A0A1D6FIR4 protein (Zea mays) - STRING interaction network

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A0A1D6FIR4

V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (186 aa)

Predicted Functional Partners:

A0A1D6FYA0

0.991

B4FZS8_MAIZE

0.989

atpF

0.988

B4FLC0_MAIZE

0.982

Pco119646(297)

0.969

B4FVD6_MAIZE

0.969

K7TLG8_MAIZE

0.969

A0A1D6KLF7

0.966

B4FMV3_MAIZE

0.964

B6SQV1_MAIZE

0.961

Your Current Organism:

Zea mays

NCBI taxonomy Id: 4577
Other names: Z. mays, Zea mays L., Zea mays var. japonica, maize

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A0A1D6FIR4	A0A1D6FYA0	A0A1D6FIR4	A0A1D6FYA0	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit d2.	0.991
A0A1D6FIR4	A0A1D6KLF7	A0A1D6FIR4	A0A1D6KLF7	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	ATP synthase subunit d, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the cent [...]	0.966
A0A1D6FIR4	B4FLC0_MAIZE	A0A1D6FIR4	B4FLC0	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit F; 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.	0.982
A0A1D6FIR4	B4FMV3_MAIZE	A0A1D6FIR4	B4FMV3	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit G; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	0.964
A0A1D6FIR4	B4FVD6_MAIZE	A0A1D6FIR4	B4FVD6	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit D.	0.969
A0A1D6FIR4	B4FZS8_MAIZE	A0A1D6FIR4	B4FZS8	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	Vacuolar ATP synthase 21 kDa proteolipid subunit; Belongs to the V-ATPase proteolipid subunit family.	0.989
A0A1D6FIR4	B6SQV1_MAIZE	A0A1D6FIR4	B6SQV1	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit e1.	0.961
A0A1D6FIR4	K7TLG8_MAIZE	A0A1D6FIR4	K7TLG8	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	V-type proton ATPase subunit D.	0.969
A0A1D6FIR4	Pco119646(297)	A0A1D6FIR4	B4FDN9	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	Vacuolar ATP synthase subunit D 1.	0.969
A0A1D6FIR4	atpF	A0A1D6FIR4	P48186	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	ATP synthase subunit b, chloroplastic; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.	0.988
A0A1D6FYA0	A0A1D6FIR4	A0A1D6FYA0	A0A1D6FIR4	V-type proton ATPase subunit d2.	V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	0.991
A0A1D6FYA0	A0A1D6KLF7	A0A1D6FYA0	A0A1D6KLF7	V-type proton ATPase subunit d2.	ATP synthase subunit d, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the cent [...]	0.448
A0A1D6FYA0	B4FLC0_MAIZE	A0A1D6FYA0	B4FLC0	V-type proton ATPase subunit d2.	V-type proton ATPase subunit F; 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.	0.999
A0A1D6FYA0	B4FMV3_MAIZE	A0A1D6FYA0	B4FMV3	V-type proton ATPase subunit d2.	V-type proton ATPase subunit G; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.	0.998
A0A1D6FYA0	B4FVD6_MAIZE	A0A1D6FYA0	B4FVD6	V-type proton ATPase subunit d2.	V-type proton ATPase subunit D.	0.998
A0A1D6FYA0	B4FZS8_MAIZE	A0A1D6FYA0	B4FZS8	V-type proton ATPase subunit d2.	Vacuolar ATP synthase 21 kDa proteolipid subunit; Belongs to the V-ATPase proteolipid subunit family.	0.999
A0A1D6FYA0	B6SQV1_MAIZE	A0A1D6FYA0	B6SQV1	V-type proton ATPase subunit d2.	V-type proton ATPase subunit e1.	0.996
A0A1D6FYA0	K7TLG8_MAIZE	A0A1D6FYA0	K7TLG8	V-type proton ATPase subunit d2.	V-type proton ATPase subunit D.	0.998
A0A1D6FYA0	Pco119646(297)	A0A1D6FYA0	B4FDN9	V-type proton ATPase subunit d2.	Vacuolar ATP synthase subunit D 1.	0.998
A0A1D6FYA0	atpF	A0A1D6FYA0	P48186	V-type proton ATPase subunit d2.	ATP synthase subunit b, chloroplastic; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.	0.454

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