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 P70704

Entry ID Method Resolution Chain Position Source
AF-P70704-F1 Predicted AlphaFoldDB

60 variants for P70704

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3395325181 61 V>M No EVA
rs3388764940 86 L>P No EVA
rs3388757762 145 I>T No EVA
rs3388765512 189 D>E No EVA
rs3388752858 193 N>I No EVA
rs3388757394 193 N>K No EVA
rs3388767361 240 H>R No EVA
rs3395703424 253 R>* No EVA
rs3388765458 273 D>V No EVA
rs3395462508 326 K>N No EVA
rs3395333911 330 L>H No EVA
rs3388767425 425 T>I No EVA
rs3388760013 426 I>M No EVA
rs234738063 434 V>A No EVA
rs3388746648 439 D>E No EVA
rs3388764867 440 Y>* No EVA
rs3388757388 445 D>E No EVA
rs1132070624 454 D>N No EVA
rs1135189842 455 E>V No EVA
rs864292200 464 L>P No EVA
rs3388764596 468 Q>R No EVA
rs3388736570 471 H>R No EVA
rs3388750493 472 P>L No EVA
rs251535852 486 V>I No EVA
rs3388746690 521 V>F No EVA
rs3388736522 576 T>I No EVA
rs864262113 622 W>C No EVA
rs864305380 623 R>W No EVA
rs3388757409 645 E>K No EVA
rs3388771336 681 I>L No EVA
rs3388764588 683 I>V No EVA
rs3388736545 686 G>E No EVA
rs3388762383 686 G>W No EVA
rs3395648534 698 S>T No EVA
rs3388748627 703 K>E No EVA
rs3395705455 707 G>E No EVA
rs3388764599 754 T>I No EVA
rs3388736559 779 L>F No EVA
rs3388736542 794 V>A No EVA
rs3388748553 809 I>N No EVA
rs3388762437 812 A>V No EVA
rs3388752810 815 G>S No EVA
rs3395653027 864 Y>* No EVA
rs3395593953 864 Y>F No EVA
rs3395674164 865 K>* No EVA
rs3388746629 891 W>* No EVA
rs3388771384 897 N>I No EVA
rs3388765517 905 P>T No EVA
rs3388752866 943 V>I No EVA
rs3388771355 983 F>L No EVA
rs3388755941 1017 L>P No EVA
rs3388762045 1024 I>F No EVA
rs3388764943 1097 V>L No EVA
rs3388765143 1100 G>E No EVA
rs3395461446 1104 T>S No EVA
rs3388764889 1107 A>V No EVA
rs3388763989 1153 A>S No EVA
rs3388758508 1162 D>E No EVA
rs3388736521 1162 D>V No EVA
rs3388748580 1165 W>C No EVA

No associated diseases with P70704

1 regional properties for P70704

Type Name Position InterPro Accession
domain SUN domain 203 - 362 IPR012919

Functions

Description
EC Number 7.6.2.1 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane ; Multi-pass membrane protein
  • Cytoplasmic granule
  • Cell membrane
  • Endoplasmic reticulum
  • Golgi apparatus
  • Cytoplasmic vesicle
  • Endomembrane system
  • Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B
  • In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures (By similarity)
  • Localizes to plasma membranes of red blood cells (PubMed:16643453)
  • Localizes predominantly in the intracellular membranes, rather than the cell membrane of platelets (PubMed:30674456)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
chromaffin granule membrane The lipid bilayer surrounding a chromaffin granule, a specialized secretory vesicle found in the cells of adrenal glands and various other organs, which is concerned with the synthesis, storage, metabolism, and secretion of epinephrine and norepinephrine.
cytoplasmic vesicle A vesicle found in the cytoplasm of a cell.
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).
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
integral component of synaptic vesicle membrane The component of the synaptic vesicle 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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
organelle membrane A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle.
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.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.

6 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.
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphatidylserine flippase activity Catalysis of the movement of phosphatidylserine from the exoplasmic to the cytosolic leaftlet of a membrane, using energy from the hydrolysis of ATP.
phosphatidylserine floppase activity Catalysis of the movement of phosphatidylserine from the cytosolic to the exoplasmic leaftlet of a membrane, using energy from the hydrolysis of ATP.

5 GO annotations of biological process

Name Definition
aminophospholipid translocation The movement of an aminophospholipid molecule from one leaflet of a membrane bilayer to the opposite leaflet.
learning Any process in an organism in which a relatively long-lasting adaptive behavioral change occurs as the result of experience.
phospholipid translocation The movement of a phospholipid molecule from one leaflet of a membrane bilayer to the opposite leaflet.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
positive regulation of phospholipid translocation Any process that increases the frequency, rate or extent of the translocation, or flipping, of phospholipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P39524 DRS2 Phospholipid-transporting ATPase DRS2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) EV
Q9P241 ATP10D Phospholipid-transporting ATPase VD Homo sapiens (Human) PR
Q8TF62 ATP8B4 Probable phospholipid-transporting ATPase IM Homo sapiens (Human) PR
P98198 ATP8B2 Phospholipid-transporting ATPase ID Homo sapiens (Human) PR
O43520 ATP8B1 Phospholipid-transporting ATPase IC Homo sapiens (Human) EV
Q9Y2Q0 ATP8A1 Phospholipid-transporting ATPase IA Homo sapiens (Human) PR
Q148W0 Atp8b1 Phospholipid-transporting ATPase IC Mus musculus (Mouse) SS
P98199 Atp8b2 Phospholipid-transporting ATPase ID Mus musculus (Mouse) PR
D4AA47 Atp8b1 Phospholipid-transporting ATPase IC Rattus norvegicus (Rat) SS
Q9U280 tat-1 Phospholipid-transporting ATPase tat-1 Caenorhabditis elegans PR
Q5BL50 atp8b1 Phospholipid-transporting ATPase IC Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
10 20 30 40 50 60
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN
70 80 90 100 110 120
VITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED
130 140 150 160 170 180
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLL SLSSSEPQAM
190 200 210 220 230 240
CYIETSNLDG ETNLKIRQGL PATSDIKDID SLMRISGRIE CESPNRHLYD FVGNIRLDGH
250 260 270 280 290 300
GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
310 320 330 340 350 360
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL HLHYGGASNF GLNFLTFIIL FNNLIPISLL
370 380 390 400 410 420
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
430 440 450 460 470 480
FKKCTIAGVA YGHVPEPEDY GCSPDEWQSS QFGDEKTFND PSLLDNLQNN HPTAPIICEF
490 500 510 520 530 540
LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER
550 560 570 580 590 600
YELLNVLEFT SARKRMSVVV RTPSGKLRLY CKGADTVIYE RLAETSKYKE ITLKHLEQFA
610 620 630 640 650 660
TEGLRTLCFA VAEISESDFE EWRAVYHRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE
670 680 690 700 710 720
DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCR LLKRNMGMIV INEGSLDGTR
730 740 750 760 770 780
ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ
790 800 810 820 830 840
KSEVVEMVKK QVKVITLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
850 860 870 880 890 900
KNLLMVHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
910 920 930 940 950 960
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL
970 980 990 1000 1010 1020
KALQYGTVFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV
1030 1040 1050 1060 1070 1080
FFGIYSSLWP AVPMAPDMSG EAAMLFSSGV FWVGLLSIPV ASLLLDVLYK VIKRTAFKTL
1090 1100 1110 1120 1130 1140
VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD
1150 1160
ENGIVSQSEV IRAYDTTKQR PDEW