P53264

PR
Gene name
CLD1 (YGR110W, G6140)
Protein name
Cardiolipin-specific deacylase 1, mitochondrial
Names
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YGR110W
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-138 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P53264

Entry ID Method Resolution Chain Position Source
AF-P53264-F1 Predicted AlphaFoldDB

8 variants for P53264

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-713745 11 R>S No SGRP
s07-713785 25 S>P No SGRP
s07-713792 27 N>S No SGRP
s07-713810 33 P>L No SGRP
s07-714106 132 K>E No SGRP
s07-714428 239 Y>C No SGRP
s07-714526 272 V>I No SGRP
s07-714924 404 R>S No SGRP

No associated diseases with P53264

1 regional properties for P53264

Type Name Position InterPro Accession
domain Alpha/beta hydrolase fold-1 142 - 430 IPR000073

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

3 GO annotations of molecular function

Name Definition
carboxylic ester hydrolase activity Catalysis of the hydrolysis of a carboxylic ester bond.
lysophosphatidic acid acyltransferase activity Catalysis of the transfer of acyl groups from an acyl-CoA to lysophosphatidic acid to form phosphatidic acid.
phospholipase A2 activity Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = 1-acyl-sn-glycero-3-phospholipid + a fatty acid. This reaction removes the fatty acid attached to the sn2-position. Substrates include phosphatidylcholine, phosphatidylethanolamine, choline plasmalogen and phosphatides.

4 GO annotations of biological process

Name Definition
cardiolipin acyl-chain remodeling Remodeling the acyl chains of premature (de novo synthesized) cardiolipin (1,3-bis(3-phosphatidyl)glycerol), through sequential deacylation and re-acylation reactions, to generate mature cardiolipin containing high-levels of unsaturated fatty acids.
cardiolipin metabolic process The chemical reactions and pathways involving cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
lipid homeostasis Any process involved in the maintenance of an internal steady state of lipid within an organism or cell.
phosphatidic acid biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q04623 ECM18 Protein ECM18 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MFKSTLNSII RRPLKGFQLL RGADSSNTRP QSPRASARDV TEKQILRTPS APTAIPLREI
70 80 90 100 110 120
IYRVPSLFPR PLEDSVKDFR DFIKNEDAFQ TELLKTLPFY PTPSESKTAR LIRTVVDDEG
130 140 150 160 170 180
NYINEFCIRP RKTSVPEADL KHLVFIHGYG AGLGFFIKNF EDIPLLDNEW CIHAIDLPGY
190 200 210 220 230 240
GFSSRPKFPF EYPRDNIHSV QDWFHERIHT WFSKRNLLNR PEKNIVMAHS LGSYLMALYL
250 260 270 280 290 300
QKYKESPSFK KLILCSPAGV SYRDFNNTAS EVEKWKPPPW WYVKLWDRNI SPFTLVRNFR
310 320 330 340 350 360
QLGSKITSGW SYRRFKHILN GDPEQSKRFE ALHRYAYAIF NKRGSGEYLL SFALKCGGEP
370 380 390 400 410 420
RLSLEQQLFD GKKSDILKNS NCDWLWLYGD DDWMDVNGGL RVSRFLKEKL KQKSNVIIVP
430 440
HSGHHLYLDN YKFFNNILTK EMQKI