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Integral membrane protein 2B (Immature BRI2) (imBRI2) (Protein E25B) (Transmembrane protein BRI) (Bri) [Cleaved into: BRI2, membrane form (Mature BRI2) (mBRI2); BRI2 intracellular domain (BRI2 ICD); BRI2C, soluble form; Bri23 peptide (Bri2-23) (ABri23) (C-terminal peptide) (P23 peptide)]

 ITM2B_HUMAN             Reviewed;         266 AA.
Q9Y287; Q5W0A3; Q96B24; Q9NYH1;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=Integral membrane protein 2B;
AltName: Full=Immature BRI2;
Short=imBRI2;
AltName: Full=Protein E25B;
AltName: Full=Transmembrane protein BRI;
Short=Bri;
Contains:
RecName: Full=BRI2, membrane form;
AltName: Full=Mature BRI2;
Short=mBRI2;
Contains:
RecName: Full=BRI2 intracellular domain;
Short=BRI2 ICD;
Contains:
RecName: Full=BRI2C, soluble form;
Contains:
RecName: Full=Bri23 peptide;
Short=Bri2-23;
AltName: Full=ABri23;
AltName: Full=C-terminal peptide;
AltName: Full=P23 peptide;
Name=ITM2B; Synonyms=BRI, BRI2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN CAA-ITM2B1, AND VARIANT
CAA-ITM2B1 ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS.
TISSUE=Pituitary;
PubMed=10391242; DOI=10.1038/21637;
Vidal R., Frangione B., Rostagno A., Mead S., Revesz T., Plant G.,
Ghiso J.;
"A stop-codon mutation in the BRI gene associated with familial
British dementia.";
Nature 399:776-781(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN CAA-ITM2B2, AND VARIANT
CAA-ITM2B2 SER-266 DELINS
PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR.
PubMed=10781099; DOI=10.1073/pnas.080076097;
Vidal R., Revesz T., Rostagno A., Kim E., Holton J.L., Bek T.,
Bojsen-Moeller M., Braendgaard H., Plant G., Ghiso J., Frangione B.;
"A decamer duplication in the 3' region of the BRI gene originates an
amyloid peptide that is associated with dementia in a Danish
kindred.";
Proc. Natl. Acad. Sci. U.S.A. 97:4920-4925(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
Ren S., Shi J., Huang C., Jiang C., Li Y., Zhou J., Yu Y., Xu S.,
Wang Y., Fu G., Chen Z., Han Z.;
"A novel gene expressed in human adrenal gland.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-15.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-15.
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INVOLVEMENT IN RDGCA, AND VARIANT RDGCA ALA-261.
PubMed=24026677; DOI=10.1093/hmg/ddt439;
Audo I., Bujakowska K., Orhan E., El Shamieh S., Sennlaub F.,
Guillonneau X., Antonio A., Michiels C., Lancelot M.E., Letexier M.,
Saraiva J.P., Nguyen H., Luu T.D., Leveillard T., Poch O., Dollfus H.,
Paques M., Goureau O., Mohand-Said S., Bhattacharya S.S., Sahel J.A.,
Zeitz C.;
"The familial dementia gene revisited: a missense mutation revealed by
whole-exome sequencing identifies ITM2B as a candidate gene underlying
a novel autosomal dominant retinal dystrophy in a large family.";
Hum. Mol. Genet. 23:491-501(2014).
[10]
CHARACTERIZATION OF VARIANT CAA-ITM2B1
ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS, TOPOLOGY,
CLEAVAGE BY FURIN, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=10526337; DOI=10.1038/14783;
Kim S.H., Wang R., Gordon D.J., Bass J., Steiner D.F., Lynn D.G.,
Thinakaran G., Meredith S.C., Sisodia S.S.;
"Furin mediates enhanced production of fibrillogenic ABri peptides in
familial British dementia.";
Nat. Neurosci. 2:984-988(1999).
