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P19483

- ATPA_BOVIN

UniProt

P19483 - ATPA_BOVIN

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Protein

ATP synthase subunit alpha, mitochondrial

Gene
ATP5A1, ATP5A2
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.UniRule annotation

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  4. 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; Peripheral membrane protein; Extracellular side By similarity
Note: Colocalizes with HRG on the cell surface of T-cells By similarity.UniRule annotation

GO - Cellular componenti

  1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  2. plasma membrane Source: UniProtKB-SubCell
  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, mitochondrialUniRule annotationPRO_0000002423Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity.UniRule annotation

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.1 Publication

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP19483.
SMRiP19483. Positions 59-553.

Miscellaneous databases

EvolutionaryTraceiP19483.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
HOGENOMiHOG000130111.
InParanoidiP19482.
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

MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE    50
VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 100
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV 150
VDALGNAIDG KGPIGSKARR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 200
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 250
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 300
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 350
RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 400
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 450
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 500
PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL KEIVTNFLAG 550
FEA 553
Length:553
Mass (Da):59,720
Last modified:February 1, 1991 - v1
Checksum:i188E9531B3B815E0
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 [» ]
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 P19482.
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: September 3, 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

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