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 P50903

Entry ID Method Resolution Chain Position Source
AF-P50903-F1 Predicted AlphaFoldDB

No variants for P50903

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P50903

No associated diseases with P50903

3 regional properties for P50903

Type Name Position InterPro Accession
domain PLAT/LH2 domain 355 - 465 IPR001024
domain Lipase 18 - 352 IPR013818
domain Lipase, N-terminal 51 - 348 IPR033906

Functions

Description
EC Number 3.1.1.3 Carboxylic ester hydrolases
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity Catalysis of the reaction: all-trans-retinyl palmitate + H2O = all-trans-retinol + H+ + palmitate.
metal ion binding Binding to a metal ion.
triglyceride lipase activity Catalysis of the reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate.

1 GO annotations of biological process

Name Definition
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLLLWILSLF LETVAGGEVC FDRLGCFSDN KPWAGTSERP RKGLPWDPSA INVRFLLYTN
70 80 90 100 110 120
ENPNNYQRIT ADSSVIRSSD FKTDRKTRFI IHGFIDKGEE NWLADLCKAL FQVESVNCIC
130 140 150 160 170 180
VDWRGGSRTL YSQASQNIQV VGAEVAYLIN FLQSQLDYPP SSVHIIGHSL GSHAAGEAGR
190 200 210 220 230 240
RTNGAIGRIT GLDPAEPYFQ YTPEIVRLDP SDAQFVDVIH TDGNPIIPNL GFGMSQTVGH
250 260 270 280 290 300
LDFFPNGGLQ MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYIDS ITNPKGFAGF
310 320 330 340 350 360
SCDSYSSFSS NKCFPCATGE CPQMGHYADK FPGKTKENFQ NFYLNTGDKS NFSRWRYRIA
370 380 390 400 410 420
VTLSGQKVTG HVLVSLFGDA GNTKQYEIYR GSLKPGNNHS NEIDSDVDVG DLQKVKFIWY
430 440 450 460
NNVINITLPK VGASRITVTR SDGRVFDFCS QDTVREEVLL TLQPC