Integral membrane protein 2B - Rattus norvegicus (Rat)

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Q5XIE8 (ITM2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Integral membrane protein 2B

Alternative name(s):
Immature BRI2
Short name=imBRI2
Transmembrane protein BRI
Short name=Bri

Cleaved into the following 4 chains:

BRI2, membrane form
Alternative name(s):
Mature BRI2
Short name=mBRI2
BRI2 intracellular domain
Short name=BRI2 ICD
BRI2C, soluble form
Bri23 peptide
Short name=Bri2-23
Alternative name(s):
ABri23
C-terminal peptide
P23 peptide

Gene names

Name:

Itm2b

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Plays a regulatory role in the processing of the beta-amyloid A4 precursor protein (APP) and acts as an inhibitor of the beta-amyloid peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites By similarity. Mature BRI2 (mBRI2) functions as a modulator of the beta-amyloid A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed beta-amyloid protein 40 and beta-amyloid protein 42 By similarity. Bri23 peptide prevents aggregation of APP beta-amyloid protein 42 peptide into toxic oligomers By similarity.
Subunit structure	Homodimer; disulfide-linked. Interacts with SPPL2A and SPPL2B. Interacts with APP. Mature BRI2 (mBRI2) interacts with the APP amyloid beta A4 protein; the interaction occurs at the cell surface and in the endocytic compartments and enable alpha- and beta-secretase-induced APP cleavage inhibition. Mature BRI2 (mBRI2) interacts with the APP C99; the interaction occurs in the endocytic compartments and enable gamma-secretase-induced C99 cleavage inhibition. May form heterodimers with Bri23 peptide and APP beta-amyloid protein 40 By similarity.
Subcellular location	Integral membrane protein 2B: Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Note: Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted By similarity. BRI2, membrane form: Cell membrane; Single-pass type II membrane protein By similarity. Endosome membrane; Single-pass type II membrane protein By similarity. Note: Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing By similarity. Bri23 peptide: Secreted By similarity. Note: Detected in the cerebral spinal fluid (CSF) By similarity. BRI2C, soluble form: Secreted By similarity.
Post-translational modification	The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragment (BRI2C, membrane form) is further proteolytically processed by SPPL2A and SPPL2B through regulated intramembrane proteolysis producing a secreted C-peptide and a BRI2 intracellular domain (BRI2 ICD) released in the cytosol. Shedding by ADAM10 facilitates intramembrane cleavage but is not absolutely required for BRI2 ICD generation By similarity. Glycosylation at Asn-170 is important for cell surface localization, but doesn't affect furin- and ADAM10-induced proteolytic processing By similarity.
Sequence similarities	Belongs to the ITM2 family. Contains 1 BRICHOS domain.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara negative regulation of amyloid precursor protein biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi-associated vesicle membrane Inferred from sequence or structural similarity. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from sequence or structural similarity. Source: UniProtKB integral to organelle membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara beta-amyloid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 266

266

Integral membrane protein 2B

PRO_0000154824

Chain

1 – 243

243

BRI2, membrane form By similarity

PRO_0000417487

Chain

1 – ?

BRI2 intracellular domain By similarity

PRO_0000417488

Chain

? – 243

BRI2C, soluble form By similarity

PRO_0000417489

Peptide

244 – 266

Bri23 peptide By similarity

PRO_0000417490

Regions

Topological domain

1 – 54

Cytoplasmic Potential

Transmembrane

55 – 75

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

76 – 266

191

Lumenal Potential

Domain

137 – 231

BRICHOS

Region

102 – 134

Necessary for interaction with APP and inhibitor effects on APP processing By similarity

Sites

Site

243 – 244

Cleavage; by furin By similarity

Amino acid modifications

Glycosylation

170

N-linked (GlcNAc...) Potential

Disulfide bond

Interchain By similarity

Disulfide bond

164 ↔ 223

By similarity

Disulfide bond

248 ↔ 265

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5XIE8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: E3925091C653C449
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FASTA

266

30,314

        10         20         30         40         50         60 
MVKVTFNSAL AQKEAKKDEP KSSEEALIAP PDAVAVDCKD PDDVVPVGQR RAWCWCMCFG 

        70         80         90        100        110        120 
LAFMLAGVIL GGAYLYKYFA LQPDDVYYCG LKYIKDDVIL SEPSADAPAA RYQTIEENIK 

       130        140        150        160        170        180 
IFEEDAVEFI SVPVPEFADS DPANIVHDFN KKLTAYLDLN LDKCYVIPLN TSIVMPPRNL 

       190        200        210        220        230        240 
LELLINIKAG TYLPQSYLIH EHMVITDRIE NVDHLGFFIY RLCHDKETYK LQRRETIRGI 

       250        260 
QKREASNCFT IRHFENKFAV ETLICS

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References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC083735 mRNA. Translation: AAH83735.1.
IPI	IPI00211916.
RefSeq	NP_001006964.1. NM_001006963.1.
UniGene	Rn.107335.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000023037.
PTM databases
PhosphoSite	Q5XIE8.
Proteomic databases
PaxDb	Q5XIE8.
PRIDE	Q5XIE8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000023037; ENSRNOP00000023037; ENSRNOG00000016271.
GeneID	290364.
KEGG	rno:290364.
UCSC	RGD:620727. rat.
Organism-specific databases
CTD	9445.
RGD	620727. Itm2b.
Phylogenomic databases
eggNOG	NOG283703.
GeneTree	ENSGT00390000005162.
HOGENOM	HOG000231259.
HOVERGEN	HBG059373.
InParanoid	Q5XIE8.
OMA	VDHLGFF.
OrthoDB	EOG48D0WD.
Gene expression databases
Genevestigator	Q5XIE8.
GermOnline	ENSRNOG00000016271. Rattus norvegicus.
Family and domain databases
InterPro	IPR007084. BRICHOS_dom. [Graphical view]
Pfam	PF04089. BRICHOS. 1 hit. [Graphical view]
SMART	SM01039. BRICHOS. 1 hit. [Graphical view]
PROSITE	PS50869. BRICHOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	630989.

Entry information

Entry name

ITM2B_RAT

Accession

Primary (citable) accession number: Q5XIE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	November 23, 2004
Last modified:	April 3, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 4 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents