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P19483

- ATPA_BOVIN

UniProt

P19483 - ATPA_BOVIN

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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5A1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei413 – 4131Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2198ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:ATP5A1
Synonyms:ATP5A2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Mitochondrion inner membrane By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
Note: Colocalizes with HRG on the cell surface of T-cells.By similarity

GO - Cellular componenti

  1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  2. plasma membrane Source: UniProtKB-KW
  3. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion1 PublicationAdd
BLAST
Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Pyrrolidone carboxylic acid
Modified residuei76 – 761PhosphoserineBy similarity
Glycosylationi76 – 761O-linked (GlcNAc)By similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
Modified residuei230 – 2301N6-succinyllysine; alternateBy similarity
Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei261 – 2611N6-acetyllysine; alternateBy similarity
Modified residuei261 – 2611N6-succinyllysine; alternateBy similarity
Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
Modified residuei427 – 4271N6-acetyllysine; alternateBy similarity
Modified residuei427 – 4271N6-succinyllysine; alternateBy similarity
Modified residuei434 – 4341N6-acetyllysineBy similarity
Modified residuei498 – 4981N6-acetyllysine; alternateBy similarity
Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
Modified residuei506 – 5061N6-acetyllysine; alternateBy similarity
Modified residuei506 – 5061N6-succinyllysine; alternateBy similarity
Modified residuei531 – 5311N6-acetyllysine; alternateBy similarity
Modified residuei531 – 5311N6-succinyllysine; alternateBy similarity
Modified residuei539 – 5391N6-acetyllysine; alternateBy similarity
Modified residuei539 – 5391N6-succinyllysine; alternateBy similarity
Modified residuei541 – 5411N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP19483.
PRIDEiP19483.

2D gel databases

UCD-2DPAGEP19483.

Expressioni

Tissue specificityi

Heart and liver.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with BLOC1S1. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency.3 Publications

Protein-protein interaction databases

DIPiDIP-35479N.
IntActiP19483. 4 interactions.
MINTiMINT-5006839.
STRINGi9913.ENSBTAP00000003259.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 608Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 788Combined sources
Beta strandi81 – 866Combined sources
Beta strandi95 – 984Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi114 – 1207Combined sources
Helixi122 – 1243Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi139 – 1435Combined sources
Helixi144 – 1463Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi187 – 1893Combined sources
Helixi194 – 1996Combined sources
Beta strandi209 – 2135Combined sources
Helixi218 – 22811Combined sources
Helixi230 – 2334Combined sources
Beta strandi234 – 2363Combined sources
Turni238 – 2403Combined sources
Beta strandi243 – 2508Combined sources
Helixi253 – 26513Combined sources
Helixi269 – 2713Combined sources
Beta strandi272 – 2776Combined sources
Helixi283 – 30220Combined sources
Beta strandi306 – 3127Combined sources
Helixi314 – 32714Combined sources
Helixi334 – 3363Combined sources
Helixi341 – 3499Combined sources
Beta strandi353 – 3553Combined sources
Helixi357 – 3593Combined sources
Beta strandi363 – 3719Combined sources
Beta strandi373 – 3753Combined sources
Helixi380 – 3889Combined sources
Beta strandi389 – 3957Combined sources
Helixi397 – 4026Combined sources
Turni410 – 4123Combined sources
Beta strandi414 – 4174Combined sources
Helixi418 – 4214Combined sources
Helixi424 – 44118Combined sources
Helixi444 – 4463Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 4533Combined sources
Helixi455 – 47016Combined sources
Helixi481 – 49212Combined sources
Turni493 – 4986Combined sources
Helixi501 – 5033Combined sources
Helixi504 – 51714Combined sources
Helixi520 – 52910Combined sources
Helixi534 – 55118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMFX-ray2.85A/B/C44-553[»]
1COWX-ray3.10A/B/C45-553[»]
1E1QX-ray2.61A/B/C44-553[»]
1E1RX-ray2.50A/B/C44-553[»]
1E79X-ray2.40A/B/C44-553[»]
1EFRX-ray3.10A/B/C45-553[»]
1H8EX-ray2.00A/B/C44-553[»]
1H8HX-ray2.90A/B/C44-553[»]
1NBMX-ray3.00A/B/C44-553[»]
1OHHX-ray2.80A/B/C44-553[»]
1QO1X-ray3.90A/B/C44-553[»]
1W0JX-ray2.20A/B/C44-553[»]
1W0KX-ray2.85A/B/C44-553[»]
2CK3X-ray1.90A/B/C44-553[»]
2JDIX-ray1.90A/B/C44-553[»]
2JIZX-ray2.30A/B/C/H/I/J44-553[»]
2JJ1X-ray2.70A/B/C/H/I/J44-553[»]
2JJ2X-ray2.40A/B/C/H/I/J44-553[»]
2JMXNMR-B44-68[»]
2V7QX-ray2.10A/B/C45-553[»]
2W6EX-ray6.50A/B/C1-553[»]
2W6FX-ray6.00A/B/C1-553[»]
2W6GX-ray6.00A/B/C1-553[»]
2W6HX-ray5.00A/B/C1-553[»]
2W6IX-ray4.00A/B/C1-553[»]
2W6JX-ray3.84A/B/C1-553[»]
2WSSX-ray3.20A/B/C/J/K/L44-553[»]
2XNDX-ray3.50A/B/C62-553[»]
4ASUX-ray2.60A/B/C44-553[»]
4TSFX-ray3.20A/B/C44-553[»]
4TT3X-ray3.21A/B/C44-553[»]
ProteinModelPortaliP19483.
SMRiP19483. Positions 59-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19483.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
HOGENOMiHOG000130111.
InParanoidiP19483.
KOiK02132.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19483-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE
60 70 80 90 100
VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV
160 170 180 190 200
VDALGNAIDG KGPIGSKARR RVGLKAPGII PRISVREPMQ TGIKAVDSLV
210 220 230 240 250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG
260 270 280 290 300
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
310 320 330 340 350
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
360 370 380 390 400
RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF
410 420 430 440 450
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG
460 470 480 490 500
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE
510 520 530 540 550
PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL KEIVTNFLAG

