P21440
PR
Gene name |
Abcb4 |
Protein name |
Phosphatidylcholine translocator ABCB4 |
Names |
ATP-binding cassette sub-family B member 4, Multidrug resistance protein 2, Multidrug resistance protein 3, P-glycoprotein 2, P-glycoprotein 3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:18670 |
EC number |
7.6.2.1: 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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P21440
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P21440-F1 | Predicted | AlphaFoldDB |
47 variants for P21440
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs8280043 | 13 | R>H | No | EVA | |
| rs3388733089 | 158 | E>G | No | EVA | |
| rs3388717420 | 160 | G>S | No | EVA | |
| rs8279986 | 178 | V>I | No | EVA | |
| rs3394908740 | 228 | T>R | No | EVA | |
| rs3388739792 | 238 | F>L | No | EVA | |
| rs3388717375 | 303 | L>M | No | EVA | |
| rs3388736126 | 309 | Y>* | No | EVA | |
| rs3388717423 | 327 | I>V | No | EVA | |
| rs31401258 | 386 | N>S | No | EVA | |
| rs235269040 | 449 | K>T | No | EVA | |
| rs3388717429 | 480 | S>T | No | EVA | |
| rs3395247491 | 516 | P>S | No | EVA | |
| rs3395192464 | 517 | Q>* | No | EVA | |
| rs3388733072 | 518 | K>N | No | EVA | |
| rs3388746797 | 546 | R>C | No | EVA | |
| rs3388748940 | 579 | R>Q | No | EVA | |
| rs3388735782 | 587 | R>Q | No | EVA | |
| rs31405434 | 630 | A>S | No | EVA | |
| rs8277382 | 673 | P>S | No | EVA | |
| rs8277405 | 713 | V>I | No | EVA | |
| rs8277381 | 742 | A>T | No | EVA | |
| rs225705157 | 779 | I>V | No | EVA | |
| rs3388729909 | 780 | L>H | No | EVA | |
| rs3388742829 | 794 | R>S | No | EVA | |
| rs3388742843 | 826 | G>E | No | EVA | |
| rs3388735750 | 830 | A>T | No | EVA | |
| rs3388726797 | 860 | V>F | No | EVA | |
| rs3388739456 | 894 | T>I | No | EVA | |
| rs3388742972 | 979 | L>P | No | EVA | |
| rs8277171 | 999 | L>M | No | EVA | |
| rs3388743402 | 1003 | Y>N | No | EVA | |
| rs3388743043 | 1034 | N>I | No | EVA | |
| rs3388743401 | 1053 | S>G | No | EVA | |
| rs3388729918 | 1060 | Q>K | No | EVA | |
| rs3388729848 | 1072 | K>N | No | EVA | |
| rs3388739804 | 1086 | M>T | No | EVA | |
| rs3388740894 | 1090 | V>M | No | EVA | |
| rs8277266 | 1099 | K>Q | No | EVA | |
| rs8277263 | 1108 | Q>H | No | EVA | |
| rs31393834 | 1139 | D>E | No | EVA | |
| rs3388743374 | 1150 | I>V | No | EVA | |
| rs3388742560 | 1216 | K>R | No | EVA | |
| rs3388733104 | 1219 | E>D | No | EVA | |
| rs3388739428 | 1225 | V>L | No | EVA | |
| rs3388729841 | 1234 | Q>H | No | EVA | |
| rs3388746725 | 1236 | A>T | No | EVA |
No associated diseases with P21440
8 regional properties for P21440
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 391 - 627 | IPR003439-1 |
| domain | ABC transporter-like, ATP-binding domain | 1031 - 1269 | IPR003439-2 |
| domain | AAA+ ATPase domain | 418 - 610 | IPR003593-1 |
| domain | AAA+ ATPase domain | 1058 - 1246 | IPR003593-2 |
| domain | ABC transporter type 1, transmembrane domain | 54 - 356 | IPR011527-1 |
| domain | ABC transporter type 1, transmembrane domain | 709 - 996 | IPR011527-2 |
| conserved_site | ABC transporter-like, conserved site | 530 - 544 | IPR017871-1 |
| conserved_site | ABC transporter-like, conserved site | 1172 - 1186 | IPR017871-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.6.2.1 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
13 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. |
| apical plasma membrane | The region of the plasma membrane located at the apical end of the cell. |
| clathrin-coated vesicle | A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
| intercellular canaliculus | An extremely narrow tubular channel located between adjacent cells. An instance of this is the secretory canaliculi occurring between adjacent parietal cells in the gastric mucosa of vertebrates. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type transporter activity | Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. |
| 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. |
| ceramide floppase activity | Catalysis of the movement of ceramide from the cytosolic to the exoplasmic leaftlet of a membrane, using energy from the hydrolysis of ATP. |
| phosphatidylcholine floppase activity | Catalysis of the movement of phosphatidylcholine from the cytosolic to the exoplasmic leaftlet of a membrane, using energy from the hydrolysis of ATP. |
| phosphatidylethanolamine flippase activity | Catalysis of the movement of phosphatidylethanolamine from the exoplasmic to the cytosolic leaftlet of a membrane, using energy from the hydrolysis of ATP. |
