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P04191

- AT2A1_RABIT

UniProt

P04191 - AT2A1_RABIT

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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

ATP2A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- 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. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).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. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi304 – 3041Calcium 2; via carbonyl oxygen
Metal bindingi305 – 3051Calcium 2; via carbonyl oxygen
Metal bindingi307 – 3071Calcium 2; via carbonyl oxygen
Metal bindingi309 – 3091Calcium 2
Active sitei351 – 35114-aspartylphosphate intermediate
Metal bindingi703 – 7031MagnesiumBy similarity
Metal bindingi707 – 7071MagnesiumBy similarity
Metal bindingi768 – 7681Calcium 1
Metal bindingi771 – 7711Calcium 1
Metal bindingi796 – 7961Calcium 2
Metal bindingi799 – 7991Calcium 1
Metal bindingi800 – 8001Calcium 1
Metal bindingi800 – 8001Calcium 2
Metal bindingi908 – 9081Calcium 1

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. calcium-transporting ATPase activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: UniProtKB
  2. calcium ion transmembrane transport Source: GOC
  3. calcium ion transport Source: UniProtKB
  4. negative regulation of striated muscle contraction Source: UniProtKB
  5. positive regulation of fast-twitch skeletal muscle fiber contraction Source: UniProtKB
  6. regulation of striated muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP04191.

Names & Taxonomyi

Protein namesi
Recommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (EC:3.6.3.8)
Short name:
SERCA1
Short name:
SR Ca(2+)-ATPase 1
Alternative name(s):
Calcium pump 1
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene namesi
Name:ATP2A1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum membrane Source: UniProtKB
  4. H zone Source: UniProtKB
  5. I band Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. membrane Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
  9. sarcoplasmic reticulum Source: BHF-UCL
  10. sarcoplasmic reticulum membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1PRO_0000046189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi876 ↔ 888

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP04191.

Expressioni

Tissue specificityi

Skeletal muscle, fast twitch muscle (type II) fibers.1 Publication

Developmental stagei

Isoform SERCA1A and isoform SERCA1B are predominantly found in adult and neonatal skeletal muscle respectively.1 Publication

Inductioni

Increased contractile activity leads to a decrease in SERCA1 expression, while decreased contractile activity leads to an increase in SERCA1 expression.

Interactioni

Subunit structurei

Associated with sarcolipin (SLN) (By similarity) and phospholamban (PLN).

Protein-protein interaction databases

IntActiP04191. 5 interactions.

Structurei

Secondary structure

1
1001
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Helixi9 – 168
Turni20 – 223
Helixi26 – 3611
Helixi49 – 546
Helixi55 – 573
Helixi60 – 7516
Beta strandi76 – 783
Beta strandi80 – 823
Helixi83 – 853
Beta strandi86 – 883
Helixi89 – 11123
Helixi115 – 1195
Helixi120 – 1223
Beta strandi125 – 1317
Beta strandi138 – 1414
Helixi142 – 1443
Beta strandi150 – 1545
Beta strandi161 – 1688
Beta strandi170 – 1723
Beta strandi173 – 1764
Helixi178 – 1814
Beta strandi187 – 1893
Helixi201 – 2033
Beta strandi213 – 2164
Beta strandi218 – 2258
Helixi227 – 2293
Helixi231 – 24010
Helixi248 – 27326
Helixi274 – 2807
Beta strandi283 – 2864
Helixi288 – 30619
Helixi311 – 32818
Beta strandi331 – 3344
Helixi338 – 3436
Beta strandi347 – 3526
Turni353 – 3553
Beta strandi362 – 37312
Beta strandi376 – 3849
Beta strandi387 – 3915
Beta strandi395 – 3973
Beta strandi400 – 4023
Helixi404 – 4063
Helixi408 – 41912
Beta strandi424 – 4285
Turni429 – 4324
Beta strandi433 – 4386
Helixi440 – 45213
Beta strandi460 – 4623
Turni464 – 4663
Helixi467 – 4693
Helixi470 – 4789
Beta strandi479 – 48810
Turni489 – 4924
Beta strandi493 – 50210
Helixi503 – 5086
Beta strandi511 – 5166
Helixi518 – 5236
Beta strandi525 – 5306
Beta strandi533 – 5364
Helixi539 – 55416
Turni555 – 5573
Beta strandi560 – 56910
Helixi573 – 5753
Helixi581 – 5833
Helixi584 – 5874
Beta strandi590 – 60011
Helixi607 – 61610
Beta strandi620 – 6278
Helixi629 – 63810
Beta strandi640 – 6423
Turni649 – 6513
Beta strandi652 – 6543
Helixi655 – 6595
Helixi663 – 67210
Beta strandi675 – 6784
Helixi683 – 69210
Turni693 – 6953
Beta strandi698 – 7025
Helixi705 – 7073
Helixi708 – 7136
Beta strandi716 – 7205
Helixi725 – 7295
Beta strandi732 – 7354
Helixi740 – 78041
Helixi789 – 7979
Turni798 – 8003
Helixi801 – 8077
Helixi816 – 8183
Beta strandi824 – 8263
Helixi831 – 85525
Turni856 – 8583
Beta strandi860 – 8623
Turni866 – 8683
Helixi870 – 8723
Helixi873 – 8753
Beta strandi876 – 8794
Turni880 – 8823
Beta strandi884 – 8863
Helixi890 – 8923
Helixi894 – 91320
Beta strandi916 – 9194
Turni922 – 9243
Helixi927 – 9293
Helixi931 – 94919
Helixi952 – 9565
Helixi964 – 97411
Helixi976 – 99015

