Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q920R6

Entry ID Method Resolution Chain Position Source
AF-Q920R6-F1 Predicted AlphaFoldDB

46 variants for Q920R6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388791072 9 E>* No EVA
rs3388809805 10 M>V No EVA
rs3388806515 91 R>W No EVA
rs3388806486 93 M>L No EVA
rs3396653011 135 Q>L No EVA
rs3396716309 136 D>G No EVA
rs3388815904 153 T>I No EVA
rs47125959 161 T>A No EVA
rs3388812844 210 D>Y No EVA
rs3388809817 220 N>K No EVA
rs3388825068 251 E>K No EVA
rs3388828650 292 W>R No EVA
rs3388815896 309 L>Q No EVA
rs3396670006 312 C>F No EVA
rs3388823182 318 Q>* No EVA
rs3396492268 319 Q>E No EVA
rs3388809754 324 E>K No EVA
rs220819603 351 I>V No EVA
rs3388816531 362 D>N No EVA
rs3388815932 366 F>I No EVA
rs3388825076 368 R>K No EVA
rs3388809786 372 F>I No EVA
rs3396716342 392 N>S No EVA
rs3388817844 408 M>I No EVA
rs3388823194 425 M>L No EVA
rs3388822115 467 N>Y No EVA
rs3388809764 468 D>G No EVA
rs3388809793 522 I>F No EVA
rs3388823148 523 D>E No EVA
rs216680762 550 A>V No EVA
rs3388824381 571 N>Y No EVA
rs3388806538 578 P>S No EVA
rs260824859 649 V>L No EVA
rs3388815920 664 A>T No EVA
rs3396720269 678 E>V No EVA
rs50582078 681 V>L No EVA
rs3413074056 682 E>D No EVA
rs3396250307 683 G>R No EVA
rs225201366 702 G>D No EVA
rs242943001 702 G>S No EVA
rs3388802334 754 M>L No EVA
rs1132229897 788 V>I No EVA
rs3396668955 803 W>* No EVA
rs3396715514 809 K>* No EVA
rs3396580538 809 K>M No EVA
rs3388789827 813 G>E No EVA

No associated diseases with Q920R6

No regional properties for Q920R6

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q920R6

Functions

Description
EC Number
Subcellular Localization
  • Apical cell membrane ; Multi-pass membrane protein
  • Basolateral cell membrane ; Multi-pass membrane protein
  • Localizes to the apical surface of alpha-intercalated cells in the cortical collecting ducts of the distal nephron (PubMed:11495928, PubMed:11498539)
  • Localizes to the basolateral surface of beta-intercalated cells in the cortical collecting ducts of the distal nephron (PubMed:11495928, PubMed:11498539)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
apical part of cell The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
apical plasma membrane The region of the plasma membrane located at the apical end of the cell.
basolateral plasma membrane The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
brush border The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
brush border membrane The portion of the plasma membrane surrounding the brush border.
endosome A vacuole to which materials ingested by endocytosis are delivered.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
vacuolar proton-transporting V-type ATPase complex A proton-transporting two-sector ATPase complex found in the vacuolar membrane, where it acts as a proton pump to mediate acidification of the vacuolar lumen.
vacuolar proton-transporting V-type ATPase, V0 domain The V0 domain of a proton-transporting V-type ATPase found in the vacuolar membrane.

3 GO annotations of molecular function

Name Definition
ATPase binding Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
P-type proton-exporting transporter activity Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons 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.

