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 Q09891

Entry ID Method Resolution Chain Position Source
AF-Q09891-F1 Predicted AlphaFoldDB

6 variants for Q09891

Variant ID(s) Position Change Description Diseaes Association Provenance
I_228085_G_A 174 R>C No Jeffares_SNPs
I_227869_C_T 246 A>T No Jeffares_SNPs
I_226434_G_A 724 T>I No Jeffares_SNPs
I_226282_C_G 775 E>Q No Jeffares_SNPs
I_224944_T_C 1221 I>V No Jeffares_SNPs
I_224558_A_T,G 1349 N>K No Jeffares_SNPs

No associated diseases with Q09891

4 regional properties for Q09891

Type Name Position InterPro Accession
ptm P-type ATPase, phosphorylation site 569 - 575 IPR018303
domain P-type ATPase, C-terminal 1038 - 1287 IPR032630
domain P-type ATPase, N-terminal 81 - 127 IPR032631
domain P-type ATPase, haloacid dehalogenase domain 549 - 1061 IPR044492

Functions

Description
EC Number 7.6.2.1 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.
phospholipid-translocating ATPase complex A protein complex that functions as a phospholipid-translocating P-Type ATPase.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATPase-coupled intramembrane lipid transporter activity Catalysis of the movement of lipids from one membrane leaflet to the other, driven by ATP hydrolysis. This includes flippases and floppases.
glycolipid floppase activity Catalysis of the movement of a glycolipid from the cytosolic to the exoplasmic leaftlet of a membrane, using energy from the hydrolysis of ATP.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
glycolipid translocation The translocation, or flipping, of glycolipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.
phospholipid translocation The movement of a phospholipid molecule from one leaflet of a membrane bilayer to the opposite leaflet.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MESVEEKSKQ RRWLPNFKAL RLKVYRLADR LNIPLADAAR VELEEYDGSD PQSLRGLQKL
70 80 90 100 110 120
PRTLYFGLPL PDSELDDTGE AKRWFPRNKI RTAKYTPIDF IPKNIFLQFQ NVANLFFLFL
130 140 150 160 170 180
VILQSISIFG EQVNPGLAAV PLIVVVGITA VKDAIEDFRR TMLDIHLNNT PTLRLSHYQN
190 200 210 220 230 240
PNIRTEYISY FRRFKKRISA LFRVFLAKQE EKKRAKRLND AVPLEDMAGS ESRPSYDSIF
250 260 270 280 290 300
RESFEAKRSF EDSKGKVPLS ALDGTATILQ SRPMDIIDYE AEATGECHFK KTYWKDVRVG
310 320 330 340 350 360
DFVKVMDNDE IPADIVIINS SDPEGICYIE TKNLDGETNL KMRHALTCGK NVVDEASCER
370 380 390 400 410 420
CRFWIESEPP HANLYEYNGA CKSFVHSEAG GSDTSQTVSE PISLDSMLLR GCVLRNTKWV
430 440 450 460 470 480
IGVVVFTGDD TKIMLNSGAP PLKRSRITRN LNWNVYLNFI ILFSMCFVCA VVEGIAWRGH
490 500 510 520 530 540
SRSSYYFEFG SIGGSPAKDG VVTFFTGVIL FQNLVPISLY ISIEIVKTIQ AIFIYFDKDM
550 560 570 580 590 600
YYKKLKYACT PKSWNISDDL GQVEYIFSDK TGTLTQNVME FKKCTINGVA YGEAFTEAMA
610 620 630 640 650 660
GMAKREGKDT EELTLQKQSF IERDRMQMIS QMRNMHDNKY LVDDNLTFIS SQFVHDLAGK
670 680 690 700 710 720
AGEEQSLACY EFFLALALCH SVVADRVGDR IVYKAQSPDE AALVGTARDV GFVFLDQRRD
730 740 750 760 770 780
IMVTRALGET QRFKLMDTIE FSSARKRMSV IVKGPDNRYV LICKGADSII FERLEPNEQV
790 800 810 820 830 840
ELRKTTSEHL RIFALEGLRT LCIAKRELTE EEYYEWKEKY DIAASAIENR EEQIEEVADL
850 860 870 880 890 900
IESHLTLLGG TAIEDRLQEG VPDSIALLAQ AGIKLWVLTG DKMETAINIG FSCNLLDAGM
910 920 930 940 950 960
DMIKFDVDQE VSTPELEVIL ADYLYRYFGL SGSVEELEAA KKDHDTPSGS HALVIDGSVL
970 980 990 1000 1010 1020
KRVLDGPMRT KFLLLCKRCK AVLCCRVSPA QKADVVQLVR ESLEVMTLAI GDGANDVAMI
1030 1040 1050 1060 1070 1080
QKADIGVGIV GEEGRAAAMS ADYAIGQFRF LSKLVLVHGR WDYNRVAEMV NNFFYKSVVW
1090 1100 1110 1120 1130 1140
TFTLFWYQIY NNFDANYLFD YTYVMLFNLI FSSLPVIVMG VYDQDVNADL SLRIPQLYKR
1150 1160 1170 1180 1190 1200
GILQLNSARK IFIGYMLDGF YQSVICFFFS FLVINNVTTA AQNGRDTMAV QDLGVYVAAP
1210 1220 1230 1240 1250 1260
TIMVVDTYVI LNQSNWDVFS IGLWALSCLT FWFWTGVYSQ SLYTYEFYKS ASRIFRTPNF
1270 1280 1290 1300 1310 1320
WAVLCGTIVS CLFPKFLFMT TQKLFWPYDV DIIRESYRTK RLHELDEEEE IENAEQSPDW
1330 1340 1350 1360 1370 1380
ASSTLQVPFN ASSSSLATPK KEPLRLDTNS LTLTSSMPRS FTPSYTPSFL EGSPVFSDEI
1390 1400
LNRGEYMPHR GSISSSEQPL RP