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 Q8K442

Entry ID Method Resolution Chain Position Source
AF-Q8K442-F1 Predicted AlphaFoldDB

93 variants for Q8K442

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389207463 17 C>F No EVA
rs250803674 45 I>T No EVA
rs235965615 50 L>M No EVA
rs3389216313 75 F>Y No EVA
rs3389176168 76 M>T No EVA
rs3389176145 86 T>I No EVA
rs3389222462 113 M>T No EVA
rs3389216381 114 T>R No EVA
rs247941291 140 I>L No EVA
rs27050016 166 Y>S No EVA
rs27050021 232 R>C No EVA
rs3389176214 250 K>R No EVA
rs27050026 284 S>L No EVA
rs251507700 299 F>L No EVA
rs3389222397 303 F>I No EVA
rs3389229179 316 L>S No EVA
rs3389213791 332 L>P No EVA
rs3389183871 342 G>V No EVA
rs1135064706 406 D>N No EVA
rs3402382394 423 S>V No EVA
rs3389188618 437 S>P No EVA
rs234439215 470 M>I No EVA
rs262410736 470 M>T No EVA
rs3389188644 488 I>L No EVA
rs262017523 493 R>H No EVA
rs3389210214 499 D>G No EVA
rs3389222473 632 D>Y No EVA
rs27050034 656 F>L No EVA
rs3402765995 715 S>C No EVA
rs3389216383 718 C>Y No EVA
rs3389217302 722 R>* No EVA
rs3402792404 744 L>M No EVA
rs3389216310 760 Y>H No EVA
rs3389201327 765 R>I No EVA
rs3389176147 782 T>S No EVA
rs225099143 867 V>I No EVA
rs256224590 868 L>W No EVA
rs3389176127 883 M>I No EVA
rs242098850 894 A>T No EVA
rs3389213694 904 Q>L No EVA
rs228505930 908 P>L No EVA
rs3389188599 947 G>D No EVA
rs221682026 996 A>T No EVA
rs236534530 1018 D>N No EVA
rs213154038 1020 L>V No EVA
rs259356576 1025 L>S No EVA
rs3411747160 1077 A>V No EVA
rs225071811 1086 F>L No EVA
rs3389207440 1097 T>R No EVA
rs3389225011 1099 G>S No EVA
rs3389188643 1100 D>E No EVA
rs3389216315 1100 D>G No EVA
rs3389183912 1101 L>R No EVA
rs3389211038 1101 L>V No EVA
rs3389210991 1102 F>L No EVA
rs3389216336 1104 Q>* No EVA
rs221480499 1153 I>F No EVA
rs255526154 1159 I>T No EVA
rs223079875 1162 F>Y No EVA
rs255485791 1165 I>T No EVA
rs27050038 1189 I>V No EVA
rs219096617 1198 S>F No EVA
rs3389213783 1214 V>G No EVA
rs3389217347 1216 L>F No EVA
rs3389210220 1217 R>L No EVA
rs27050044 1221 R>S No EVA
rs236450074 1223 F>L No EVA
rs3389183887 1230 T>M No EVA
rs3389216351 1231 D>E No EVA
rs3389176188 1264 T>I No EVA
rs3389207460 1266 N>K No EVA
rs3389214778 1287 E>* No EVA
rs3389207447 1288 Y>* No EVA
rs3389207421 1299 S>R No EVA
rs3389183841 1318 V>I No EVA
rs3389229234 1319 G>* No EVA
rs227065705 1326 A>P No EVA
rs3389176219 1330 T>I No EVA
rs3389183840 1333 K>* No EVA
rs6171634 1351 S>G No EVA
rs245018298 1421 V>M No EVA
rs3389214781 1444 S>T No EVA
rs234849330 1466 T>K No EVA
rs3389148478 1471 L>V No EVA
rs3389213745 1492 S>C No EVA
rs3389229221 1492 S>T No EVA
rs3389207465 1493 G>D No EVA
rs3389211034 1538 A>D No EVA
rs3389217275 1548 M>K No EVA
rs3389188665 1569 T>S No EVA
rs27007088 1600 D>E No EVA
rs3389213766 1614 L>F No EVA
rs1132287258 1620 A>T No EVA

No associated diseases with Q8K442

7 regional properties for Q8K442

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 478 - 713 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1284 - 1517 IPR003439-2
domain AAA+ ATPase domain 506 - 690 IPR003593-1
domain AAA+ ATPase domain 1314 - 1494 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 32 - 416 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 935 - 1157 IPR013525-2
conserved_site ABC transporter-like, conserved site 615 - 629 IPR017871

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
  • Basolateral cell membrane
  • Predominantly expressed on the sinusoidal plasma membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
basolateral plasma membrane The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
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).
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.
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.
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
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.
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.
lipid transporter activity Enables the directed movement of lipids into, out of or within a cell, or between cells.