6 GO annotations of biological process

Name Definition
ossification The formation of bone or of a bony substance, or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
proton transmembrane transport The directed movement of a proton across a membrane.
regulation of pH Any process involved in the maintenance of an internal equilibrium of hydrogen ions, thereby modulating the internal pH, within an organism or cell.
renal tubular secretion The elimination of substances from peritubular capillaries (or surrounding hemolymph in invertebrates) into the renal tubules to be incorporated subsequently into the urine. Substances that are secreted include organic anions, ammonia, potassium and drugs.
sensory perception of sound The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
vacuolar acidification Any process that reduces the pH of the vacuole, measured by the concentration of the hydrogen ion.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32563 VPH1 V-type proton ATPase subunit a, vacuolar isoform Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q29466 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Bos taurus (Bovine) PR
O97681 ATP6V0A2 V-type proton ATPase 116 kDa subunit a 2 Bos taurus (Bovine) PR
Q9I8D0 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Gallus gallus (Chicken) PR
Q13488 TCIRG1 V-type proton ATPase 116 kDa subunit a 3 Homo sapiens (Human) PR
Q93050 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Homo sapiens (Human) PR
Q9Y487 ATP6V0A2 V-type proton ATPase 116 kDa subunit a 2 Homo sapiens (Human) PR
Q9HBG4 ATP6V0A4 V-type proton ATPase 116 kDa subunit a 4 Homo sapiens (Human) PR
P15920 Atp6v0a2 V-type proton ATPase 116 kDa subunit a 2 Mus musculus (Mouse) PR
Q9Z1G4 Atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Mus musculus (Mouse) PR
P25286 Atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Rattus norvegicus (Rat) PR
P30628 unc-32 V-type proton ATPase 116 kDa subunit a 1 Caenorhabditis elegans PR
Q8RWZ7 VHA-a1 V-type proton ATPase subunit a1 Arabidopsis thaliana (Mouse-ear cress) PR
Q8W4S4 VHA-a3 V-type proton ATPase subunit a3 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SJT7 VHA-a2 V-type proton ATPase subunit a2 Arabidopsis thaliana (Mouse-ear cress) PR
A1A5G6 atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MASVFRSEEM CLSQVFLQVE AAYCCVAELG ELGLVQFKDL NANVNSFQRK FVNEVRRCES
70 80 90 100 110 120
LERILRFLED EMQNEILIQV PEKDAETPLP REMITLETTL EKLEGELQEA NQSHQALKKS
130 140 150 160 170 180
FLELTELKYL LKKTQDFFET ETNLGEDFFV EDTSGLLELR TIPAFMTGKL GFTAGVINRE
190 200 210 220 230 240
RMASFERLLW RVCRGNVYLK FSEMDTLLED PVTKEEIKKN IFIIFYQGEQ LRLKIKKICD
250 260 270 280 290 300
GFRATIYPCP EHAAERREML TSVNVRLEDL ITVITQTESH RQRLLQEAAA NWHSWVIKVQ
310 320 330 340 350 360
KMKAVYHVLN MCNIDVTQQC IIAEIWFPVA DTRHIKKALE QGMELSGSSM IPIMTEVETK
370 380 390 400 410 420
TDPPTFNRTN KFTAGFQNIV DAYGVGSYRE INPAPYTIIT FPFLFAVMFG DCGHGMVMLM
430 440 450 460 470 480
AALWMVLNER HLLAQKSTNE MWNIFFNGRY LILLMGIFSI YTGLIYNDCF SKSFNIFGSS
490 500 510 520 530 540
WSVQPMFRNG TWNTHIVENS PYLQLDPAIP GVYSGNPYPF GIDPIWNLAS NKLTFLNSYK
550 560 570 580 590 600
MKMSVILGIA HMIFGVILSL FNHIYFRRTL NIILQFIPEM IFMLSLFGYL VFMIIFKWCR
610 620 630 640 650 660
YDAHTSRKAP SILIHFIGMF LFDYDDSSNA PLYGHQQEVQ TFFVIIALVS VPWMLLIKPF
670 680 690 700 710 720
VLRAKHQKSQ LQSFTIHEDA VEGDHSGHSS KKTAGAHGMK DGHEEEFNFG DIFVHQAIHT
730 740 750 760 770 780
IEYCLGCISN TASYLRLWAL SLAHAELSEV LWTMVMSIGL RLQGWAGLVG VFIIFAVFAV
790 800 810 820 830
LTVAILLVME GLSAFLHALR LHWVEFQNKF YEGAGSKFSP FSFKHVLEGT AEE