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 Q8T6J2

Entry ID Method Resolution Chain Position Source
AF-Q8T6J2-F1 Predicted AlphaFoldDB

No variants for Q8T6J2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8T6J2

No associated diseases with Q8T6J2

8 regional properties for Q8T6J2

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 505 - 739 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1322 - 1557 IPR003439-2
domain AAA+ ATPase domain 533 - 719 IPR003593-1
domain AAA+ ATPase domain 1352 - 1535 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 23 - 390 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 873 - 1264 IPR013525-2
conserved_site ABC transporter-like, conserved site 641 - 655 IPR017871-1
conserved_site ABC transporter-like, conserved site 1459 - 1473 IPR017871-2

Functions

Description
EC Number
Subcellular Localization
  • Membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.

4 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.
lipid transporter activity Enables the directed movement of lipids into, out of or within a cell, or between cells.

3 GO annotations of biological process

Name Definition
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.
sorocarp development The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum.
sorocarp morphogenesis The process in which the sorocarp is generated and organized. An example of this process is found in Dictyostelium discoideum.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGEKSSQLKT LLKKNLLLKS KSKCGICCEI VFPIIIVLLV FAILVLVQLF KPNYDLIKTT
70 80 90 100 110 120
QFSNRINENN IIIYGGKAGS LNVEQKGVID MMKFQLSNEL NKSISEVDVY FKEINDKSEM
130 140 150 160 170 180
ENYFQINSTQ VFGGIWFESN QLSSVANTTN TNTTTNSFKY SIRLDSNSVL DSNKVKDNGI
190 200 210 220 230 240
DSSDYLTKNW AYIQIAMDQA IFGYFGLDYK LVINGQRYPD PYVELWQKWI NGRESVFKSA
250 260 270 280 290 300
GSVFVSAALL IFTFRLVTEL VVEKETKIRE GMSIMGLNQY CYFISWIITS LVTALPIDLI
310 320 330 340 350 360
IIVILKGSQV IHSTSWIIVI VTLILYLLTL QLLAFIFSMF FDKSKFAGLL TFLTILLINI
370 380 390 400 410 420
CGIFIGEYEI INIHIKLLLC CIFSPIGIAC SFYIMSIRDI PDTISTINLN QVISEKQIIG
430 440 450 460 470 480
TFVFNIIFYT FLIWYLDKIV KTEYGTKEPW YFLFTKRYWT VGAGKINKKN KNKEYNYNDI
490 500 510 520 530 540
ESTIQNNNND NIEMVPIEVR NKTTISIRNL RKEFKTGDGL RIAVNDLNLD MFDGQIHGLL
550 560 570 580 590 600
GPNGSGKSTT ISMLTGLLSP TSGTAFILGN DITYQMNEIR KCTGVCLQTD IIWNQLTVLE
610 620 630 640 650 660
HLEIYASLKG ITNKKQIKSE SLKMANEIDL GEKLHTPAGS LSGGQKRKLC LGIAFIGRST
670 680 690 700 710 720
IIFLDEVSSG MDPSSRRKVW DFLLSHKKGK TIILTTHYLD EADYLSDRIS IISHGKLITD
730 740 750 760 770 780
GSSLFLKNKY GVGYLLTCSK SLNTIDQFNV DQVTQFIRDQ IPDVTVLSNA GSEISFRLPT
790 800 810 820 830 840
ASLPVFSKFF KDFDENLSNF HIDSYGISVT TLEEVFLKIG TDIDTDALSI ADGNGNDDEL
850 860 870 880 890 900
KRSIGVSSTG IKSKQQLKAL LIKRVKTSSK DFKAFLLSLL LPLLVIIGSI IVFKEVDNEV
910 920 930 940 950 960
IFYNNSTEPL TFSLLQQYGK NDIVPIQLAG TTSEFDFNKF LSNSPYFNQF QYLNNSINFN
970 980 990 1000 1010 1020
QYLINNYKQS SGSINFTIPL SSSLINNTTK VISYNSLFNF NYIHSWPVHV NLINDALLRN
1030 1040 1050 1060 1070 1080
HNGIGIECTS LPFDHILTSF QKASQGMNIQ SIVYFIVIMM AGFSLMAGSF AGSISQERTN
1090 1100 1110 1120 1130 1140
RIKRLLYISG CKKYIYWVSN LLWDYFFAFI LLLITCIILA IVDDKFNDQF GLFFLSLVLF
1150 1160 1170 1180 1190 1200
SLSIIPLSYL FSFKFSSFGK STGAITAIHF SIGVIMTIAM IILRIEVIIK NSSSLENIAD
1210 1220 1230 1240 1250 1260
IIDIVFNILS PLYAFSRVIF IISGFPGSLR LGALKIDDYW SLHYASTPII ILSVHVVVWT
1270 1280 1290 1300 1310 1320
IFILLIDYSP EFKGYLRNPK TILPPPPPID EDSDVSAERI RLESMSPIPS TDQGSGGGGD
1330 1340 1350 1360 1370 1380
MLQYKGLHKL FIGKGKNPNK NAVYNSTLGI PQGQTFGLLG LNGAGKTTTV SMLAGDILPT
1390 1400 1410 1420 1430 1440
SGQITINGHD LVTDRAQALR GVSVCPQFDA LITLLTAREQ LSLYCAIKGV PDDKISLVVE
1450 1460 1470 1480 1490 1500
AFIKMMDLGK IANSNTGGYS GGNKRKVSLS IAMLGNPSVV LIDEASSGCD PIIRYRQCQV
1510 1520 1530 1540 1550 1560
ISELGKNKVI ILTSHSMSEI QALCSRMTIM RDGQFKCLGS TQHIKSKFGA GYSVEVKFKK
1570 1580 1590 1600 1610 1620
SCLEVGIPQS LQCVLECFPN ATILDQHDLM ASLELPNPPE NPIKVSEIFN ILSTELSSIL
1630 1640 1650 1660
DDYSVSQTSL EQVFLKLTGA THEDRLNLNN QQQQQQTIPN SD