FEA
Length:553
Mass (Da):59,720
Last modified:February 1, 1991 - v1
Checksum:i188E9531B3B815E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41V → M in AAI16060. 1 PublicationCurated
Sequence conflicti6 – 61V → I in AAA30399. (PubMed:2896000)Curated
Sequence conflicti31 – 333IAA → VGT in AAA30399. (PubMed:2896000)Curated
Sequence conflicti41 – 411S → T in AAA30399. (PubMed:2896000)Curated
Sequence conflicti51 – 511V → M in AAA30399. (PubMed:2896000)Curated
Sequence conflicti144 – 1441E → D in AAA30399. (PubMed:2896000)Curated
Sequence conflicti164 – 1641I → V in AAA30399. (PubMed:2896000)Curated
Sequence conflicti168 – 1681A → I in AAA30399. (PubMed:2896000)Curated
Sequence conflicti358 – 3581A → S in AAA30399. (PubMed:2896000)Curated
Sequence conflicti524 – 5241S → G in AAI16060. 1 PublicationCurated
Sequence conflicti524 – 5241S → G AA sequence (PubMed:2864455)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22465 mRNA. Translation: AAB59266.1.
X64565 Genomic DNA. Translation: CAA45865.1.
BC116059 mRNA. Translation: AAI16060.1.
M19680 mRNA. Translation: AAA30399.1.
PIRiA27693.
S27201. PWBOA.
RefSeqiNP_777109.1. NM_174684.2.
UniGeneiBt.7194.

