Protein detail
SPPL3
Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23.-) (Intramembrane protease 2) (IMP-2) (Presenilin homologous protein 1) (PSH1) (Presenilin-like protein 4)
Entry name SPPL3 | UniProt ID | EVMP score 0.50 |
Frequency 1 | Transmembrane count 9 | Protein classification EnzymesPredicted membrane proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23.-) (Intramembrane protease 2) (IMP-2) (Presenilin homologous protein 1) (PSH1) (Presenilin-like protein 4)
Protein Class
EnzymesPredicted membrane proteins
Protein Function
- Peptidases:Aspartic-type peptidases
- Enzymes
Transmembrane
9..29; Helical; 75..95; Helical; 98..118; Helical; 137..159; Helical; 165..185; Helical; 191..211; Helical; 263..283; Helical; 312..332; Helical; 340..360; Helical
Transmembrane Count
9
Ensembl
Entrez Gene Symbol
Gene Synonym
DKFZP586C1324IMP2MGC126674MGC126676MGC90402PSL4
Gene Description
Signal peptide peptidase like 3
Chromosome
12
Position
120762510-120904358
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Tissue Specificsalivary glandCell SpecificBasal prostatic cellsSingle-Nuclei Brain Specificmedium spiny neuron
Function & Pathway
Protein Function
- Peptidases:Aspartic-type peptidases
- Enzymes
Cellular Component
- GO:0005791 rough endoplasmic reticulum
- GO:0005794 Golgi apparatus
- GO:0005886 plasma membrane
- GO:0016020 membrane
- GO:0030660 Golgi-associated vesicle membrane
- GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane
- GO:0043231 intracellular membrane-bounded organelle
- GO:0098553 lumenal side of endoplasmic reticulum membrane
- GO:0098554 cytoplasmic side of endoplasmic reticulum membrane
Molecular Function
Biological Process
Mediation Categories
Fusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
12 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | No | No |
| transmembrane | transmembrane | TopDB | No | No | No | No | No |
| transmembrane | transmembrane | LOCATE | No | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
0 records.
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Mass spectrometry | 0 |
Sequence, Structure & Domains
Sequences
Length
384
Mass
42,261
Sequence
MAEQTYSWAYSLVDSSQVSTFLISILLIVYGSFRSLNMDFENQDKEKDSNSSSGSFNGNSTNNSIQTIDSTQALFLPIGASVSLLVMFFFFDSVQVVFTICTAVLATIAFAFLLLPMCQYLTRPCSPQNKISFGCCGRFTAAELLSFSLSVMLVLIWVLTGHWLLMDALAMGLCVAMIAFVRLPSLKVSCLLLSGLLIYDVFWVFFSAYIFNSNVMVKVATQPADNPLDVLSRKLHLGPNVGRDVPRLSLPGKLVFPSSTGSHFSMLGIGDIVMPGLLLCFVLRYDNYKKQASGDSCGAPGPANISGRMQKVSYFHCTLIGYFVGLLTATVASRIHRAAQPALLYLVPFTLLPLLTMAYLKGDLRRMWSEPFHSKSSSSRFLEV
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=2; IsoId=Q8TCT6-2; Sequence=Displayed; Name=3; IsoId=Q8TCT6-3; Sequence=VSP_005205
Alternative Sequence
1..215; Missing (in isoform 3)
3D Structural Models
Domain & Motif Annotations
Motif
341..343; PAL
Domain (CC)
The first transmembrane domain may act as a type I signal anchor (PubMed:15385547). The catalytic loops is exposed toward the lumen (PubMed:15385547). The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family (By similarity).
Protein Families
Peptidase A22B family
Sequence Similarities
Belongs to the peptidase A22B family.