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 Q7ZYJ3

Entry ID Method Resolution Chain Position Source
AF-Q7ZYJ3-F1 Predicted AlphaFoldDB

No variants for Q7ZYJ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7ZYJ3

No associated diseases with Q7ZYJ3

2 regional properties for Q7ZYJ3

Type Name Position InterPro Accession
domain Diacylglycerol kinase, catalytic domain 61 - 202 IPR001206
domain Acylglycerol kinase, C-terminal 209 - 422 IPR045579

Functions

Description
EC Number 2.7.1.94 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
  • Mitochondrion intermembrane space
  • Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane
  • It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
integral component of mitochondrial inner membrane The component of the mitochondrial inner membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial intermembrane space The region between the inner and outer lipid bilayers of the mitochondrial envelope.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
TIM22 mitochondrial import inner membrane insertion complex A multi-subunit complex embedded in the mitochondrial inner membrane that mediates the inner membrane insertion of multi-transmembrane spanning proteins that contain internal targeting elements. In yeast cells, TIM22 is a 300-kDa complex, consisting of four membrane integral subunits, Tim22, Tim54, Tim18 and Sdh3, and a peripheral chaperone complex consisting of the small TIM proteins, Tim9-Tim10-Tim12.

5 GO annotations of molecular function

Name Definition
acylglycerol kinase activity Catalysis of the reaction: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ceramide kinase activity Catalysis of the reaction: ATP + ceramide = ADP + ceramide-1-phosphate.
diacylglycerol kinase activity Catalysis of the reaction: NTP + 1,2-diacylglycerol = NDP + 1,2-diacylglycerol-3-phosphate.
dihydroceramide kinase activity Catalysis of the reaction: ATP + a dihydroceramide = ADP + H+ + a dihydroceramide 1-phosphate.

2 GO annotations of biological process

Name Definition
glycerolipid metabolic process The chemical reactions and pathways involving glycerolipids, any lipid with a glycerol backbone. Diacylglycerol and phosphatidate are key lipid intermediates of glycerolipid biosynthesis.
protein insertion into mitochondrial inner membrane The processes mediating the insertion of proteins into the mitochondrial inner membrane. Mitochondrial inner membrane proteins can get inserted from the cytosol, by crossing the outer membrane and being guided by an inner membrane translocase complex into their final destination in the inner membrane. Some proteins present in the intermembrane space can get inserted into the inner mitochondrial membrane. Finally, some proteins are inserted into the inner membrane from the matrix side of the membrane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MARVVRIFKT LRNHWKKSTV GFCLLAYGSH WLYGKHCDNL LRRAACEEAQ VFGNHQILPH
70 80 90 100 110 120
SAIKKATVFL NPAACKGKAR TLFEKNAAPV LHLAGIDITV VKTDYEGQAK KLLELMEKTD
130 140 150 160 170 180
LIIVAGGDGT VQEVITGLLR RDDEASFSKI PIGFIPLGGT NTLSHTLYPE RENKVEQITE
190 200 210 220 230 240
ATLSILKGET VPLDVLQIKG EQDQPVFAVQ GIRWGSYRDA SVKVSKYWYL GPLKARAAHL
250 260 270 280 290 300
FSALKEWPQQ HQASISYLGP AERPPEEPEQ KPSRPPLYVR IYRRLALYWS PPKVEVPVEP
310 320 330 340 350 360
TPEPWEEAQL SAVELSITTQ NHQPDLLRTL DSMSIHIEPD TISKGKFIQL GAQKMTDPLL
370 380 390 400 410 420
HPEDSQVLLA SRCSLHLPQG TEGHFSIDSE EYEAMSVDVT LLPRKLHFLC HPTRKQELLQ
SPTATAQS