[11]
FUNCTION, TOPOLOGY, PROTEOLYTIC CLEAVAGE, CHARACTERIZATION OF VARIANT
CAA-ITM2B1 ARG-THR-VAL-LYS-LYS-ASN-ILE-ILE-GLU-GLU-ASN-266 INS,
CHARACTERIZATION OF VARIANT CAA-ITM2B2 SER-266 DELINS
PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR, AND SUBCELLULAR
LOCATION.
PubMed=14656991; DOI=10.1096/fj.03-0730fje;
Choi S.I., Vidal R., Frangione B., Levy E.;
"Axonal transport of British and Danish amyloid peptides via secretory
vesicles.";
FASEB J. 18:373-375(2004).
[12]
FUNCTION, AND INTERACTION WITH APP.
PubMed=15983050; DOI=10.1074/jbc.C500217200;
Matsuda S., Giliberto L., Matsuda Y., Davies P., McGowan E.,
Pickford F., Ghiso J., Frangione B., D'Adamio L.;
"The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta
precursor protein and inhibits amyloid-beta production.";
J. Biol. Chem. 280:28912-28916(2005).
[13]
FUNCTION, AND INTERACTION WITH APP.
PubMed=16027166; DOI=10.1074/jbc.C500231200;
Fotinopoulou A., Tsachaki M., Vlavaki M., Poulopoulos A., Rostagno A.,
Frangione B., Ghiso J., Efthimiopoulos S.;
"BRI2 interacts with amyloid precursor protein (APP) and regulates
amyloid beta (Abeta) production.";
J. Biol. Chem. 280:30768-30772(2005).
[14]
CHARACTERIZATION OF VARIANT CAA-ITM2B2 SER-266 DELINS
PHE-ASN-LEU-PHE-LEU-ASN-SER-GLN-GLU-LYS-HIS-TYR.
PubMed=16091362; DOI=10.1074/jbc.M504038200;
Tomidokoro Y., Lashley T., Rostagno A., Neubert T.A.,
Bojsen-Moller M., Braendgaard H., Plant G., Holton J., Frangione B.,
Revesz T., Ghiso J.;
"Familial Danish dementia: co-existence of Danish and Alzheimer
amyloid subunits (ADan AND A{beta}) in the absence of compact
plaques.";
J. Biol. Chem. 280:36883-36894(2005).
[15]
SUBCELLULAR LOCATION, TOPOLOGY, CLEAVAGE BY ADAM10; FURIN; SPPL2A AND
SPPL2B, INTERACTION WITH SPPL2A AND SPPL2B, AND MUTAGENESIS OF
243-ARG-GLU-244.
PubMed=17965014; DOI=10.1074/jbc.M706661200;
Martin L., Fluhrer R., Reiss K., Kremmer E., Saftig P., Haass C.;
"Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and
SPPL2a/SPPL2b.";
J. Biol. Chem. 283:1644-1652(2008).
[16]
FUNCTION OF SECRETED BRI23 PEPTIDE, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18524908; DOI=10.1523/JNEUROSCI.0891-08.2008;
Kim J., Miller V.M., Levites Y., West K.J., Zwizinski C.W.,
Moore B.D., Troendle F.J., Bann M., Verbeeck C., Price R.W.,
Smithson L., Sonoda L., Wagg K., Rangachari V., Zou F., Younkin S.G.,
Graff-Radford N., Dickson D., Rosenberry T., Golde T.E.;
"BRI2 (ITM2b) inhibits Abeta deposition in vivo.";
J. Neurosci. 28:6030-6036(2008).
[17]
FUNCTION.
PubMed=18753367; DOI=10.1523/JNEUROSCI.2094-08.2008;
Matsuda S., Giliberto L., Matsuda Y., McGowan E.M., D'Adamio L.;
"BRI2 inhibits amyloid beta-peptide precursor protein processing by
interfering with the docking of secretases to the substrate.";
J. Neurosci. 28:8668-8676(2008).
[18]
CLEAVAGE BY ADAM10; FURIN AND SPPL2B, AND SUBCELLULAR LOCATION.