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQUmodel-A1-993[»]
1IWOX-ray3.10A/B1-994[»]
1KJUelectron microscopy6.00A1-994[»]
1SU4X-ray2.40A1-994[»]
1T5SX-ray2.60A1-993[»]
1T5TX-ray2.90A1-993[»]
1VFPX-ray2.90A/B1-994[»]
1WPGX-ray2.30A/B/C/D1-993[»]
1XP5X-ray3.00A1-993[»]
2AGVX-ray2.40A/B1-993[»]
2BY4X-ray3.30A1-993[»]
2C88X-ray3.10A1-993[»]
2C8KX-ray2.80A1-993[»]
2C8LX-ray3.10A1-993[»]
2C9MX-ray3.00A/B1-993[»]
2DQSX-ray2.50A1-993[»]
2EARX-ray3.10A1-993[»]
2EASX-ray3.40A1-993[»]
2EATX-ray2.90A1-993[»]
2EAUX-ray2.80A1-993[»]
2O9JX-ray2.65A1-993[»]
2OA0X-ray3.40A1-993[»]
2VOYelectron microscopy18.00B36-77[»]
C967-988[»]
D832-854[»]
E86-115[»]
G243-278[»]
H289-336[»]
K749-780[»]
L789-809[»]
2YFYX-ray3.10A1-993[»]
2ZBDX-ray2.40A1-993[»]
2ZBEX-ray3.80A/B1-993[»]
2ZBFX-ray2.40A1-993[»]
2ZBGX-ray2.55A1-993[»]
3AR2X-ray2.50A1-994[»]
3AR3X-ray2.30A1-994[»]
3AR4X-ray2.15A1-994[»]
3AR5X-ray2.20A1-994[»]
3AR6X-ray2.20A1-994[»]
3AR7X-ray2.15A1-994[»]
3AR8X-ray2.60A1-994[»]
3AR9X-ray2.60A1-994[»]
3B9BX-ray2.65A1-993[»]
3B9RX-ray3.00A/B1-993[»]
3BA6X-ray2.80A1-993[»]
3FGOX-ray2.50A/B1-994[»]
3FPBX-ray2.55A1-994[»]
3FPSX-ray3.20A1-994[»]
3N5KX-ray2.20A/B1-994[»]
3N8GX-ray2.58A1-993[»]
3W5AX-ray3.01A/B1-993[»]
3W5BX-ray3.20A1-993[»]
3W5CX-ray2.50A1-993[»]
3W5DX-ray2.45A1-993[»]
4BEWX-ray2.50A/B1-994[»]
4H1WX-ray3.10A1-993[»]
4J2TX-ray3.20A1-993[»]
4KYTX-ray2.83A1-993[»]
4NABX-ray3.50A1-993[»]
ProteinModelPortaliP04191.
SMRiP04191. Positions 1-993.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04191.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848CytoplasmicAdd
BLAST
Topological domaini70 – 8920LumenalAdd
BLAST
Topological domaini111 – 253143CytoplasmicAdd
BLAST
Topological domaini274 – 29522LumenalAdd
BLAST
Topological domaini314 – 757444CytoplasmicAdd
BLAST
Topological domaini778 – 78710Lumenal
Topological domaini809 – 82820CytoplasmicAdd
BLAST
Topological domaini852 – 89746LumenalAdd
BLAST
Topological domaini918 – 93013CytoplasmicAdd
BLAST
Topological domaini950 – 96415LumenalAdd
BLAST
Topological domaini986 – 100116CytoplasmicAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei49 – 6921Helical; Name=1Add
BLAST
Transmembranei90 – 11021Helical; Name=2Add
BLAST
Transmembranei254 – 27320Helical; Name=3Add
BLAST
Transmembranei296 – 31318Helical; Name=4Add
BLAST
Transmembranei758 – 77720Helical; Name=5Add
BLAST
Transmembranei788 – 80821Helical; Name=6Add
BLAST
Transmembranei829 – 85123Helical; Name=7Add
BLAST
Transmembranei898 – 91720Helical; Name=8Add
BLAST
Transmembranei931 – 94919Helical; Name=9Add
BLAST
Transmembranei965 – 98521Helical; Name=10Add
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 40031Interacts with phospholamban 1Add
BLAST
Regioni788 – 80821Interacts with phospholamban 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
HOVERGENiHBG105648.
InParanoidiP04191.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR005782. 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]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform SERCA1B (identifier: P04191-1) [UniParc]FASTAAdd to Basket

