Protein detail

RAI2

Retinoic acid-induced protein 2

Entry name RAI2	UniProt ID Q9Y5P3	EVMP confidence score 0.38
Supporting publications (n) 1	Transmembrane count	Protein classification Predicted intracellular proteins

EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information10

Protein Names

Retinoic acid-induced protein 2

Protein Class

Predicted intracellular proteins

Protein Function

Predicted intracellular proteins

Ensembl

ENSG00000131831

Entrez Gene Symbol

RAI2

Gene Description

Retinoic acid induced 2

Chromosome

Position

17800049-17861337

Supporting publications (n)

EVMP confidence score

0.38

Fluorescence & Localization4

Cell SpecificAlveolar cells type 1Blood Cell SpecificgdT-cellBlood Lineage SpecificT-cells

Function & Pathway5

Protein Function

Predicted intracellular proteins

Cellular Component (2)

Molecular Function (2)

Biological Process (3)

Mediation Categories

Other mediation

Relations & Evidence6

Ligand-Receptor Signaling (3)

3 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	OmniPath	No	No	No	No	No

Protein Complex Composition (2)

2 records.

Component Name	Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs	References
	CTBP2 RAI2	P56545 Q9Y5P3	4:3	PDB	PDB:8ati
	CTBP1 RAI2	Q13363 Q9Y5P3	24:10	PDB	PDB:8ari

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
	Mass spectrometry	0

Sequence, Structure & Domains8

Sequences

Length

530

Mass

57,180

Sequence

MDDLQSQNLSMDMTDSPPALANNRLENGMAQLITTEAWNINSTDLVKKALVTVPAPSILNPPAESQSGMALKVAATVLQPLCLGESPVVMPIHMQVEGSSAPELNPNGNATYVMTTQGPVQLPVVLEQHVFQHLNSPLVLPQEAPCSSSTIHNNLFQGAEDPEAQPQLLDLRIPSQPQEPTLPFEAVLQNLFPSQGTLGPPPCQPPPGYAPVPPQPFSSPLSPLVPPATLLVPYPVIVPLPVPVPIPIPIPMPQSSESKFSSSFPKPPSSFGLHPFKGTQTPLEKDELKPFDILQPKEYFQLSRHTVIKMGSENEALDLSMKSVPWLKAGEVSPPIFQEDAALDLSVAAHRKSEPPPETLYDSGASVDSSGHTVMEKLPSGMEISFAPATSHEAPAMMDSHISSSDAATEMLSQPNHPSGEVKAENNIEMVGESQAAKVIVSVEDAVPTIFCGKIKGLSGVSTKNFSFKREDSVLQGYDINSQGEESMGNAEPLRKPIKNRSIKLKKVNSQEIHMLPIKKQRLATFFPRK

Alternative Products

Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9Y5P3-1; Sequence=Displayed; Name=2; IsoId=Q9Y5P3-2; Sequence=VSP_047524

Alternative Sequence

46..95; Missing (in isoform 2)

3D Structural Models

3D Structure

Electron microscopy (1); X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias

1..13; Polar residues

Region

1..22; Disordered

Clinical Relevance4

Antibody

HPA051054

Interaction Protein (3)

ENSG00000159692ENSG00000175029ENSG00000197860

Interaction Count

Interaction Dataset

intact_biogrid

Supporting Publications1

PMID	Title	Abstract
34265469	Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.	Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.