PubMed=19114711; DOI=10.1074/jbc.M807485200;
Martin L., Fluhrer R., Haass C.;
"Substrate requirements for SPPL2b-dependent regulated intramembrane
proteolysis.";
J. Biol. Chem. 284:5662-5670(2009).
[19]
FUNCTION OF SECRETED BRI23 PEPTIDE, SUBUNIT, INTERACTION WITH APP
AMYLOID-BETA PROTEIN 40, DISULFIDE BOND, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20036644; DOI=10.1016/j.bbrc.2009.12.122;
Peng S., Fitzen M., Jornvall H., Johansson J.;
"The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-
23) and amyloid beta-peptide (Abeta1-40): Implications for Bri2
effects on processing of amyloid precursor protein and Abeta
aggregation.";
Biochem. Biophys. Res. Commun. 393:356-361(2010).
[20]
SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=18440095; DOI=10.1016/j.neurobiolaging.2008.03.004;
Tsachaki M., Ghiso J., Rostagno A., Efthimiopoulos S.;
"BRI2 homodimerizes with the involvement of intermolecular disulfide
bonds.";
Neurobiol. Aging 31:88-98(2010).
[21]
CLEAVAGE BY ADAM10; FURIN AND SPPL2B, GLYCOSYLATION AT ASN-170,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-170.
PubMed=21752865; DOI=10.1093/glycob/cwr097;
Tsachaki M., Serlidaki D., Fetani A., Zarkou V., Rozani I., Ghiso J.,
Efthimiopoulos S.;
"Glycosylation of BRI2 on asparagine 170 is involved in its
trafficking to the cell surface but not in its processing by furin or
ADAM10.";
Glycobiology 21:1382-1388(2011).
[22]
FUNCTION OF MBRI2 IN APP PROCESSING INHIBITION, INTERACTION WITH APP
AMYLOID-BETA A4 AND APP C99, PROTEOLYTIC CLEAVAGE, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 243-ARG-GLU-244.
PubMed=19748705; DOI=10.1016/j.neurobiolaging.2009.08.005;
Matsuda S., Matsuda Y., Snapp E.L., D'Adamio L.;
"Maturation of BRI2 generates a specific inhibitor that reduces APP
processing at the plasma membrane and in endocytic vesicles.";
Neurobiol. Aging 32:1400-1408(2011).
[23]
FUNCTION OF MBRI2 IN APP PROCESSING INHIBITION, AND INTERACTION WITH
APP AMYLOID-BETA A4 AND APP C99.
PubMed=22170863; DOI=10.1002/emmm.201100195;
Tamayev R., Matsuda S., Arancio O., D'Adamio L.;
"beta- but not gamma-secretase proteolysis of APP causes synaptic and
memory deficits in a mouse model of dementia.";
EMBO Mol. Med. 4:171-179(2012).
[24]
CLEAVAGE BY SPPL2A AND SPPL2B, AND MUTAGENESIS OF GLY-60.
PubMed=22194595; DOI=10.1074/jbc.M111.328104;
Fluhrer R., Martin L., Klier B., Haug-Kroper M., Grammer G.,
Nuscher B., Haass C.;
"The alpha-helical content of the transmembrane domain of the British
dementia protein-2 (Bri2) determines its processing by signal peptide
peptidase-like 2b (SPPL2b).";
J. Biol. Chem. 287:5156-5163(2012).
-!- FUNCTION: Plays a regulatory role in the processing of the
amyloid-beta A4 precursor protein (APP) and acts as an inhibitor
of the amyloid-beta 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.
-!- FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the
amyloid-beta A4 precursor protein (APP) processing leading to a
strong reduction in the secretion of secretase-processed amyloid-
beta protein 40 and amyloid-beta protein 42.
-!- FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta
protein 42 into toxic oligomers.
-!- SUBUNIT: 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 amyloid-beta protein 40. {ECO:0000269|PubMed:15983050,
ECO:0000269|PubMed:16027166, ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:18440095, ECO:0000269|PubMed:19748705,
ECO:0000269|PubMed:20036644, ECO:0000269|PubMed:22170863}.
