Protein detail
SPP2B
Signal peptide peptidase-like 2B (SPP-like 2B) (SPPL2b) (EC 3.4.23.-) (Intramembrane protease 4) (IMP-4) (Presenilin homologous protein 4) (PSH4) (Presenilin-like protein 1)
Protein symbol SPP2B | UniProt ID | EVMP score 0.50 |
Frequency 2 | 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 2B (SPP-like 2B) (SPPL2b) (EC 3.4.23.-) (Intramembrane protease 4) (IMP-4) (Presenilin homologous protein 4) (PSH4) (Presenilin-like protein 1)
Protein Class
EnzymesPredicted membrane proteins
Protein Function
- Peptidases:Aspartic-type peptidases
- Enzymes
Transmembrane
175..195; Helical; 222..244; Helical; 249..271; Helical; 294..314; Helical; 320..340; Helical; 349..369; Helical; 413..433; Helical; 446..466; Helical; 471..491; Helical
Transmembrane Count
9
Ensembl
Entrez Gene Symbol
Gene Synonym
IMP4KIAA1532PSL1
Gene Description
Signal peptide peptidase like 2B
Chromosome
19
Position
2328615-2355095
Frequency
2
EVMP Score
0.50
Fluorescence & Localization
Tissue SpecificliverCell SpecificcDCSingle-Nuclei Brain Specificcentral nervous system macrophageBlood Cell Specificplasmacytoid DCBlood Lineage Specificdendritic cellsSecretome LocationIntracellular and membraneSecretome FunctionReceptor
Function & Pathway
Protein Function
- Peptidases:Aspartic-type peptidases
- Enzymes
Cellular Component
- GO:0000139 Golgi membrane
- GO:0005654 nucleoplasm
- GO:0005765 lysosomal membrane
- GO:0005813 centrosome
- GO:0005886 plasma membrane
- GO:0010008 endosome membrane
- GO:0015629 actin cytoskeleton
- GO:0016020 membrane
- GO:0030660 Golgi-associated vesicle membrane
- GO:0098553 lumenal side of endoplasmic reticulum membrane
- GO:0098554 cytoplasmic side of endoplasmic reticulum membrane
Molecular Function
Biological Process
Canonical Pathways
- M5883 Naba secreted factors
- M5885 Naba matrisome associated
- M5889 Naba matrisome
Mediation Categories
Fusion and delivery mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
18 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | Yes | No |
| intracellular | intracellular | GO_Intercell | No | No | No | Yes | No |
| intracellular | intracellular | UniProt_location | No | No | No | Yes | No |
| intracellular | intracellular | OmniPath | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | Yes | No |
| transmembrane | transmembrane | TopDB | No | No | No | Yes | No |
| transmembrane | transmembrane | LOCATE | No | No | No | Yes | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | Yes | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationDensity Gradient CentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyMicrofluidics-Based Methods | Mass spectrometry | 41 | 3371834237862381392904593994949028054239315085003410865938225453398737264122729640545963394435443279541434341426231615132450511426801919268848412772398430550287306087003229583333709510337292553420285537926697390229904078452922106071273124283768636638164498384909583076053841216884403116164009145531588238331147683132059137309723 |
Sequence, Structure & Domains
Sequences
Length
592
Mass
64,644
Sequence
MAAAVAAALARLLAAFLLLAAQVACEYGMVHVVSQAGGPEGKDYCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAALYAPKEPVLDYNMVIIFIMAVGTVAIGGYWAGSRDVKKRYMKHKRDDGPEKQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYDLLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHKRPQARMLLLALFCVAVSVVWGVFRNEDQWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFLTKSGSSIMVEVATGPSDSATREKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFAKVLPPSPWAPAPADGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAESEGRDQAQPSPVTQPGASA
Alternative Products
Event=Alternative splicing; Named isoforms=3; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=Q8TCT7-1; Sequence=Displayed; Name=2; IsoId=Q8TCT7-2; Sequence=VSP_005204; Name=4; IsoId=Q8TCT7-4; Sequence=VSP_009221, VSP_009222
Alternative Sequence
320..592; Missing (in isoform 2); 506..511; KVLPPS -> VNTSLL (in isoform 4); 512..592; Missing (in isoform 4)
3D Structural Models
Domain & Motif Annotations
Compositional Bias
512..524; Pro residues; 580..592; Polar residues
Motif
472..474; PAL
Domain (CC)
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; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP.
Domain (FT)
71..149; PA
Region
512..592; Disordered
Protein Families
Peptidase A22B family
Sequence Similarities
Belongs to the peptidase A22B family.