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 P0CE68

Entry ID Method Resolution Chain Position Source
AF-P0CE68-F1 Predicted AlphaFoldDB

28 variants for P0CE68

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-652743 9 Y>F No SGRP
s11-652871 52 G>R No SGRP
s11-653085 123 S>N No SGRP
s11-653091 125 P>L No SGRP
s11-653139 141 F>Y No SGRP
s11-653432 239 N>D No SGRP
s11-653543 276 D>N No SGRP
s11-653694 326 F>Y No SGRP
s11-653750 345 K>Q No SGRP
s11-654117 467 T>M No SGRP
s11-654410 565 L>F No SGRP
s11-654495 593 T>K No SGRP
s11-654623 636 S>P No SGRP
s11-655113 799 R>K No SGRP
s11-655217 834 C>R No SGRP
s11-655266 850 H>R No SGRP
s11-655299 861 W>* No SGRP
s11-655304 863 V>M No SGRP
s11-655434 906 R>K No SGRP
s11-655479 921 G>E No SGRP
s11-655619 968 S>A No SGRP
s11-655678 987 D>E No SGRP
s11-655710 998 L>R No SGRP
s11-655748 1011 L>I No SGRP
s11-655763 1016 I>V No SGRP
s11-655772 1019 L>F No SGRP
s11-656252 1179 R>G No SGRP
s11-656374 1219 S>Y No SGRP

No associated diseases with P0CE68

5 regional properties for P0CE68

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 651 - 892 IPR003439
domain AAA+ ATPase domain 678 - 869 IPR003593
domain ABC transporter type 1, transmembrane domain 315 - 621 IPR011527-1
domain ABC transporter type 1, transmembrane domain 962 - 1218 IPR011527-2
conserved_site ABC transporter-like, conserved site 792 - 806 IPR017871

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

3 GO annotations of cellular component

Name Definition
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

3 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.

2 GO annotations of biological process

Name Definition
macroautophagy The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P14772 BPT1 Bile pigment transporter 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P38735 VMR1 ABC transporter ATP-binding protein/permease VMR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q96J66 ABCC11 ATP-binding cassette sub-family C member 11 Homo sapiens (Human) PR
Q80WJ6 Abcc12 ATP-binding cassette sub-family C member 12 Mus musculus (Mouse) PR
Q6Y306 Abcc12 ATP-binding cassette sub-family C member 12 Rattus norvegicus (Rat) PR
Q9C8H0 ABCC12 ABC transporter C family member 12 Arabidopsis thaliana (Mouse-ear cress) PR
Q9C8G9 ABCC1 ABC transporter C family member 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q8VZZ4 ABCC6 ABC transporter C family member 6 Arabidopsis thaliana (Mouse-ear cress) PR
Q9M1C7 ABCC9 ABC transporter C family member 9 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MIKNGTCPYW ERDDLSECAR REYIEFKFPL FILLTGMIYA FCKVFRAFYL RGKNHTNEAP
70 80 90 100 110 120
EFEEQGNGNH EYARFSVLRL KSAWESRSFC NVNNRSTFDK FKKFIEGAFI VLQLTIHLYI
130 140 150 160 170 180
LSSMPMDNKK FFHQGFLVQM FLWILLLVVI TLRLISASQS FRWVLACKRD LWAVSFYSYA
190 200 210 220 230 240
SLFTLSILPL RSVFIGKIKD KIMVKYIISE TFIDLALLLL LSTSSIEGTR YSFLVENENK
250 260 270 280 290 300
KLPPAPTVFG LLTFSRIDRL IWKAYKHCLG NADIWDLDIN NKSIAILANF EMSSKKGRLL
310 320 330 340 350 360
PNIICYFKAV FISQLFLAFV SSFLNFVPSL LMPRILSYVN DPKSKSWNLV SLYVSSMLVS
370 380 390 400 410 420
KIIATTCRGQ GLFLGEKGTM QLRTVLISNI YSKTLRRTIL KDSTTSLQKN ASTSFEENPD
430 440 450 460 470 480
SSEAEPRKKS SRKDNSVNNV MSIDAFKVSE AMNTFYLACE AVFMTVTALM ILYSLLGWSA
490 500 510 520 530 540
FAGTFALLAM IPLNFWCATF YGNYQADQLI LTDKRTSGIS EALNSIRVIK LLAWENLFYQ
550 560 570 580 590 600
KIINVRDGEI RLLKKKATIF FLNHLIWFFG PTLVSAITFS VFIKFQNQTL TPTIAFTALS
610 620 630 640 650 660
LFAILRTPMD QIASTVSLLI QSFISLERIQ DYLNESETRK YEILEQSNTK FGFEDASMEW
670 680 690 700 710 720
EAAETSFKLK NISIDFKLNS LNAIIGPTGS GKSSLLLGLL GELNLLSGKI YVPTVESRDD
730 740 750 760 770 780
LEIGKDGMTN SMAYCSQTPW LISGTIKDNV VFGEIFNKQK FDDVMKSCCL DKDIKAMTAG
790 800 810 820 830 840
IRTDVGDGGF SLSGGQQQRI ALARAIYSSS RYLILDDCLS AVDPETALYI YEECLCGPMM
850 860 870 880 890 900
KGRTCIITSH NISLVTKRAD WLVILDRGEV KSQGKPSDLI KSNEFLRESI NNDSKNTTHN
910 920 930 940 950 960
QIDLKRSTTS KKTKNGDPEG GNSQDEVCAE VENFEETKME GSVKFSAYKW LADYFGGLGV
970 980 990 1000 1010 1020
VFVFTSSSIL IHGITLSQGF WLRYWLDTGS SGSKSTWLYR IVEGHSNIYF LLTYIIIGLV
1030 1040 1050 1060 1070 1080
SSFLTSGKVW IAIISGTNVT KKIFAKLLSS ILYAKLRFHN VTPTGRIMNR FSKDMDIIDQ
1090 1100 1110 1120 1130 1140
QLIPNFEGLS YSVVVCLWII LLIGYVTPQF LLFAIPLCAL YYTVCTLYLR ASRELKRIDN
1150 1160 1170 1180 1190 1200
INISPIHQLF AEAIKGVTTI RALADERRFI TQSLVAIDRS NAPFFYLNMA TEWITYRVDI
1210
IGTLVLFSSS VMIIMKAS