-!- INTERACTION:
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-2866431, EBI-749265;
Q58DX5:NAALADL2; NbExp=3; IntAct=EBI-2866431, EBI-10178964;
Q8N205:SYNE4; NbExp=3; IntAct=EBI-2866431, EBI-7131783;
-!- SUBCELLULAR LOCATION: Integral membrane protein 2B: Golgi
apparatus membrane {ECO:0000269|PubMed:14656991,
ECO:0000269|PubMed:19114711}; Single-pass type II membrane protein
{ECO:0000269|PubMed:10526337}. 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.
-!- SUBCELLULAR LOCATION: BRI2, membrane form: Cell membrane
{ECO:0000269|PubMed:18440095, ECO:0000269|PubMed:19748705,
ECO:0000269|PubMed:21752865}; Single-pass type II membrane protein
{ECO:0000269|PubMed:10526337}. Endosome membrane
{ECO:0000269|PubMed:19748705}; Single-pass type II membrane
protein {ECO:0000269|PubMed:10526337}. 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. {ECO:0000269|PubMed:19748705}.
-!- SUBCELLULAR LOCATION: Bri23 peptide: Secreted
{ECO:0000269|PubMed:10526337, ECO:0000269|PubMed:14656991,
ECO:0000269|PubMed:18524908}. Note=Detected in the cerebral spinal
fluid (CSF). {ECO:0000269|PubMed:18524908}.
-!- SUBCELLULAR LOCATION: BRI2C, soluble form: Secreted
{ECO:0000269|PubMed:17965014}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y287-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y287-2; Sequence=VSP_055326;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in brain.
-!- PTM: 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.
-!- PTM: Glycosylation at Asn-170 is important for cell surface
localization, but doesn't affect furin- and ADAM10-induced
proteolytic processing. {ECO:0000269|PubMed:21752865}.
-!- DISEASE: Cerebral amyloid angiopathy, ITM2B-related 1 (CAA-ITM2B1)
[MIM:176500]: A disorder characterized by amyloid deposition in
the walls of cerebral blood vessels and neurodegeneration in the
central nervous system. Cerebral amyloid angiopathy, non-neuritic
and perivascular plaques and neurofibrillary tangles are the
predominant pathological lesions. Clinical features include
progressive mental deterioration, spasticity and muscular
rigidity. {ECO:0000269|PubMed:10391242,
ECO:0000269|PubMed:10526337, ECO:0000269|PubMed:14656991}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. A single base substitution at the stop
codon of ITM2B generates a 277-residue precursor that is cleaved
at the normal furin processing site to generate the ABri
amyloidogenic peptide (PubMed:10391242). ABri accumulates in the
brain and produces amyloid fibrils responsible for neuronal
dysfunction and dementia. ABri peptide variant forms fibrils in
vitro (PubMed:10526337). {ECO:0000269|PubMed:10391242,
ECO:0000269|PubMed:10526337}.
-!- DISEASE: Cerebral amyloid angiopathy, ITM2B-related 2 (CAA-ITM2B2)
[MIM:117300]: A disorder characterized by amyloid deposition in
the walls of the blood vessels of the cerebrum, choroid plexus,
cerebellum, spinal cord and retina. Plaques and neurofibrillary
tangles are observed in the hippocampus. Clinical features include
progressive ataxia, dementia, cataracts and deafness.
{ECO:0000269|PubMed:10781099, ECO:0000269|PubMed:14656991,
ECO:0000269|PubMed:16091362}. Note=The disease is caused by
mutations affecting the gene represented in this entry. A decamer
duplication in the 3' region of ITM2B results in the production of
the ADan amyloidogenic peptide (PubMed:10781099). ADan is
generated by cleavage of the mutated precursor at the normal furin
processing site. ADan accumulates in the brain and produces
amyloid fibrils responsible for neuronal dysfunction and dementia.
{ECO:0000269|PubMed:10781099}.