Also known as: Neonatal

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
MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI
160 170 180 190 200
VEVAVGDKVP ADIRILSIKS TTLRVDQSIL TGESVSVIKH TEPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAL GIVATTGVST EIGKIRDQMA ATEQDKTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCKMFIID KVDGDFCSLN EFSITGSTYA PEGEVLKNDK
410 420 430 440 450
PIRSGQFDGL VELATICALC NDSSLDFNET KGVYEKVGEA TETALTTLVE
460 470 480 490 500
KMNVFNTEVR NLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP
510 520 530 540 550
AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPMTGP VKEKILSVIK
560 570 580 590 600
EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML
610 620 630 640 650
DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD
660 670 680 690 700
RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM
710 720 730 740 750
TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG
760 770 780 790 800
RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD
810 820 830 840 850
GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG
860 870 880 890 900
AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA
910 920 930 940 950
LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV
960 970 980 990 1000
DPLPMIFKLK ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR

K
Length:1,001
Mass (Da):110,459
Last modified:March 20, 1987 - v1
Checksum:i1F0D8C36CF975266
GO
Isoform SERCA1A (identifier: P04191-2) [UniParc]FASTAAdd to Basket

Also known as: Adult

The sequence of this isoform differs from the canonical sequence as follows:
     994-1001: DPEDERRK → G

Show »
Length:994
Mass (Da):109,490
Checksum:i148C462A8653A3E5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei994 – 10018DPEDERRK → G in isoform SERCA1A. 1 PublicationVSP_000356

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12898 mRNA. Translation: AAA31165.1.
M15351 mRNA. Translation: AAA31166.1.
M15158 mRNA. Translation: AAA31167.1.
PIRiA01075. PWRBFC.
RefSeqiNP_001082787.1. NM_001089318.1. [P04191-1]
UniGeneiOcu.1829.
Ocu.6937.

Genome annotation databases

GeneIDi100037716.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12898 mRNA. Translation: AAA31165.1 .
M15351 mRNA. Translation: AAA31166.1 .
M15158 mRNA. Translation: AAA31167.1 .
PIRi A01075. PWRBFC.
RefSeqi NP_001082787.1. NM_001089318.1. [P04191-1 ]
UniGenei Ocu.1829.
Ocu.6937.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FQU model - A 1-993 [» ]
1IWO X-ray 3.10 A/B 1-994 [» ]
1KJU electron microscopy 6.00 A 1-994 [» ]
1SU4 X-ray 2.40 A 1-994 [» ]
1T5S X-ray 2.60 A 1-993 [» ]
1T5T X-ray 2.90 A 1-993 [» ]
1VFP X-ray 2.90 A/B 1-994 [» ]
1WPG X-ray 2.30 A/B/C/D 1-993 [» ]
1XP5 X-ray 3.00 A 1-993 [» ]
2AGV X-ray 2.40 A/B 1-993 [» ]
2BY4 X-ray 3.30 A 1-993 [» ]
2C88 X-ray 3.10 A 1-993 [» ]
2C8K X-ray 2.80 A 1-993 [» ]
2C8L X-ray 3.10 A 1-993 [» ]
2C9M X-ray 3.00 A/B 1-993 [» ]
2DQS X-ray 2.50 A 1-993 [» ]
2EAR X-ray 3.10 A 1-993 [» ]
2EAS X-ray 3.40 A 1-993 [» ]
2EAT X-ray 2.90 A 1-993 [» ]
2EAU X-ray 2.80 A 1-993 [» ]
2O9J X-ray 2.65 A 1-993 [» ]
2OA0 X-ray 3.40 A 1-993 [» ]
2VOY electron microscopy 18.00 B 36-77 [» ]
C 967-988 [» ]
D 832-854 [» ]
E 86-115 [» ]
G 243-278 [» ]
H 289-336 [» ]
K 749-780 [» ]
L 789-809 [» ]
2YFY X-ray 3.10 A 1-993 [» ]
2ZBD X-ray 2.40 A 1-993 [» ]
2ZBE X-ray 3.80 A/B 1-993 [» ]
2ZBF X-ray 2.40 A 1-993 [» ]
2ZBG X-ray 2.55 A 1-993 [» ]
3AR2 X-ray 2.50 A 1-994 [» ]
3AR3 X-ray 2.30 A 1-994 [» ]
3AR4 X-ray 2.15 A 1-994 [» ]
3AR5 X-ray 2.20 A 1-994 [» ]
3AR6 X-ray 2.20 A 1-994 [» ]
3AR7 X-ray 2.15 A 1-994 [» ]
3AR8 X-ray 2.60 A 1-994 [» ]
3AR9 X-ray 2.60 A 1-994 [» ]
3B9B X-ray 2.65 A 1-993 [» ]
3B9R X-ray 3.00 A/B 1-993 [» ]
3BA6 X-ray 2.80 A 1-993 [» ]
3FGO X-ray 2.50 A/B 1-994 [» ]
3FPB X-ray 2.55 A 1-994 [» ]
3FPS X-ray 3.20 A 1-994 [» ]
3N5K X-ray 2.20 A/B 1-994 [» ]
3N8G X-ray 2.58 A 1-993 [» ]
3W5A X-ray 3.01 A/B 1-993 [» ]
3W5B X-ray 3.20 A 1-993 [» ]
3W5C X-ray 2.50 A 1-993 [» ]
3W5D X-ray 2.45 A 1-993 [» ]
4BEW X-ray 2.50 A/B 1-994 [» ]
4H1W X-ray 3.10 A 1-993 [» ]
4J2T X-ray 3.20 A 1-993 [» ]
4KYT X-ray 2.83 A 1-993 [» ]
4NAB X-ray 3.50 A 1-993 [» ]
ProteinModelPortali P04191.
SMRi P04191. Positions 1-993.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P04191. 5 interactions.

