Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
CuratedUniProtKB
According to TCDB this is a transporter from family:
H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily 3.A.2.2.4
A cDNA encoding the 14-kDa subunit of vacuolar ATPase was cloned from human fetal brain. The sequence was composed of 680 nucleotides containing an open reading frame of 357 nucleotides. The deduced peptide sequence consisted of 119 amino acid residues with a calculated molecular weight of 13,369 Da and a pI of 5.19. Overall, this amino-acid sequence was respectively 69% and 70% identical to those of Manduca sexta and Drosophila melanogaster 14-kDa subunits, although the two representatives of Class Insecta were remarkably similar to one another (91% identity). Three regions in particular (the N-terminal, amino acids 5-36; the middle, residues 58-68; and the C-terminal, residues 88-118) were highly conserved. Hence, we think that the 14-kDa subunits have evolved from the same ancestral gene, and that the three conserved regions are important for the structure and function of vacuolar ATPase. A single 0.8-kb band was detected in various human tissues by Northern blot analysis. Since the human 14-kDa subunit is expressed ubiquitously, it might be a housekeeping protein. A separate transcript found in the cDNA library lacked a 6-bp segment in the 5' non-coding region (nucleotides -40 to -35) and also carried a 23C to T (8Thr to Ile) point mutation in the coding region; these minor differences likely reflected normal polymorphism.
A cDNA encoding the 14-kDa subunit of vacuolar ATPase was cloned from human fetal brain. The sequence was composed of 680 nucleotides containing an open reading frame of 357 nucleotides. The deduced peptide sequence consisted of 119 amino acid residues with a calculated molecular weight of 13,369 Da and a pI of 5.19. Overall, this amino-acid sequence was respectively 69% and 70% identical to those of Manduca sexta and Drosophila melanogaster 14-kDa subunits, although the two representatives of Class Insecta were remarkably similar to one another (91% identity). Three regions in particular (the N-terminal, amino acids 5-36; the middle, residues 58-68; and the C-terminal, residues 88-118) were highly conserved. Hence, we think that the 14-kDa subunits have evolved from the same ancestral gene, and that the three conserved regions are important for the structure and function of vacuolar ATPase. A single 0.8-kb band was detected in various human tissues by Northern blot analysis. Since the human 14-kDa subunit is expressed ubiquitously, it might be a housekeeping protein. A separate transcript found in the cDNA library lacked a 6-bp segment in the 5' non-coding region (nucleotides -40 to -35) and also carried a 23C to T (8Thr to Ile) point mutation in the coding region; these minor differences likely reflected normal polymorphism.
Hydrogen ion transporting ATP synthase activity, rotational mechanismdefinition[GO:0046933]‹silver
Catalysis of protons from one side of a membrane to the other according to the reaction: ADP + phosphate = ATP + H2O, coupled with transport of H+ down a concentration gradient, by a rotational mechanism.
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Evidence
1:
Inferred from Physical InteractionUniProtKB
The multi-subunit vacuolar-type H(+)-ATPase consists of a V(1) domain (A-H subunits) catalyzing ATP hydrolysis and a V(0) domain (a, c, c', c", d, e) responsible for H(+) translocation. The mammalian V(0) d subunit is one of the least-well characterized, and its function and position within the pump are still unclear. It has two different forms encoded by separate genes, d1 being ubiquitous while d2 is predominantly expressed at the cell surface in kidney and osteoclast. To determine whether it forms part of the pump's central stalk as suggested by bacterial A-ATPase studies, or is peripheral as hypothesized from a yeast model, we investigated both human d subunit isoforms. In silico structural modelling demonstrated that human d1 and d2 are structural orthologues of bacterial subunit C, despite poor sequence identity. Expression studies of d1 and d2 showed that each can pull down the central stalk's D and F subunits from human kidney membrane, and in vitro studies using D and F further showed that the interactions between these proteins and the d subunit is direct. These data indicate that the d subunit in man is centrally located within the pump and is thus important in its rotary mechanism.
Catalysis of the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.
The directed movement of protons (hydrogen ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
A cDNA encoding the 14-kDa subunit of vacuolar ATPase was cloned from human fetal brain. The sequence was composed of 680 nucleotides containing an open reading frame of 357 nucleotides. The deduced peptide sequence consisted of 119 amino acid residues with a calculated molecular weight of 13,369 Da and a pI of 5.19. Overall, this amino-acid sequence was respectively 69% and 70% identical to those of Manduca sexta and Drosophila melanogaster 14-kDa subunits, although the two representatives of Class Insecta were remarkably similar to one another (91% identity). Three regions in particular (the N-terminal, amino acids 5-36; the middle, residues 58-68; and the C-terminal, residues 88-118) were highly conserved. Hence, we think that the 14-kDa subunits have evolved from the same ancestral gene, and that the three conserved regions are important for the structure and function of vacuolar ATPase. A single 0.8-kb band was detected in various human tissues by Northern blot analysis. Since the human 14-kDa subunit is expressed ubiquitously, it might be a housekeeping protein. A separate transcript found in the cDNA library lacked a 6-bp segment in the 5' non-coding region (nucleotides -40 to -35) and also carried a 23C to T (8Thr to Ile) point mutation in the coding region; these minor differences likely reflected normal polymorphism.
Protein involved in the transport of ions. Such proteins are usually transmembrane and mediate a movement of ions across cell membranes. Transport may be passive (facilitated diffusion; down the electrochemical gradient), or active (against the electrochemical gradient). Active transport requires energy which may come from light, oxidation reactions, ATP hydrolysis, or cotransport of other ions or molecules.
Protein involved in the transport of a molecule (metabolite, protein, etc), a ion or an electron across cell membranes, inside the cell or in a tissue fluid.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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