Q9P7V2

PR
Gene name
abc4
Protein name
ATP-binding cassette transporter abc4
Names
ABC transporter abc4, ATP-energized glutathione S-conjugate pump abc4, Glutathione S-conjugate-transporting ATPase abc4
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC30.04c
EC number
7.6.2.2: Linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

799-902 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9P7V2

Entry ID Method Resolution Chain Position Source
AF-Q9P7V2-F1 Predicted AlphaFoldDB

14 variants for Q9P7V2

Variant ID(s) Position Change Description Diseaes Association Provenance
I_4400196_G_A 49 A>V No Jeffares_SNPs
I_4400139_A_G 68 L>S No Jeffares_SNPs
I_4400051_C_A 97 L>F No Jeffares_SNPs
I_4399347_A_G 332 V>A No Jeffares_SNPs
I_4399231_C_T 371 V>I No Jeffares_SNPs
I_4398462_C_A 627 G>V No Jeffares_SNPs
I_4397778_A_G 855 V>A No Jeffares_SNPs
I_4397779_C_T 855 V>I No Jeffares_SNPs
I_4397763_G_A 860 A>V No Jeffares_SNPs
I_4396713_C_T 1210 G>E No Jeffares_SNPs
I_4396699_T_C 1215 N>D No Jeffares_SNPs
I_4396648_C_G 1232 V>L No Jeffares_SNPs
I_4396627_T_C 1239 S>G No Jeffares_SNPs
I_4396602_C_T 1247 R>H No Jeffares_SNPs

No associated diseases with Q9P7V2

8 regional properties for Q9P7V2

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 611 - 840 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1214 - 1453 IPR003439-2
domain AAA+ ATPase domain 640 - 817 IPR003593-1
domain AAA+ ATPase domain 1238 - 1430 IPR003593-2
domain ABC transporter type 1, transmembrane domain 297 - 580 IPR011527-1
domain ABC transporter type 1, transmembrane domain 898 - 1176 IPR011527-2
conserved_site ABC transporter-like, conserved site 740 - 754 IPR017871-1
conserved_site ABC transporter-like, conserved site 1356 - 1370 IPR017871-2

Functions

Description
EC Number 7.6.2.2 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Vacuole membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
fungal-type vacuole A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
vacuolar membrane The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.

3 GO annotations of molecular function

Name Definition
ABC-type xenobiotic transporter activity Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATPase-coupled transmembrane transporter activity Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source.

4 GO annotations of biological process

Name Definition
glutathione transmembrane import into vacuole The directed movement of glutathione into the vacuole across the vacuolar membrane.
phytochelatin 2 import into vacuole The directed movement of phytochelatin 2 (PC2) into the vacuole. Phytochelatin 2 is a glutathione-related peptide composed of (gamma-Glu-Cys)n-Gly where n=2, and where the Glu and Cys residues are linked through a gamma-carboxylamide bond.
response to toxic substance Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MENFHHRPFK GGFGVGRVPT SLYYSLSDFS LSAISIFPTH YDQPYLNEAP SWYKYSLESG
70 80 90 100 110 120
LVCLYLYLIY RWITRSFTVK QTVGSEFSGL RKAHGILLWL LSILFLGMTA FMFVNDAFPT
130 140 150 160 170 180
AFSDPPVKIC LLAYSVHLFL LHSLRMIYPR ARPTLYHAAV LLNLLLLPPI FHFYSYPFFF
190 200 210 220 230 240
VDHPPLSSYS PFLWFYFFIT IVGNFIPLFT PRVWYPLFPE DNYQPSAEQV CSMFNFACSY
250 260 270 280 290 300
GYLNPLVLTA KRRVVEVDDT PVIPDYDKNK AWTYRFERMK TPSLFITIHK IFWRQILGMG
310 320 330 340 350 360
VSSFMVSVCQ FLSPIALNRL LKHLESPSSS SVNPLVWIVL LLTGPFLTSL FTQFYLFMST
370 380 390 400 410 420
RYLARSYTTL VQQIYNKVIR SRFVQNKSGD SKVGRSNNLI STDVDDIGEI REFIHIIVRA
430 440 450 460 470 480
PVEIAGSIYL LQKLLGWSAY VGLALTVLTC SVPIVLGPLV AKLTLRANRA TDSRIELMSE
490 500 510 520 530 540
LLQSIRITKF FGWELPMLDR VKQRRQVELN RTWKLLLMEI CIQVLVESLP VFSMFATFVV
550 560 570 580 590 600
FTTIMGQTIT PSIAFTSISL FSFIRTQFSW IAYLMRQIVQ IFVSIGRVSD FLNDPDEVDP
610 620 630 640 650 660
VNTIEDTSQE IGFFNASLTW VSNPSPGDFC LRDLNIVFPR NKLSIVIGPT GSGKSSLISA
670 680 690 700 710 720
LLGELSLNKG SYNLPRSKGV SYVSQVPWLR NATIRDNILF DYPYIEERYK KVIQACGLLT
730 740 750 760 770 780
DLQSFVASDL TEIGEKGVTL SGGQKQRIAL ARAVYSPTSI VLMDDVFSAL DIHTSNWIYK
790 800 810 820 830 840
HCFQSSLMEN RTVILVTHNV HLFMDSAAFI VTVKNGSAFP VTDKSSPLLF LAEQAASASE
850 860 870 880 890 900
AAAPDLAAIP IPNEVDDAEA ADEKDGKLVE EEQRVTGDVV FSEIFSYMKH FGSGFYVAAV
910 920 930 940 950 960
LLFFVTTQAT SILIDLWVAF WTNSSVNSPD VNNNKFLFVY GTMLLAYSLL DFLRTVSYDR
970 980 990 1000 1010 1020
GAWWASRKLH DSMLESVFGT FASWFDKTPT GRIVNRFAKD IRSIDMNLSG WLFFSINCFL
1030 1040 1050 1060 1070 1080
SVAGGILSVS SAMPIFMIPA VIVCLAGYYF GLLYTRAQVG VKRLISIYTS PIFSLLGESI
1090 1100 1110 1120 1130 1140
VGVSVIRAFN RQTIFKQMFS ERLDNLVRLQ STSYNLNRWV AVRTDGISGL VGAIAGLIAL
1150 1160 1170 1180 1190 1200
LQKDLSPGVV GFSLNQAVIF SSSVLLFVRS CNSLQAEMNS YERVLEYSKL PQEPAPTIAG
1210 1220 1230 1240 1250 1260
QVPATWPKEG DIVFNHVSVS YSAAGPTILK DVNLHINPSE KVAVVGRTGS GKSTLGLTLL
1270 1280 1290 1300 1310 1320
RFTHRISGEI YINGRETQSV NLNALRQRIS FIPQDPILFS GTVRSNLDPF DELEDNFLNE
1330 1340 1350 1360 1370 1380
ALKTSGASSM IMAHTDDQKP IHITLDTHVA SEGSNFSQGQ KQVLALARAI VRRSKIIILD
1390 1400 1410 1420 1430 1440
ECTASVDDAM DQKIQKTLRE AFGDATMLCI AHRLKTIVDY DKVMVLDKGV LVEYGPPAVL
1450 1460
YHNNGHFRRM CDGSGITFLP PETRGSKSA