Reviewed, UniProtKB/Swiss-Prot P38078 (VATA_CANTR)

Names and origin

Protein names

Recommended name:
    V-type proton ATPase catalytic subunit A
      Short name=V-ATPase subunit A
    EC=3.6.3.14
Alternative name(s):
    Vacuolar proton pump subunit A
Cleaved into the following chain:
    1- Recommended name:
            Endonuclease PI-CtrI
              EC=3.1.-.-
        Alternative name(s):
            VMA1-derived endonuclease
              Short name=VDE
            Ctr VMA intein

Gene names

Name:

VMA1

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1088 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca2+ homeostasis. This is a catalytic subunit. VDE is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it By similarity.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out).
Subunit structure	V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).
Subcellular location	Endomembrane system. Note: Membranes of various intracellular acidic compartments.
Post-translational modification	This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
Sequence similarities	Belongs to the ATPase alpha/beta chains family. Contains 1 DOD-type homing endonuclease domain.

Ontologies

Keywords
Biological process	Hydrogen ion transport Intron homing Ion transport Transport
Cellular component	Membrane
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Autocatalytic cleavage Protein splicing
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro intein-mediated protein splicing Inferred from electronic annotation. Source: InterPro intron homing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting two-sector ATPase complex, catalytic domain Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	V-type proton ATPase catalytic subunit A, 1st part		PRO_0000002455
	Chain	284 – 754	471	Endonuclease PI-CtrI		PRO_0000002456
	Chain	755 – 1088	334	V-type proton ATPase catalytic subunit A, 2nd part		PRO_0000002457
Regions
	Domain	485 – 662	178	DOD-type homing endonuclease
	Nucleotide binding	257 – 264	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38078-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 77258751E455B62A	FASTA	1,088	119,154
	10 20 30 40 50 60 MAGALENARK EIKRLSLDDT NESQYGQIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE 70 80 90 100 110 120 VIRINGDKAT IQVYEETAGV TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKDES 130 140 150 160 170 180 QSIYIPRGID VPALSRTVQY DFTPGQLKVG DHITGGDIFG SIYENSLLDD HKILLPPRAR 190 200 210 220 230 240 GTITSIAEAG SYNVEEPVLE VEFDGKKHKY SMMHTWPVRV PRPVAEKLTA DHPLLTGQRV 250 260 270 280 290 300 LDSLFPCVQG GTTCIPGAFG CGKTVISQSL SKFSNSDVII YVGCFTKGTQ VMMADGADKS 310 320 330 340 350 360 IESIEVGDKV MGKDGMPREV VGLPRGYDDM YKVRQLSSTR RNAKSEGLMD FTVSADHKLI 370 380 390 400 410 420 LKTKQDVKIA TRKIGGNTYT GVTFYVLEKT KTGIELVKAK TKVFGHHIHG QNGAEEKAAT 430 440 450 460 470 480 FAAGIDSKEY IDWIIEARDY VQVDEIVKTS TTQMINPVHF ESGKLGNWLH EHKQNKSLAP 490 500 510 520 530 540 QLGYLLGTWA GIGNVKSSAF TMNSKDDVKL ATRIMNYSSK LGMTCSSTES GELNVAENEE 550 560 570 580 590 600 EFFNNLGAEK DEAGDFTFDE FTDAMDELTI NVHGAAASKK NNLLWNALKS LGFRAKSTDI 610 620 630 640 650 660 VKSIPQHIAV DDIVVRESLI AGLVDAAGNV ETKSNGSIEA VVRTSFRHVA RGLVKIAHSL 670 680 690 700 710 720 GIESSINIKD THIDAAGVRQ EFACIVNLTG APLAGVLSKC ALARNQTPVV KFTRDPVLFN 730 740 750 760 770 780 FDLIKSAKEN YYGITLAEET DHQFLLSNMA LVHNCGERGN EMAEVLMEFP ELFTEISGRK 790 800 810 820 830 840 EPIMKRTTLV ANTSNMPVAA REASIYTGIT LAEYFRDQGK NVSMIADSSS RWAEALREIS 850 860 870 880 890 900 GRLGEMPADQ GFPAYLGAKL ASFYERAGKA TALGSPDRVG SVSIVAAVSP AGGDFSDPVT 910 920 930 940 950 960 TSTLGITQVF WGLDKKLAQR KHFPSINTSV SYSKYTNVLN KYYDSNYPEF PQLRDKIREI 970 980 990 1000 1010 1020 LSNAEELEQV VQLVGKSALS DSDKITLDVA TLIKEDFLQQ NGYSSYDAFC PIWKTFDMMR 1030 1040 1050 1060 1070 1080 AFISYYDEAQ KAIANGAQWS KLAESTSDVK HAVSSAKFFE PSRGQKEGEK EFGDLLTTIS ERFAEASE

References

[1]	"Peptide splicing in the vacuolar ATPase subunit A from Candida tropicalis." Gu H.H., Xu J., Gallagher M., Dean G.E. J. Biol. Chem. 268:7372-7381(1993) [PubMed: 8463270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64984 Genomic DNA. Translation: AAB03895.1.
PIR	A46080.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.6.3.14. 1242.
Family and domain databases
InterPro	IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR003587. Hedgehog_hint_N. IPR007869. Hom_end. IPR007868. Hom_end_hint. IPR004042. Intein_endonuc. IPR006141. Intein_splicing_site. [Graphical view]
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. PF05204. Hom_end. 1 hit. PF05203. Hom_end_hint. 1 hit. [Graphical view]
SMART	SM00306. HintN. 1 hit. [Graphical view]
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. PS50818. INTEIN_C_TER. False negative. PS50819. INTEIN_ENDONUCLEASE. 1 hit. PS50817. INTEIN_N_TER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VATA_CANTR

Accession

Primary (citable) accession number: P38078

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 24, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)