P19483 (ATPA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha, mitochondrial

Gene names

Name:	ATP5A1
Synonyms:	ATP5A2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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) By similarity.
Subcellular location	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.
Tissue specificity	Heart and liver.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell membrane Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 43

43

Mitochondrion Ref.5

Chain

44 – 553

510

ATP synthase subunit alpha, mitochondrial

PRO_0000002423

Regions

Nucleotide binding

212 – 219

8

ATP By similarity

Sites

Site

413

1

Required for activity By similarity

Amino acid modifications

Modified residue

44

1

Pyrrolidone carboxylic acid

Modified residue

161

1

N6-acetyllysine By similarity

Modified residue

434

1

N6-acetyllysine By similarity

Modified residue

506

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

4

1

V → M in AAI16060. Ref.3

Sequence conflict

6

1

V → I in AAA30399. Ref.4

Sequence conflict

31 – 33

3

IAA → VGT in AAA30399. Ref.4

Sequence conflict

41

1

S → T in AAA30399. Ref.4

Sequence conflict

51

1

V → M in AAA30399. Ref.4

Sequence conflict

144

1

E → D in AAA30399. Ref.4

Sequence conflict

164

1

I → V in AAA30399. Ref.4

Sequence conflict

168

1

A → I in AAA30399. Ref.4

Sequence conflict

358

1

A → S in AAA30399. Ref.4

Sequence conflict

524

1

S → G in AAI16060. Ref.3

Sequence conflict

524

1

S → G AA sequence Ref.5

Secondary structure

1

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553

Helix Strand Turn

Details...

Turn

68 – 70

3

Beta strand

71 – 78

8

Beta strand

81 – 86

6

Beta strand

95 – 98

4

Beta strand

103 – 110

8

Beta strand

113 – 120

8

Helix

122 – 124

3

Beta strand

130 – 132

3

Beta strand

139 – 143

5

Helix

144 – 146

3

Beta strand

150 – 152

3

Beta strand

159 – 161

3

Beta strand

167 – 173

7

Helix

194 – 199

6

Beta strand

207 – 213

7

Helix

218 – 228

11

Helix

230 – 233

4

Helix

238 – 240

3

Beta strand

243 – 250

8

Helix

253 – 265

13

Helix

269 – 271

3

Beta strand

272 – 277

6

Helix

283 – 302

20

Beta strand

306 – 312

7

Helix

314 – 327

14

Helix

334 – 336

3

Helix

341 – 349

9

Beta strand

353 – 355

3

Helix

357 – 359

3

Beta strand

363 – 373

11

Helix

380 – 388

9

Beta strand

389 – 395

7

Helix

397 – 401

5

Turn

410 – 412

3

Beta strand

414 – 417

4

Helix

418 – 421

4

Helix

424 – 443

20

Helix

444 – 446

3

Helix

455 – 469

15

Helix

481 – 492

12

Turn

493 – 498

6

Helix

501 – 503

3

Helix

504 – 518

15

Helix

520 – 528

9

Helix

534 – 551

18

Sequences

	Sequence		Length	Mass (Da)
	P19483 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 188E9531B3B815E0	FASTA	553	59,720
	10 20 30 40 50 60 MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE VSSILEERIL 70 80 90 100 110 120 GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG 130 140 150 160 170 180 NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKARR RVGLKAPGII 190 200 210 220 230 240 PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK 250 260 270 280 290 300 KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 310 320 330 340 350 360 RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG 370 380 390 400 410 420 GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA 430 440 450 460 470 480 AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA 490 500 510 520 530 540 IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL 550 KEIVTNFLAG FEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2527557] [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: 1420306] [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: 2896000] [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: 2864455] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-552. Tissue: Heart.
[6]	"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: 8065448] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[7]	"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: 8790345] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[8]	"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: 9687365] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22465 mRNA. Translation: AAB59266.1.
X64565 Genomic DNA. Translation: CAA45865.1.
BC116059 mRNA. Translation: AAI16060.1.
M19680 mRNA. Translation: AAA30399.1.

IPI

IPI00694295.

PIR

A27693.
PWBOA. S27201.

RefSeq

NP_777109.1. NM_174684.2.

UniGene

Bt.7194.

3D structure databases

PDBe
RCSB PDB
PDBj

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	45-553	[»]
2JJ1	X-ray	2.70	A/B/C/H/I/J	45-553	[»]
2JJ2	X-ray	2.40	A/B/C/H/I/J	45-553	[»]
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	[»]

ProteinModelPortal

P19483.

SMR

P19483. Positions 59-553.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35479N.

IntAct

P19483. 3 interactions.

MINT

MINT-5006839.

STRING

P19483.

2D gel databases

UCD-2DPAGE

P19483.

Proteomic databases

PRIDE

P19483.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

282578.

KEGG

bta:282578.

Organism-specific databases

CTD

498.

Phylogenomic databases

GeneTree

ENSGT00550000074846.

InParanoid

P19483.

OrthoDB

EOG4ZCT48.

PhylomeDB

P19483.

Family and domain databases

InterPro

IPR020003. ATPase_a/bsu_AS.
IPR005294. ATPase_F1-cplx_asu.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]

Gene3D

G3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.

KO

K02132.

Pfam

PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.

TIGRFAMs

TIGR00962. AtpA. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATPA_BOVIN

Accession

Primary (citable) accession number: P19483
Secondary accession number(s): P05629, P19482, Q1JQC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	November 16, 2011
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program