AiPD: Autoinhibited Protein Database

Gene name	Lmln
Protein name	Leishmanolysin-like peptidase
Names
Species	Mus musculus (Mouse)
KEGG Pathway	mmu:239833
EC number
Protein Class

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

1-82 (Predicted disordered autoinhibitory region) PR

1-82 (Predicted disordered autoinhibitory region)

cis-regPred

No accessory elements

Entry ID	Method	Resolution	Chain	Position	Source
AF-Q8BMN4-F1	Predicted				AlphaFoldDB

Variant ID(s)	Position	Change	Diseaes Association	Provenance
rs214899330	8	G>R	No	EVA
rs263661790	18	G>S	No	EVA
rs3389416544	72	N>K	No	EVA
rs3389411476	73	H>Y	No	EVA
rs3389423712	169	E>K	No	EVA
rs3389416552	191	D>G	No	EVA
rs3389393120	229	K>Q	No	EVA
rs3389412417	261	H>R	No	EVA
rs3389423669	273	L>P	No	EVA
rs3389428901	373	L>I	No	EVA
rs3389428938	417	G>*	No	EVA
rs3389428926	462	R>*	No	EVA
rs260168342	490	P>S	No	EVA
rs3406876082	499	G>R	No	EVA
rs582950717	500	S>A	No	EVA
rs4171218	559	I>V	No	EVA
rs3389411542	561	E>*	No	EVA
rs3389393104	565	R>G	No	EVA
rs3389362438	572	W>L	No	EVA
rs3389419407	592	D>G	No	EVA
rs3389393050	608	I>T	No	EVA
rs238884045	640	A>V	No	EVA
rs3389428895	644	R>Q	No	EVA
rs3389412355	659	V>F	No	EVA

Type	Name	Position	InterPro Accession
No domain, repeats, and functional sites for Q8BMN4

		Description
EC Number
Subcellular Localization	Cytoplasm Lipid droplet	Found in ring-like structures resembling invadopodia In migrating cells it relocalizes from internal structures to the leading edge of cells (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category	No pathway information available

Name	Definition
cytoplasm	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol	The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
focal adhesion	A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
lipid droplet	An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
membrane	A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

Name	Definition
metal ion binding	Binding to a metal ion.
metalloendopeptidase activity	Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
peptidase activity	Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.

Name	Definition
cell adhesion	The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
cell cycle	The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division	The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
proteolysis	The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
Q96KR4	LMLN	Leishmanolysin-like peptidase	Homo sapiens (Human)	PR