Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P04191

- AT2A1_RABIT

UniProt

P04191 - AT2A1_RABIT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848CytoplasmicAdd
BLAST
Transmembranei49 – 6921Helical; Name=1Add
BLAST
Topological domaini70 – 8920LumenalAdd
BLAST
Transmembranei90 – 11021Helical; Name=2Add
BLAST
Topological domaini111 – 253143CytoplasmicAdd
BLAST
Transmembranei254 – 27320Helical; Name=3Add
BLAST
Topological domaini274 – 29522LumenalAdd
BLAST
Transmembranei296 – 31318Helical; Name=4Add
BLAST
Topological domaini314 – 757444CytoplasmicAdd
BLAST
Transmembranei758 – 77720Helical; Name=5Add
BLAST
Topological domaini778 – 78710Lumenal
Transmembranei788 – 80821Helical; Name=6Add
BLAST
Topological domaini809 – 82820CytoplasmicAdd
BLAST
Transmembranei829 – 85123Helical; Name=7Add
BLAST
Topological domaini852 – 89746LumenalAdd
BLAST
Transmembranei898 – 91720Helical; Name=8Add
BLAST
Topological domaini918 – 93013CytoplasmicAdd
BLAST
Transmembranei931 – 94919Helical; Name=9Add
BLAST
Topological domaini950 – 96415LumenalAdd
BLAST
Transmembranei965 – 98521Helical; Name=10Add
BLAST
Topological domaini986 – 100116CytoplasmicAdd
BLAST

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4UU0X-ray2.50A1-993[»]
4UU1X-ray2.80A1-993[»]
ProteinModelPortaliP04191.
SMRiP04191. Positions 1-993.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04191.

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:
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.

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 .
PIRi A01075. PWRBFC.
RefSeqi NP_001082787.1. NM_001089318.1. [P04191-1 ]
UniGenei Ocu.1829.
Ocu.6937.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4UU0 X-ray 2.50 A 1-993 [» ]
4UU1 X-ray 2.80 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.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 146 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

Dasty 3