| xenobiotic transmembrane transporter activity | Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| bile acid secretion | The regulated release of bile acid, composed of any of a group of steroid carboxylic acids occurring in bile, by a cell or a tissue. |
| cellular response to bile acid | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bile acid stimulus. |
| lipid homeostasis | Any process involved in the maintenance of an internal steady state of lipid within an organism or cell. |
| phospholipid translocation | The movement of a phospholipid molecule from one leaflet of a membrane bilayer to the opposite leaflet. |
| positive regulation of cholesterol transport | Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| 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. |
| positive regulation of phospholipid transport | Any process that activates or increases the frequency, rate or extent of phospholipid transport. |
| response to fenofibrate | 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 fenofibrate stimulus. |
10 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O95342 | ABCB11 | Bile salt export pump | Homo sapiens (Human) | PR |
| P08183 | ABCB1 | ATP-dependent translocase ABCB1 | Homo sapiens (Human) | PR |
| P06795 | Abcb1b | ATP-dependent translocase ABCB1 | Mus musculus (Mouse) | PR |
| P21447 | Abcb1a | ATP-dependent translocase ABCB1 | Mus musculus (Mouse) | PR |
| Q9QY30 | Abcb11 | Bile salt export pump | Mus musculus (Mouse) | PR |
| Q9DC29 | Abcb6 | ATP-binding cassette sub-family B member 6 | Mus musculus (Mouse) | PR |
| O70127 | Abcb11 | Bile salt export pump | Rattus norvegicus (Rat) | PR |
| Q8H1R4 | ABCI10 | ABC transporter I family member 10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LJX0 | ABCB19 | ABC transporter B family member 19 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9ZR72 | ABCB1 | ABC transporter B family member 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDLEAARNGT | ARRLDGDFEL | GSISNQGREK | KKKVNLIGLL | TLFRYSDWQD | KLFMFLGTLM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AIAHGSGLPL | MMIVFGEMTD | KFVDNTGNFS | LPVNFSLSML | NPGRILEEEM | TRYAYYYSGL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GGGVLVAAYI | QVSFWTLAAG | RQIKKIRQKF | FHAILRQEMG | WFDIKGTTEL | NTRLTDDVSK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ISEGIGDKVG | MFFQAIATFF | AGFIVGFIRG | WKLTLVIMAI | SPILGLSTAV | WAKILSTFSD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KELAAYAKAG | AVAEEALGAI | RTVIAFGGQN | KELERYQKHL | ENAKKIGIKK | AISANISMGI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AFLLIYASYA | LAFWYGSTLV | ISKEYTIGNA | MTVFFSILIG | AFSVGQAAPC | IDAFANARGA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AYVIFDIIDN | NPKIDSFSER | GHKPDNIKGN | LEFSDVHFSY | PSRANIKILK | GLNLKVKSGQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TVALVGNSGC | GKSTTVQLLQ | RLYDPTEGKI | SIDGQDIRNF | NVRCLREIIG | VVSQEPVLFS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TTIAENIRYG | RGNVTMDEIE | KAVKEANAYD | FIMKLPQKFD | TLVGDRGAQL | SGGQKQRIAI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARALVRNPKI | LLLDEATSAL | DTESEAEVQA | ALDKAREGRT | TIVIAHRLST | IRNADVIAGF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EDGVIVEQGS | HSELMKKEGI | YFRLVNMQTA | GSQILSEEFE | VELSDEKAAG | DVAPNGWKAR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IFRNSTKKSL | KSPHQNRLDE | ETNELDANVP | PVSFLKVLKL | NKTEWPYFVV | GTVCAIANGA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LQPAFSIILS | EMIAIFGPGD | DAVKQQKCNM | FSLVFLGLGV | LSFFTFFLQG | FTFGKAGEIL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TTRLRSMAFK | AMLRQDMSWF | DDHKNSTGAL | STRLATDAAQ | VQGATGTRLA | LIAQNTANLG |
| 850 | 860 | 870 | 880 | 890 | 900 |
| TGIIISFIYG | WQLTLLLLSV | VPFIAVAGIV | EMKMLAGNAK | RDKKEMEAAG | KIATEAIENI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| RTVVSLTQER | KFESMYVEKL | HGPYRNSVRK | AHIYGITFSI | SQAFMYFSYA | GCFRFGSYLI |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| VNGHMRFKDV | ILVFSAIVLG | AVALGHASSF | APDYAKAKLS | AAYLFSLFER | QPLIDSYSGE |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| GLWPDKFEGS | VTFNEVVFNY | PTRANVPVLQ | GLSLEVKKGQ | TLALVGSSGC | GKSTVVQLLE |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| RFYDPMAGSV | LLDGQEAKKL | NVQWLRAQLG | IVSQEPILFD | CSIAENIAYG | DNSRVVPHDE |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| IVRAAKEANI | HPFIETLPQK | YNTRVGDKGT | QLSGGQKQRI | AIARALIRQP | RVLLLDEATS |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| ALDTESEKVV | QEALDKAREG | RTCIVIAHRL | STIQNADLIV | VIENGKVKEH | GTHQQLLAQK |
| 1270 | |||||
| GIYFSMVNIQ | AGTQNL |