interactors.
MINTiP11607.

Structurei

Secondary structure

11042
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Helixi9 – 16Combined sources8
Turni20 – 22Combined sources3
Helixi26 – 36Combined sources11
Helixi49 – 57Combined sources9
Helixi60 – 75Combined sources16
Helixi84 – 87Combined sources4
Helixi89 – 109Combined sources21
Helixi115 – 119Combined sources5
Helixi120 – 122Combined sources3
Beta strandi125 – 131Combined sources7
Beta strandi134 – 136Combined sources3
Beta strandi138 – 141Combined sources4
Helixi142 – 144Combined sources3
Beta strandi150 – 153Combined sources4
Beta strandi161 – 168Combined sources8
Beta strandi174 – 176Combined sources3
Helixi178 – 181Combined sources4
Beta strandi185 – 188Combined sources4
Helixi201 – 203Combined sources3
Beta strandi205 – 208Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi219 – 225Combined sources7
Helixi227 – 229Combined sources3
Helixi231 – 239Combined sources9
Helixi248 – 274Combined sources27
Beta strandi278 – 280Combined sources3
Turni288 – 290Combined sources3
Helixi291 – 306Combined sources16
Helixi311 – 327Combined sources17
Turni328 – 330Combined sources3
Beta strandi331 – 335Combined sources5
Helixi338 – 341Combined sources4
Beta strandi347 – 350Combined sources4
Helixi352 – 356Combined sources5
Beta strandi362 – 373Combined sources12
Beta strandi376 – 384Combined sources9
Beta strandi387 – 391Combined sources5
Beta strandi395 – 401Combined sources7
Helixi404 – 406Combined sources3
Helixi408 – 419Combined sources12
Beta strandi424 – 427Combined sources4
Turni429 – 431Combined sources3
Beta strandi433 – 438Combined sources6
Helixi440 – 452Combined sources13
Helixi466 – 478Combined sources13
Beta strandi479 – 488Combined sources10
Turni489 – 492Combined sources4
Beta strandi493 – 503Combined sources11
Turni504 – 506Combined sources3
Beta strandi510 – 515Combined sources6
Helixi517 – 521Combined sources5
Beta strandi524 – 529Combined sources6
Beta strandi532 – 535Combined sources4
Helixi538 – 552Combined sources15
Beta strandi553 – 556Combined sources4
Beta strandi559 – 568Combined sources10
Helixi580 – 582Combined sources3
Helixi583 – 586Combined sources4
Beta strandi589 – 599Combined sources11
Helixi606 – 615Combined sources10
Beta strandi619 – 623Combined sources5
Helixi628 – 637Combined sources10
Turni648 – 650Combined sources3
Beta strandi651 – 653Combined sources3
Helixi654 – 659Combined sources6
Helixi662 – 671Combined sources10
Beta strandi674 – 677Combined sources4
Helixi680 – 692Combined sources13
Beta strandi697 – 701Combined sources5
Helixi707 – 712Combined sources6
Beta strandi713 – 719Combined sources7
Helixi724 – 728Combined sources5
Beta strandi730 – 736Combined sources7
Helixi740 – 780Combined sources41
Helixi788 – 806Combined sources19
Helixi815 – 817Combined sources3
Helixi830 – 856Combined sources27
Beta strandi859 – 861Combined sources3
Helixi866 – 870Combined sources5
Helixi872 – 874Combined sources3
Helixi889 – 891Combined sources3
Helixi893 – 913Combined sources21
Beta strandi915 – 919Combined sources5
Beta strandi921 – 924Combined sources4
Helixi926 – 928Combined sources3
Helixi930 – 948Combined sources19
Helixi952 – 956Combined sources5
Helixi964 – 973Combined sources10
Helixi975 – 989Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MPMX-ray3.30A1-993[»]
ProteinModelPortaliP11607.
SMRiP11607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 400Interaction with phospholamban 1By similarityAdd BLAST31
Regioni575 – 594Interaction with HAX1By similarityAdd BLAST20
Regioni787 – 807Interaction with phospholamban 2By similarityAdd BLAST21
Regioni788 – 1042Interaction with TMEM64 and PDIA3By similarityAdd BLAST255

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00890000139334.
HOVERGENiHBG105648.
InParanoidiP11607.
KOiK05853.

Family and domain databases

Gene3Di3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiView protein in InterPro
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_dom_N.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom_sf.
IPR008250. ATPase_P-typ_transduc_dom_A_sf.
IPR036412. HAD-like_sf.
IPR023214. HAD_sf.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
PfamiView protein in Pfam
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PRINTSiPR00120. HATPASE.
SMARTiView protein in SMART
SM00831. Cation_ATPase_N. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81653. SSF81653. 1 hit.
SSF81660. SSF81660. 1 hit.
SSF81665. SSF81665. 3 hits.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiView protein in PROSITE
PS00154. ATPASE_E1_E2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11607-1) [UniParc]FASTAAdd to basket
Also known as: ATP2A2B, SERCA2b

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.

« Hide

        10         20         30         40         50
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI
160 170 180 190 200
VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCRMFILD KVEGDTCSLN EFTITGSTYA PIGEVHKDDK
410 420 430 440 450
PVKCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE
460 470 480 490 500
KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP
510 520 530 540 550
NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV KQKIMSVIRE
560 570 580 590 600
WGSGSDTLRC LALATHDNPM RREEMNLEDS ANFIKYETNL TFVGCVGMLD
610 620 630 640 650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK
660 670 680 690 700
AFTGREFDEL NPSAQREACL NARCFARVEP SHKSKIVEFL QSFDEITAMT
710 720 730 740 750
GDGVNDAPAL KKSEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR
760 770 780 790 800
AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG
810 820 830 840 850
LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA
860 870 880 890 900
AAWWFIAADG GPRVTFYQLS HFLQCKEDNP DFEGVDCAVF ESPYPMTMAL
910 920 930 940 950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE
960 970 980 990 1000
PLPLIFQITP LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP
1010 1020 1030 1040
ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS
Length:1,042
Mass (Da):114,792
Last modified:October 1, 1989 - v1
Checksum:iA68EC9E41494D532
GO
Isoform 2 (identifier: P11607-2) [UniParc]FASTAAdd to basket
Also known as: ATP2A2A, SERCA2a

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Show »
Length:997
Mass (Da):109,726
Checksum:i66697619E312CA3E
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000360994 – 1042GKECV…DMFWS → AILE in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15074 mRNA. Translation: CAA33170.1.
X15073 mRNA. Translation: CAA33169.1.
X53754 Genomic DNA. Translation: CAA37783.1.
X53754 Genomic DNA. Translation: CAA37784.1.
PIRiS04651.
S04652.
RefSeqiNP_999030.1. NM_213865.1. [P11607-1]
UniGeneiSsc.97090.

Genome annotation databases

EnsembliENSSSCT00000040296; ENSSSCP00000039305; ENSSSCG00000034386. [P11607-2]
ENSSSCT00000045994; ENSSSCP00000037774; ENSSSCG00000034386. [P11607-1]
ENSSSCT00000055257; ENSSSCP00000045838; ENSSSCG00000034386. [P11607-1]
GeneIDi396875.
KEGGissc:396875.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiAT2A2_PIG
AccessioniPrimary (citable) accession number: P11607
Secondary accession number(s): P11606, P79426, P79427
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: March 28, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome