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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

ATP2A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key regulator of striated muscle performance by acting as the major Ca2+ ATPase responsible for the reuptake of cytosolic Ca2+ into the sarcoplasmic reticulum. 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

Catalytic activityi

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

Enzyme regulationi

Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (PubMed:10551848, PubMed:8428955). Inhibited by phospholamban (PLN) (PubMed:10551848, PubMed:8428955). Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (PubMed:10551848, PubMed:8428955). Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium (PubMed:10551848, PubMed:8428955). This inhibition is regulated by the phosphorylation of PLN (PubMed:10551848, PubMed:8428955). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi304Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi305Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi307Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi309Calcium 2Combined sources1 Publication1
Active sitei3514-aspartylphosphate intermediate1 Publication1
Metal bindingi703MagnesiumBy similarity1
Metal bindingi707MagnesiumBy similarity1
Metal bindingi768Calcium 1Combined sources1 Publication1
Metal bindingi771Calcium 1Combined sources1 Publication1
Metal bindingi796Calcium 2Combined sources1 Publication1
Metal bindingi799Calcium 1Combined sources1 Publication1
Metal bindingi800Calcium 1Combined sources1 Publication1
Metal bindingi800Calcium 2Combined sources1 Publication1
Metal bindingi908Calcium 1Combined sources1 Publication1

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • calcium-transporting ATPase activity Source: UniProtKB

GO - Biological processi

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

BRENDAi3.6.3.8. 1749.
SABIO-RKP04191.

Protein family/group databases

TCDBi3.A.3.2.43. the p-type atpase (p-atpase) superfamily.

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
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 48CytoplasmicAdd BLAST48
Transmembranei49 – 69Helical; Name=1Add BLAST21
Topological domaini70 – 89LumenalAdd BLAST20
Transmembranei90 – 110Helical; Name=2Add BLAST21
Topological domaini111 – 253CytoplasmicAdd BLAST143
Transmembranei254 – 273Helical; Name=3Add BLAST20
Topological domaini274 – 295LumenalAdd BLAST22
Transmembranei296 – 313Helical; Name=4Add BLAST18
Topological domaini314 – 757CytoplasmicAdd BLAST444
Transmembranei758 – 777Helical; Name=5Add BLAST20
Topological domaini778 – 787Lumenal10
Transmembranei788 – 808Helical; Name=6Add BLAST21
Topological domaini809 – 828CytoplasmicAdd BLAST20
Transmembranei829 – 851Helical; Name=7Add BLAST23
Topological domaini852 – 897LumenalAdd BLAST46
Transmembranei898 – 917Helical; Name=8Add BLAST20
Topological domaini918 – 930CytoplasmicAdd BLAST13
Transmembranei931 – 949Helical; Name=9Add BLAST19
Topological domaini950 – 964LumenalAdd BLAST15
Transmembranei965 – 985Helical; Name=10Add BLAST21
Topological domaini986 – 1001CytoplasmicAdd BLAST16

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • H zone Source: UniProtKB
  • I band Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000461891 – 1001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1Add BLAST1001

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei441PhosphothreonineBy similarity1
Modified residuei569PhosphothreonineBy similarity1
Modified residuei581PhosphoserineBy similarity1
Disulfide bondi876 ↔ 8881 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiP04191.

PTM databases

SwissPalmiP04191.

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

Interacts with sarcolipin (SLN) (By similarity). Interacts with phospholamban (PLN) (PubMed:10551848, PubMed:8428955). Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF (By similarity).By similarity2 Publications

Protein-protein interaction databases

IntActiP04191. 5 interactors.
STRINGi9986.ENSOCUP00000002327.

Chemistry databases

BindingDBiP04191.

Structurei

Secondary structure

11001
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 – 54Combined sources6
Helixi55 – 57Combined sources3
Helixi60 – 75Combined sources16
Beta strandi76 – 78Combined sources3
Beta strandi80 – 82Combined sources3
Helixi83 – 85Combined sources3
Beta strandi86 – 88Combined sources3
Helixi89 – 111Combined sources23
Helixi115 – 119Combined sources5
Helixi120 – 122Combined sources3
Beta strandi125 – 131Combined sources7
Beta strandi138 – 141Combined sources4
Helixi142 – 144Combined sources3
Beta strandi150 – 154Combined sources5
Beta strandi161 – 168Combined sources8
Beta strandi170 – 172Combined sources3
Beta strandi173 – 176Combined sources4
Helixi178 – 181Combined sources4
Beta strandi187 – 189Combined sources3
Helixi201 – 203Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi218 – 225Combined sources8
Helixi227 – 229Combined sources3
Helixi231 – 240Combined sources10
Helixi248 – 273Combined sources26
Helixi274 – 280Combined sources7
Beta strandi283 – 286Combined sources4
Helixi288 – 306Combined sources19
Helixi311 – 328Combined sources18
Beta strandi331 – 334Combined sources4
Helixi338 – 343Combined sources6
Beta strandi347 – 352Combined sources6
Turni353 – 355Combined sources3
Beta strandi362 – 373Combined sources12
Beta strandi376 – 384Combined sources9
Beta strandi387 – 391Combined sources5
Beta strandi395 – 397Combined sources3
Beta strandi400 – 402Combined sources3
Helixi404 – 406Combined sources3
Helixi408 – 419Combined sources12
Beta strandi424 – 428Combined sources5
Turni429 – 432Combined sources4
Beta strandi433 – 438Combined sources6
Helixi440 – 452Combined sources13
Beta strandi460 – 462Combined sources3
Turni464 – 466Combined sources3
Helixi467 – 469Combined sources3
Helixi470 – 478Combined sources9
Beta strandi479 – 488Combined sources10
Turni489 – 492Combined sources4
Beta strandi493 – 502Combined sources10
Helixi503 – 508Combined sources6
Beta strandi511 – 516Combined sources6
Helixi518 – 523Combined sources6
Beta strandi525 – 530Combined sources6
Beta strandi533 – 536Combined sources4
Helixi539 – 554Combined sources16
Turni555 – 557Combined sources3
Beta strandi560 – 569Combined sources10
Helixi573 – 575Combined sources3
Helixi581 – 583Combined sources3
Helixi584 – 587Combined sources4
Beta strandi590 – 600Combined sources11
Helixi607 – 616Combined sources10
Beta strandi620 – 627Combined sources8
Helixi629 – 638Combined sources10
Beta strandi640 – 642Combined sources3
Beta strandi644 – 646Combined sources3
Turni649 – 651Combined sources3
Beta strandi652 – 654Combined sources3
Helixi655 – 659Combined sources5
Helixi663 – 672Combined sources10
Beta strandi675 – 678Combined sources4
Helixi683 – 692Combined sources10
Turni693 – 695Combined sources3
Beta strandi698 – 702Combined sources5
Helixi705 – 707Combined sources3
Helixi708 – 713Combined sources6
Beta strandi716 – 720Combined sources5
Helixi725 – 729Combined sources5
Beta strandi732 – 735Combined sources4
Helixi740 – 780Combined sources41
Helixi789 – 797Combined sources9
Turni798 – 800Combined sources3
Helixi801 – 807Combined sources7
Helixi816 – 818Combined sources3
Beta strandi824 – 826Combined sources3
Helixi831 – 855Combined sources25
Turni856 – 858Combined sources3
Beta strandi860 – 862Combined sources3
Turni866 – 868Combined sources3
Helixi870 – 872Combined sources3
Helixi873 – 875Combined sources3
Beta strandi876 – 879Combined sources4
Turni880 – 882Combined sources3
Beta strandi884 – 886Combined sources3
Helixi890 – 892Combined sources3
Helixi894 – 913Combined sources20
Beta strandi916 – 919Combined sources4
Turni922 – 924Combined sources3
Helixi927 – 929Combined sources3
Helixi931 – 949Combined sources19
Helixi952 – 956Combined sources5
Helixi964 – 974Combined sources11
Helixi976 – 990Combined sources15
Turni991 – 993Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3J7Telectron microscopy3.40A1-994[»]
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[»]
4UU0X-ray2.50A1-993[»]
4UU1X-ray2.80A1-993[»]
4XOUX-ray2.80A1-993[»]
4Y3UX-ray3.51A1-993[»]
4YCLX-ray3.25A1-993[»]
4YCMX-ray3.20A2-993[»]
4YCNX-ray3.50A2-993[»]
5A3QX-ray3.05A1-993[»]
5A3RX-ray3.05A1-993[»]
5A3SX-ray3.30A/B1-993[»]
ProteinModelPortaliP04191.
SMRiP04191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04191.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 400Interaction with phospholamban 11 PublicationAdd BLAST31
Regioni788 – 808Interaction with phospholamban 21 PublicationAdd BLAST21

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
HOVERGENiHBG105648.
InParanoidiP04191.
KOiK05853.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030332. SERCA1.
[Graphical view]
PANTHERiPTHR24093:SF335. PTHR24093:SF335. 2 hits.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF08282. Hydrolase_3. 1 hit.
[Graphical view]
PRINTSiPR00120. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000356994 – 1001DPEDERRK → G in isoform SERCA1A. 1 Publication8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGiocu:100037716.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3J7Telectron microscopy3.40A1-994[»]
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[»]
4UU0X-ray2.50A1-993[»]
4UU1X-ray2.80A1-993[»]
4XOUX-ray2.80A1-993[»]
4Y3UX-ray3.51A1-993[»]
4YCLX-ray3.25A1-993[»]
4YCMX-ray3.20A2-993[»]
4YCNX-ray3.50A2-993[»]
5A3QX-ray3.05A1-993[»]
5A3RX-ray3.05A1-993[»]
5A3SX-ray3.30A/B1-993[»]
ProteinModelPortaliP04191.
SMRiP04191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04191. 5 interactors.
STRINGi9986.ENSOCUP00000002327.

Chemistry databases

BindingDBiP04191.
ChEMBLiCHEMBL4693.

Protein family/group databases

TCDBi3.A.3.2.43. the p-type atpase (p-atpase) superfamily.

PTM databases

SwissPalmiP04191.

Proteomic databases

PRIDEiP04191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100037716.
KEGGiocu:100037716.

Organism-specific databases

CTDi487.

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
HOVERGENiHBG105648.
InParanoidiP04191.
KOiK05853.

Enzyme and pathway databases

BRENDAi3.6.3.8. 1749.
SABIO-RKP04191.

Miscellaneous databases

EvolutionaryTraceiP04191.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030332. SERCA1.
[Graphical view]
PANTHERiPTHR24093:SF335. PTHR24093:SF335. 2 hits.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF08282. Hydrolase_3. 1 hit.
[Graphical view]
PRINTSiPR00120. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 163 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.