7 GO annotations of biological process

Name Definition
cholesterol efflux The directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle.
cholesterol transport The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
positive regulation of cholesterol efflux Any process that increases the frequency, rate or extent of cholesterol efflux. Cholesterol efflux is the directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle.
regulation of cholesterol efflux Any process that modulates the frequency, rate or extent of cholesterol efflux. Cholesterol efflux is the directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle.
sphingomyelin biosynthetic process The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
xenobiotic transport The directed movement of a xenobiotic into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. 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.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q86UK0 ABCA12 Glucosylceramide transporter ABCA12 Homo sapiens (Human) PR
P78363 ABCA4 Retinal-specific phospholipid-transporting ATPase ABCA4 Homo sapiens (Human) PR
Q8IUA7 ABCA9 ATP-binding cassette sub-family A member 9 Homo sapiens (Human) PR
Q8N139 ABCA6 ATP-binding cassette sub-family A member 6 Homo sapiens (Human) PR
Q8WWZ4 ABCA10 ATP-binding cassette sub-family A member 10 Homo sapiens (Human) PR
Q8WWZ7 ABCA5 Cholesterol transporter ABCA5 Homo sapiens (Human) PR
Q8K448 Abca5 Cholesterol transporter ABCA5 Mus musculus (Mouse) PR
Q8K449 Abca9 ATP-binding cassette sub-family A member 9 Mus musculus (Mouse) PR
P34358 ced-7 ABC transporter ced-7 Caenorhabditis elegans PR
Q84K47 ABCA2 ABC transporter A family member 2 Arabidopsis thaliana (Mouse-ear cress) PR
Q9FKF2 ABCA11 ABC transporter A family member 11 Arabidopsis thaliana (Mouse-ear cress) PR
Q9FLT5 ABCA9 ABC transporter A family member 9 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MVKREINVCQ QTWALLCKNL LRKKRLKRDT FLEFLYTALI LLSLILFLQL HEVYDFSSLP
70 80 90 100 110 120
DVDLGRIDSF NDSTFMIVYT PITPTTQRIM DRVSLVSYMT GRKILASPNE ENMTELISMR
130 140 150 160 170 180
FSDVVGVIFT NAYSYNLKFI KGARIPTIKE HQDHTAHCHS YGEIIYCGLS EFWRDGFVAL
190 200 210 220 230 240
QAAINAAIIE VTTNHSVMEE MMSLTGKYIK IDSFVGQEGT TTDCFLFFCI IRFSPLTYYI
250 260 270 280 290 300
SAGVTRERKK MKGLMAVMGL RDSAFWLSWG LLYGVIVFVV TLLSTTIVKL VQFVFLTGFM
310 320 330 340 350 360
VIFSLFFFYG LSLISLSFLM SVLLKKSFLT DLVVFLLTVS CGSLGFTALY RYLPVSLEWL
370 380 390 400 410 420
LSLLSPFAFM LGMVQLLRLD YDVNSNADPM GNPNEVIGTI FMLFFDGVFY LLLTFYFEKV
430 440 450 460 470 480
LPSKSFHDKT YWHACKSHFF LIDYSFYIRT ALDNETDYEF SDDSFEPVSM EFHGKEAIRI
490 500 510 520 530 540
RNLTKDYIQK SKRTEALKDL TLDVYKGQIT AILGHSGAGK STLLNVLSGL CVPTKGWVTI
550 560 570 580 590 600
HNNKLSEMTD LENISKLTGV CPQCNVQFDF LTVRENLRLF AKIKGIQAHE VDNEVQRVLL
610 620 630 640 650 660
ELDMKNTQNI LVQNLSGGQK RKLTFGIAIL GDPQIFLLDE PTAGLDPFSR HRVWNFLKER
670 680 690 700 710 720
RADRVVLFST QFMDEADILA DRKVFISKGK LKCAGSSLFL KKKWGIGYHL SLQLSETCVH
730 740 750 760 770 780
ERITSLVKQH IPDSKLSAES EGKLSYILPL ERTNKFPDLY RDLERSPDLG IENYGVSITT
790 800 810 820 830 840
LTEVFLKLEG KSSIDQSDIG MTEDVQAGGA RSPERFAEVE QLVSLLNGRC KMKGGMALWW
850 860 870 880 890 900
QQLCAVTRLR FLKLKHERKS IVILILVLGI GLLHILSANI YRMVRQSDYC WELAPHMYFL
910 920 930 940 950 960
TPGQQPQPPL TNLLIVNKTG AKIDDFIHSL EQQNIALEVD AFGTRNGTED SQYNGAIILS
970 980 990 1000 1010 1020
GDEKNYNFTL ACNTKRLNCF PVLVDIVSNG LLGLFAPSAH IQTDRSTFPE ENDHRKFDYL
1030 1040 1050 1060 1070 1080
AYFFLWVLLM ACVPPYISMT SIDDYKNRAQ FQLWISGLSP SAYWFGQALF EVPVYCALIL
1090 1100 1110 1120 1130 1140
SIFIAFYASA PPESKFTVGD LFIQILYVGG YAMSVIFMTY VISFIYRKGR KNSGLWSLCF
1150 1160 1170 1180 1190 1200
YIVSFFSMCF MLIDYFRDIS LFVLIALVPP ATLGGCTLLH FENREFSEII FEPEREYSYL
1210 1220 1230 1240 1250 1260
FFLAPLLHFA IFVVILRCME RKFGMKTMRT DPVFRISPRS DRVFNNPEDP DGEDEDVSQE
1270 1280 1290 1300 1310 1320
RVWTANALTS ADFQEKPAII ASCLRKEYKG KKKCFVLKSK KKIATRNISF CVRKGEVVGL
1330 1340 1350 1360 1370 1380
LGHNGAGKST SIKMITGETK PSAGQVLLKG SSTGDTPGFL GYCPQENALW LNLTVREHLE
1390 1400 1410 1420 1430 1440
IFAAIKGMRK SDANVAIERL ADALKLQDQL KSPVKTLSEG VKRKLCFVLS ILGNPSVVLL
1450 1460 1470 1480 1490 1500
DEPSTGMDPE GQQQMWQAIQ ATFSNTERGA LLTTHYMAEA EAVCDRVAIM VSGRLRCIGS
1510 1520 1530 1540 1550 1560
IQHLKSKFGK EYLLEMKVKT PSQVEPLNTE IMRLFPQAAR QERYSSLMVY KLPREDVQPL
1570 1580 1590 1600 1610
SQAFFKLETV KQSFDLEEYS LSQSTLEQVF LELSKEQELD GFEEELDPSV KWKLLPQEEA