A8HXL8 (A8HXL8_CHLRE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
ATP synthase gamma chain RuleBase RU004001

Gene names

Name:	ATPC EMBL EDP08312.1
ORF Names:	CHLREDRAFT_134235 EMBL EDP08312.1

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF0 complex By similarity. RuleBase RU004001
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 By similarity. RuleBase RU004001
Sequence similarities	Belongs to the ATPase gamma chain family. RuleBase RU004001

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport RuleBase RU004001 Ion transport Transport
Cellular component	CF(1) RuleBase RU004001
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A8HXL8 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 3E6685F60D6880C0	FASTA	358	38,761
	10 20 30 40 50 60 MAAMLASKQG AFMGRSSFAP APKGVASRGS LQVVAGLKEV RDRIASVKNT QKITDAMKLV 70 80 90 100 110 120 AAAKVRRAQE AVVNGRPFSE NLVKVLYGVN QRVRQEDVDS PLCAVRPVKS VLLVVLTGDR 130 140 150 160 170 180 GLCGGYNNFI IKKTEARYRE LTAMGVKVNL VCVGRKGAQY FARRKQYNIV KSFSLGAAPS 190 200 210 220 230 240 TKEAQGIADE IFASFIAQES DKVELVFTKF ISLINSNPTI QTLLPMTPMG ELCDVDGKCV 250 260 270 280 290 300 DAADDEIFKL TTKGGEFAVE REKTTIETEA LDPSLIFEQE PAQILDALLP LYMSSCLLRS 310 320 330 340 350 LQEALASELA ARMNAMNNAS DNAKELKKGL TVQYNKQRQA KITQELAEIV GGAAATSG

References

[1]

"The Chlamydomonas genome reveals the evolution of key animal and plant functions." Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P. , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R. Science 318:245-250(2007) [PubMed: 17932292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-503.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS496110 Genomic DNA. Translation: EDP08312.1.
RefSeq	XP_001696335.1. XM_001696283.1.
UniGene	Cre.13218.
3D structure databases
ProteinModelPortal	A8HXL8.
ModBase	Search...
Protein-protein interaction databases
STRING	A8HXL8.
Proteomic databases
PRIDE	A8HXL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	EDP08312; EDP08312; CHLREDRAFT_134235.
GeneID	5722055.
KEGG	cre:CHLREDRAFT_134235.
Phylogenomic databases
PhylomeDB	A8HXL8.
ProtClustDB	CLSN2679503.
Family and domain databases
HAMAP	MF_00815. ATP_synth_gamma_bact. [Tree]
InterPro	IPR000131. ATPase_F1-cplx_gsu. IPR023632. ATPase_F1_gsu_CS. IPR023633. ATPase_F1_gsu_dom. [Graphical view]
KO	K02115.
PANTHER	PTHR11693. ATPase_F1_gamma. 1 hit.
Pfam	PF00231. ATP-synt. 1 hit. [Graphical view]
PRINTS	PR00126. ATPASEGAMMA.
SUPFAM	SSF52943. ATPase_gamma. 1 hit.
TIGRFAMs	TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITE	PS00153. ATPASE_GAMMA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A8HXL8_CHLRE

Accession

Primary (citable) accession number: A8HXL8

Entry history

Integrated into UniProtKB/TrEMBL:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)