Genome annotation databases

GeneIDi282578.
KEGGibta:282578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22465 mRNA. Translation: AAB59266.1 .
X64565 Genomic DNA. Translation: CAA45865.1 .
BC116059 mRNA. Translation: AAI16060.1 .
M19680 mRNA. Translation: AAA30399.1 .
PIRi A27693.
S27201. PWBOA.
RefSeqi NP_777109.1. NM_174684.2.
UniGenei Bt.7194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BMF X-ray 2.85 A/B/C 44-553 [» ]
1COW X-ray 3.10 A/B/C 45-553 [» ]
1E1Q X-ray 2.61 A/B/C 44-553 [» ]
1E1R X-ray 2.50 A/B/C 44-553 [» ]
1E79 X-ray 2.40 A/B/C 44-553 [» ]
1EFR X-ray 3.10 A/B/C 45-553 [» ]
1H8E X-ray 2.00 A/B/C 44-553 [» ]
1H8H X-ray 2.90 A/B/C 44-553 [» ]
1NBM X-ray 3.00 A/B/C 44-553 [» ]
1OHH X-ray 2.80 A/B/C 44-553 [» ]
1QO1 X-ray 3.90 A/B/C 44-553 [» ]
1W0J X-ray 2.20 A/B/C 44-553 [» ]
1W0K X-ray 2.85 A/B/C 44-553 [» ]
2CK3 X-ray 1.90 A/B/C 44-553 [» ]
2JDI X-ray 1.90 A/B/C 44-553 [» ]
2JIZ X-ray 2.30 A/B/C/H/I/J 44-553 [» ]
2JJ1 X-ray 2.70 A/B/C/H/I/J 44-553 [» ]
2JJ2 X-ray 2.40 A/B/C/H/I/J 44-553 [» ]
2JMX NMR - B 44-68 [» ]
2V7Q X-ray 2.10 A/B/C 45-553 [» ]
2W6E X-ray 6.50 A/B/C 1-553 [» ]
2W6F X-ray 6.00 A/B/C 1-553 [» ]
2W6G X-ray 6.00 A/B/C 1-553 [» ]
2W6H X-ray 5.00 A/B/C 1-553 [» ]
2W6I X-ray 4.00 A/B/C 1-553 [» ]
2W6J X-ray 3.84 A/B/C 1-553 [» ]
2WSS X-ray 3.20 A/B/C/J/K/L 44-553 [» ]
2XND X-ray 3.50 A/B/C 62-553 [» ]
4ASU X-ray 2.60 A/B/C 44-553 [» ]
4TSF X-ray 3.20 A/B/C 44-553 [» ]
4TT3 X-ray 3.21 A/B/C 44-553 [» ]
ProteinModelPortali P19483.
SMRi P19483. Positions 59-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35479N.
IntActi P19483. 4 interactions.
MINTi MINT-5006839.
STRINGi 9913.ENSBTAP00000003259.

2D gel databases

UCD-2DPAGE P19483.

Proteomic databases

PaxDbi P19483.
PRIDEi P19483.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 282578.
KEGGi bta:282578.

Organism-specific databases

CTDi 498.

Phylogenomic databases

eggNOGi COG0056.
HOGENOMi HOG000130111.
InParanoidi P19483.
KOi K02132.

Miscellaneous databases

EvolutionaryTracei P19483.
NextBioi 20806299.

Family and domain databases

Gene3Di 2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01346. ATP_synth_alpha_bact.
InterProi IPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00962. atpA. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ATP synthase from bovine mitochondria: complementary DNA sequence of the import precursor of a heart isoform of the alpha subunit."
    Walker J.E., Powell S.J., Vinas O., Runswick M.J.
    Biochemistry 28:4702-4708(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Structural organization of a nuclear gene for the alpha-subunit of the bovine mitochondrial ATP synthase complex."
    Pierce D.J., Jordan E.M., Breen G.A.M.
    Biochim. Biophys. Acta 1132:265-275(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.
  4. "Bovine liver cDNA clones encoding a precursor of the alpha-subunit of the mitochondrial ATP synthase complex."
    Breen G.A.M.
    Biochem. Biophys. Res. Commun. 152:264-269(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-359.
    Tissue: Liver.
  5. "Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
    Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
    J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-552.
    Tissue: Heart.
  6. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
    Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
    FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  7. "Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
    Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
    Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  8. "The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
    Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
    Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  9. "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
    Orriss G.L., Leslie A.G., Braig K., Walker J.E.
    Structure 6:831-837(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  10. "The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
    Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
    Nat. Struct. Biol. 10:744-750(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATPIF1; ATP5B AND ATP5C1.
  11. "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
    Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
    Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 45-553 IN COMPLEX WITH ATPIF1; ATP5B; ATP5C1; ATP5D AND ATP5E.

Entry informationi

Entry nameiATPA_BOVIN
AccessioniPrimary (citable) accession number: P19483
Secondary accession number(s): P05629, P19482, Q1JQC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 149 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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