-!- DISEASE: Retinal dystrophy with inner retinal dysfunction and
ganglion cell abnormalities (RDGCA) [MIM:616079]: An autosomal
dominant retinal dystrophy characterized by inner retinal
dysfunction in association with ganglion cell abnormalities.
Clinical features include mild photophobia, progressive loss of
central vision, night blindness, and hyperreflectivity of nerve
and ganglion cell layers. {ECO:0000269|PubMed:24026677}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/itm2b/";
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EMBL; AF152462; AAD45280.1; -; mRNA.
EMBL; AF246221; AAF66130.1; -; mRNA.
EMBL; AF136973; AAG49434.1; -; mRNA.
EMBL; AF092128; AAD40370.1; -; mRNA.
EMBL; BT006863; AAP35509.1; -; mRNA.
EMBL; AY341247; AAP88930.1; -; Genomic_DNA.
EMBL; CH471075; EAX08789.1; -; Genomic_DNA.
EMBL; CH471075; EAX08790.1; -; Genomic_DNA.
EMBL; BC000554; AAH00554.1; -; mRNA.
EMBL; BC016148; AAH16148.1; -; mRNA.
CCDS; CCDS9409.1; -. [Q9Y287-1]
RefSeq; NP_068839.1; NM_021999.4. [Q9Y287-1]
UniGene; Hs.643683; -.
ProteinModelPortal; Q9Y287; -.
BioGrid; 114835; 34.
IntAct; Q9Y287; 19.
STRING; 9606.ENSP00000367828; -.
iPTMnet; Q9Y287; -.
PhosphoSitePlus; Q9Y287; -.
SwissPalm; Q9Y287; -.
BioMuta; ITM2B; -.
DMDM; 12643343; -.
EPD; Q9Y287; -.
PaxDb; Q9Y287; -.
PeptideAtlas; Q9Y287; -.
PRIDE; Q9Y287; -.
TopDownProteomics; Q9Y287-1; -. [Q9Y287-1]
DNASU; 9445; -.
Ensembl; ENST00000378549; ENSP00000367811; ENSG00000136156. [Q9Y287-2]
Ensembl; ENST00000378565; ENSP00000367828; ENSG00000136156. [Q9Y287-1]
GeneID; 9445; -.
KEGG; hsa:9445; -.
UCSC; uc001vbz.4; human. [Q9Y287-1]
CTD; 9445; -.
DisGeNET; 9445; -.
EuPathDB; HostDB:ENSG00000136156.12; -.
GeneCards; ITM2B; -.
HGNC; HGNC:6174; ITM2B.
HPA; HPA029292; -.
HPA; HPA071992; -.
MalaCards; ITM2B; -.
MIM; 117300; phenotype.
MIM; 176500; phenotype.
MIM; 603904; gene.
MIM; 616079; phenotype.
neXtProt; NX_Q9Y287; -.
OpenTargets; ENSG00000136156; -.
Orphanet; 97345; Familial dementia, British type.
Orphanet; 97346; Familial dementia, Danish type.
Orphanet; 397758; Retinal dystrophy with inner retinal dysfunction and ganglion cell anomalies.
PharmGKB; PA29971; -.
eggNOG; KOG4681; Eukaryota.
eggNOG; ENOG410XRNN; LUCA.
GeneTree; ENSGT00390000005162; -.
HOGENOM; HOG000231259; -.
HOVERGEN; HBG059373; -.
InParanoid; Q9Y287; -.
KO; K18264; -.
OMA; KYFAFQQ; -.
OrthoDB; EOG091G0E78; -.
PhylomeDB; Q9Y287; -.
TreeFam; TF317770; -.
Reactome; R-HSA-977225; Amyloid fiber formation.
ChiTaRS; ITM2B; human.
GeneWiki; ITM2B; -.
GenomeRNAi; 9445; -.
PRO; PR:Q9Y287; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136156; -.
CleanEx; HS_ITM2B; -.
ExpressionAtlas; Q9Y287; baseline and differential.
Genevisible; Q9Y287; HS.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB.
