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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_MOUSE             Reviewed;         266 AA.
O89051; Q545S7;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 147.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9795190; DOI=10.1016/S0378-1119(98)00354-0;
Pittois K., Deleersnijder W., Merregaert J.;
"cDNA sequence analysis, chromosomal assignment and expression pattern
of the gene coding for integral membrane protein 2B.";
Gene 217:141-149(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
Inoue S., Sano H., Ohta M.;
"Growth suppression of Escherichia coli by induction of expression of
mammalian genes with transmembrane or ATPase domains.";
Biochem. Biophys. Res. Commun. 268:553-561(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Hippocampus, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta
protein 42 into toxic oligomers. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Integral membrane protein 2B: Golgi
apparatus membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass
type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}.
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.
{ECO:0000250|UniProtKB:Q9Y287}.
-!- SUBCELLULAR LOCATION: BRI2, membrane form: Cell membrane
{ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q9Y287}. Endosome membrane
{ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q9Y287}. 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:0000250|UniProtKB:Q9Y287}.
-!- SUBCELLULAR LOCATION: Bri23 peptide: Secreted
{ECO:0000250|UniProtKB:Q9Y287}. Note=Detected in the cerebral
spinal fluid (CSF). {ECO:0000250|UniProtKB:Q9Y287}.
-!- SUBCELLULAR LOCATION: BRI2C, soluble form: Secreted
{ECO:0000250|UniProtKB:Q9Y287}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Glycosylation at Asn-170 is important for cell surface
localization, but doesn't affect furin- and ADAM10-induced
proteolytic processing. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U76253; AAC63851.1; -; mRNA.
EMBL; AB030203; BAA92766.1; -; mRNA.
EMBL; AK002599; BAB22220.1; -; mRNA.
EMBL; AK003587; BAB22877.1; -; mRNA.
EMBL; AK005125; BAB23828.1; -; mRNA.
EMBL; AK076139; BAC36212.1; -; mRNA.
EMBL; AK077482; BAC36822.1; -; mRNA.
EMBL; AK150378; BAE29510.1; -; mRNA.
EMBL; AK151714; BAE30633.1; -; mRNA.
EMBL; AK151889; BAE30773.1; -; mRNA.
EMBL; AK152068; BAE30922.1; -; mRNA.
EMBL; AK152516; BAE31278.1; -; mRNA.
EMBL; AK152650; BAE31387.1; -; mRNA.
EMBL; AK152731; BAE31452.1; -; mRNA.
EMBL; AK152983; BAE31632.1; -; mRNA.
EMBL; AK153103; BAE31723.1; -; mRNA.
EMBL; AK159340; BAE35002.1; -; mRNA.
EMBL; AK159426; BAE35073.1; -; mRNA.
EMBL; AK159619; BAE35235.1; -; mRNA.
EMBL; AK159628; BAE35242.1; -; mRNA.
EMBL; AK159792; BAE35374.1; -; mRNA.
EMBL; AK159962; BAE35517.1; -; mRNA.
EMBL; AK160725; BAE35970.1; -; mRNA.
EMBL; BC004731; AAH04731.1; -; mRNA.
EMBL; BC010320; AAH10320.1; -; mRNA.
EMBL; BC021786; AAH21786.1; -; mRNA.
CCDS; CCDS27269.1; -.
RefSeq; NP_032436.1; NM_008410.2.
UniGene; Mm.4266; -.
ProteinModelPortal; O89051; -.
BioGrid; 200844; 4.
IntAct; O89051; 2.
MINT; O89051; -.
STRING; 10090.ENSMUSP00000022704; -.
iPTMnet; O89051; -.
PhosphoSitePlus; O89051; -.
SwissPalm; O89051; -.
EPD; O89051; -.
MaxQB; O89051; -.
PaxDb; O89051; -.
PeptideAtlas; O89051; -.
PRIDE; O89051; -.
Ensembl; ENSMUST00000022704; ENSMUSP00000022704; ENSMUSG00000022108.
GeneID; 16432; -.
KEGG; mmu:16432; -.
UCSC; uc007ups.1; mouse.
CTD; 9445; -.
MGI; MGI:1309517; Itm2b.
eggNOG; KOG4681; Eukaryota.
eggNOG; ENOG410XRNN; LUCA.
GeneTree; ENSGT00390000005162; -.
HOGENOM; HOG000231259; -.
HOVERGEN; HBG059373; -.
InParanoid; O89051; -.
KO; K18264; -.
OMA; KYFAFQQ; -.
OrthoDB; EOG091G0E78; -.
PhylomeDB; O89051; -.
TreeFam; TF317770; -.
ChiTaRS; Itm2b; mouse.
PRO; PR:O89051; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022108; Expressed in 299 organ(s), highest expression level in stroma of bone marrow.
CleanEx; MM_ITM2B; -.
Genevisible; O89051; MM.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
InterPro; IPR007084; BRICHOS_dom.
Pfam; PF04089; BRICHOS; 1.
SMART; SM01039; BRICHOS; 1.
PROSITE; PS50869; BRICHOS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 266 Integral membrane protein 2B.
/FTId=PRO_0000154822.
CHAIN 1 243 BRI2, membrane form. {ECO:0000250}.
/FTId=PRO_0000417471.
CHAIN 1 ? BRI2 intracellular domain. {ECO:0000250}.
/FTId=PRO_0000417472.
CHAIN ? 243 BRI2C, soluble form. {ECO:0000250}.
/FTId=PRO_0000417473.
PEPTIDE 244 266 Bri23 peptide. {ECO:0000250}.
/FTId=PRO_0000417474.
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.
{ECO:0000250}.
SITE 243 244 Cleavage; by furin. {ECO:0000250}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 89 89 Interchain. {ECO:0000250}.
DISULFID 164 223 {ECO:0000250}.
DISULFID 248 265 {ECO:0000250}.
SEQUENCE 266 AA; 30260 MW; F3EA640D6E600382 CRC64;
MVKVTFNSAL AQKEAKKDEP KSSEEALIVP PDAVAVDCKD PGDVVPVGQR RAWCWCMCFG
LAFMLAGVIL GGAYLYKYFA LQPDDVYYCG LKYIKDDVIL NEPSADAPAA RYQTIEENIK
IFEEDAVEFI SVPVPEFADS DPANIVHDFN KKLTAYLDLN LDKCYVIPLN TSIVMPPKNL
LELLINIKAG TYLPQSYLIH EHMVITDRIE NVDNLGFFIY RLCHDKETYK LQRRETIRGI
QKREASNCFT IRHFENKFAV ETLICS


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