Chemistry

BindingDBi P04191.
ChEMBLi CHEMBL4693.

Proteomic databases

PRIDEi P04191.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100037716.

Organism-specific databases

CTDi 487.

Phylogenomic databases

eggNOGi COG0474.
HOVERGENi HBG105648.
InParanoidi P04191.

Enzyme and pathway databases

SABIO-RK P04191.

Miscellaneous databases

EvolutionaryTracei P04191.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi 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 ]
Pfami PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
PR00120. HATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
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Publicationsi

  1. "Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences."
    Brandl C.J., Green N.M., Korczak B., McLennan D.H.
    Cell 44:597-607(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA1B).
  2. "Involvement of an arginyl residue in the nucleotide-binding site of Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal."
    Corbalan-Garcia S., Teruel J.A., Gomez-Fernandez J.C.
    Biochem. J. 318:179-185(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 134-140 AND 490-495.
  3. "Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling."
    Andersen J.P., Vilsen B., Collins J.H., Jorgensen P.L.
    J. Membr. Biol. 93:85-92(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 199-212; 335-348 AND 506-519.
  4. "Chemical modification of the Ca(2+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum: identification of sites labeled with aryl isothiocyanates and thiol-directed conformational probes."
    Wawrzynow A., Collins J.H.
    Biochim. Biophys. Acta 1203:60-70(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 335-365; 468-476; 493-502; 513-529; 606-615; 630-637 AND 668-671.
  5. "Interaction of 4-azido-2-nitrophenyl phosphate, a pseudosubstrate, with the sarcoplasmic reticulum Ca-ATPase."
    Lacapere J.J., Garin J.
    Biochemistry 33:2586-2593(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 506-513 AND 584-591.
  6. "Adult forms of the Ca2+ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle."
    Brandl C.J., Deleon S., Martin D.R., McLennan D.H.
    J. Biol. Chem. 262:3768-3774(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1001 (ISOFORMS SERCA1A AND SERCA1B), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution."
    Toyoshima C., Nakasako M., Nomura H., Ogawa H.
    Nature 405:647-655(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ISOFORM SERCA1A.
  8. "Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban."
    Toyofuku T., Kurzydlowski K., Tada M., McLennan D.H.
    J. Biol. Chem. 268:2809-2815(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHOSPHOLAMBAN.
  9. "Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites."
    Asahi M., Kimura Y., Kurzydlowski K., Tada M., McLennan D.H.
    J. Biol. Chem. 274:32855-32862(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHOSPHOLAMBAN.

Entry informationi

Entry nameiAT2A1_RABIT
AccessioniPrimary (citable) accession number: P04191
Secondary accession number(s): P11719
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: October 29, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

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