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

26 structures for P17255

Entry ID Method Resolution Chain Position Source
1DFA X-ray 200 A A 284-737 PDB
1EF0 X-ray 210 A A/B 283-741 PDB
1GPP X-ray 135 A PDB
1JVA X-ray 210 A A/B 274-747 PDB
1LWS X-ray 350 A A 284-737 PDB
1LWT X-ray 320 A A 284-737 PDB
1UM2 X-ray 290 A PDB
1VDE X-ray 240 A A/B 284-737 PDB
3J9T EM 690 A A/C/E 2-1071 PDB
3J9U EM 760 A A/C/E 2-1071 PDB
3J9V EM 830 A A/C/E 2-1071 PDB
5BW9 X-ray 700 A A/B/C/a/b/c 1-1071 PDB
5D80 X-ray 620 A A/B/C/a/b/c 1-1071 PDB
5VOX EM 680 A A/C/E 1-1071 PDB
5VOY EM 790 A A/C/E 1-1071 PDB
5VOZ EM 760 A A/C/E 1-1071 PDB
7FDA EM 420 A A/C/E 1-1071 PDB
7FDB EM 480 A A/C/E 1-1071 PDB
7FDC EM 660 A A/C/E 1-1071 PDB
7FDE EM 380 A A/C/E 1-1071 PDB
7TMM EM 350 A A/C/E 1-1071 PDB
7TMO EM 330 A A/C/E 1-1071 PDB
7TMP EM 330 A A/C/E 1-1071 PDB
7TMQ EM 330 A A/C/E 1-1071 PDB
7TMR EM 350 A A/C/E 1-1071 PDB
AF-P17255-F1 Predicted AlphaFoldDB

24 variants for P17255

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-126839 18 E>K No SGRP
s04-126842 19 D>N No SGRP
s04-126929 48 E>K No SGRP
s04-126975 63 R>K No SGRP
s04-127010 75 E>K No SGRP
s04-127403 206 K>E No SGRP
s04-127702 305 E>D No SGRP
s04-127768 327 R>S No SGRP
s04-127835 350 V>M No SGRP
s04-128030 415 I>V No SGRP
s04-128441 552 K>E No SGRP
s04-128444 553 V>I No SGRP
s04-128462 559 I>V No SGRP
s04-128507 574 V>I No SGRP
s04-128574 596 G>D No SGRP
s04-128718 644 V>A No SGRP
s04-128744 653 V>F No SGRP
s04-128862 692 A>V No SGRP
s04-128867 694 A>T No SGRP
s04-128874 696 A>V No SGRP
s04-128886 700 R>H No SGRP
s04-128921 712 D>N No SGRP
s04-129548 921 V>I No SGRP
s04-129843 1019 G>D No SGRP

No associated diseases with P17255

15 regional properties for P17255

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 237 - 916 IPR000194
domain Hint domain C-terminal 699 - 743 IPR003586
domain Hint domain N-terminal 282 - 389 IPR003587
domain Intein DOD homing endonuclease 494 - 642 IPR004042
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 28 - 90 IPR004100
ptm Intein N-terminal splicing region 284 - 366 IPR006141
domain Intein 491 - 503 IPR006142-1
domain Intein 600 - 612 IPR006142-2
domain Intein 732 - 741 IPR006142-3
domain Hom-end-associated Hint 284 - 736 IPR007868
domain Homing endonuclease PI-Sce 479 - 574 IPR007869-1
domain Homing endonuclease PI-Sce 585 - 690 IPR007869-2
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 907 - 916 IPR020003
domain Intein C-terminal splicing region 713 - 738 IPR030934
domain ATPsynthase alpha/beta subunit, N-terminal extension 106 - 228 IPR031686

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Endomembrane system ; Peripheral membrane protein ; Cytoplasmic side
  • Vacuole membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Membranes of various intracellular acidic compartments
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
endosome membrane The lipid bilayer surrounding an endosome.
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
proton-transporting V-type ATPase complex A proton-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of protons across a concentration gradient. The resulting transmembrane electrochemical potential of H+ is used to drive a variety of (i) secondary active transport systems via H+-dependent symporters and antiporters and (ii) channel-mediated transport systems. The complex comprises a membrane sector (V0) that carries out proton transport and a cytoplasmic compartment sector (V1) that catalyzes ATP hydrolysis. V-type ATPases are found in the membranes of organelles such as vacuoles, endosomes, and lysosomes, and in the plasma membrane.
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, V1 domain The V1 domain of a proton-transporting V-type ATPase found in the vacuolar membrane.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
endonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
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.

7 GO annotations of biological process

Name Definition
endosomal lumen acidification Any process that reduces the pH of the endosomal lumen, measured by the concentration of the hydrogen ion.
Golgi lumen acidification Any process that reduces the pH of the Golgi lumen, measured by the concentration of the hydrogen ion.
intein-mediated protein splicing The removal of an internal amino acid sequence (an intein) from a protein during protein maturation; the excision of inteins is precise and the N- and C-terminal exteins are joined by a normal peptide bond. Protein splicing involves 4 nucleophilic displacements by the 3 conserved splice junction residues.
intron homing Lateral transfer of an intron to a homologous allele that lacks the intron, mediated by a site-specific endonuclease encoded within the mobile intron.
protein metabolic process The chemical reactions and pathways involving a protein. Includes protein modification.
proton transmembrane transport The directed movement of a proton across a membrane.
vacuolar acidification Any process that reduces the pH of the vacuole, measured by the concentration of the hydrogen ion.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE
70 80 90 100 110 120
VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEES
130 140 150 160 170 180
QSIYIPRGID TPALDRTIKW QFTPGKFQVG DHISGGDIYG SVFENSLISS HKILLPPRSR
190 200 210 220 230 240
GTITWIAPAG EYTLDEKILE VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV
250 260 270 280 290 300
LDALFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC
310 320 330 340 350 360
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV PELLKFTCNA
370 380 390 400 410 420
THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG RIVELVKEVS KSYPISEGPE
430 440 450 460 470 480
RANELVESYR KASNKAYFEW TIEARDLSLL GSHVRKATYQ TYAPILYEND HFFDYMQKSK
490 500 510 520 530 540
FHLTIEGPKV LAYLLGLWIG DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE
550 560 570 580 590 600
PQVAKTVNLY SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET
610 620 630 640 650 660
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP AKVDMNGTKH
670 680 690 700 710 720
KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR GFYFELQELK EDDYYGITLS
730 740 750 760 770 780
DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM EFPELYTEMS GTKEPIMKRT TLVANTSNMP
790 800 810 820 830 840
VAAREASIYT GITLAEYFRD QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG
850 860 870 880 890 900
AKLASFYERA GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL
910 920 930 940 950 960
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL EQVVQLVGKS
970 980 990 1000 1010 1020
ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD MMRAFISYHD EAQKAVANGA
1030 1040 1050 1060 1070
NWSKLADSTG DVKHAVSSSK FFEPSRGEKE VHGEFEKLLS TMQERFAEST D