GO; GO:0031301; C:integral component of organelle membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
InterPro; IPR007084; BRICHOS_dom.
Pfam; PF04089; BRICHOS; 1.
SMART; SM01039; BRICHOS; 1.
PROSITE; PS50869; BRICHOS; 1.
1: Evidence at protein level;
Alternative splicing; Amyloid; Amyloidosis; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Deafness;
Disease mutation; Disulfide bond; Endosome; Glycoprotein;
Golgi apparatus; Membrane; Neurodegeneration; Reference proteome;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 266 Integral membrane protein 2B.
/FTId=PRO_0000045840.
CHAIN 1 243 BRI2, membrane form.
/FTId=PRO_0000417464.
CHAIN 1 ? BRI2 intracellular domain.
/FTId=PRO_0000417465.
CHAIN ? 243 BRI2C, soluble form.
/FTId=PRO_0000417466.
PEPTIDE 244 266 Bri23 peptide.
/FTId=PRO_0000016545.
TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.
TRANSMEM 55 75 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 76 266 Lumenal. {ECO:0000255}.
DOMAIN 137 231 BRICHOS. {ECO:0000255|PROSITE-
ProRule:PRU00255}.
REGION 102 134 Necessary for interaction with APP and
inhibitor effects on APP processing.
SITE 243 244 Cleavage; by furin.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21752865}.
DISULFID 89 89 Interchain.
DISULFID 164 223 {ECO:0000250}.
DISULFID 248 265 Interchain (between ADan peptide
variants).
VAR_SEQ 83 188 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_055326.
VARIANT 15 15 A -> T (in dbSNP:rs11556905).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_071047.
VARIANT 261 261 E -> A (in RDGCA; dbSNP:rs606231283).
{ECO:0000269|PubMed:24026677}.
/FTId=VAR_072434.
VARIANT 266 266 S -> FNLFLNSQEKHY (in CAA-ITM2B2; amyloid
ADan; colocalizes with APP amyloid-beta
protein 42 in parenchymal and vascular
lesions; interacts with APP amyloid-beta
protein 42; oligomerizes and is subjected
to disulfide bond formation; undergoes
cyclic pyroglutamate formation on the N-
terminus Gln residues and is further
proteolytically cleaved in the cerebral
cortex). {ECO:0000269|PubMed:10781099,
ECO:0000269|PubMed:14656991,
ECO:0000269|PubMed:16091362}.
/FTId=VAR_010240.
VARIANT 266 266 S -> SRTVKKNIIEEN (in CAA-ITM2B1; amyloid
ABri). {ECO:0000269|PubMed:10391242,
ECO:0000269|PubMed:10526337,
ECO:0000269|PubMed:14656991}.
/FTId=VAR_010239.
MUTAGEN 60 60 G->V: Reduces strongly intramembrane
cleavage by SPPL2B.
{ECO:0000269|PubMed:22194595}.
MUTAGEN 170 170 N->A: Accumulates in intracellular
compartments. Does not inhibit furin,
ADAM10 and SPPL2A extracellular
proteolytic processing activity.
{ECO:0000269|PubMed:21752865}.
MUTAGEN 243 244 RE->AA: Inhibits cleavage by furin. Does
not prevent ADAM10 shedding.
{ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:19748705}.
SEQUENCE 266 AA; 30338 MW; 3A7D8CA259F1F627 CRC64;
MVKVTFNSAL AQKEAKKDEP KSGEEALIIP PDAVAVDCKD PDDVVPVGQR RAWCWCMCFG
LAFMLAGVIL GGAYLYKYFA LQPDDVYYCG IKYIKDDVIL NEPSADAPAA LYQTIEENIK
IFEEEEVEFI SVPVPEFADS DPANIVHDFN KKLTAYLDLN LDKCYVIPLN TSIVMPPRNL
LELLINIKAG TYLPQSYLIH EHMVITDRIE NIDHLGFFIY RLCHDKETYK LQRRETIKGI
QKREASNCFA IRHFENKFAV ETLICS


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