Primary Information |
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| BoMiProt ID | Bomi6418 |
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| Protein Name | Integral membrane protein 2B/Immature BRI2/Transmembrane protein BRI/ABri23/C-terminal peptide/P23 peptide |
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| Organism | Bos taurus |
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| Uniprot ID | Q3T0P7 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001030265.1 |
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| Aminoacid Length | 266 |
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| Molecular Weight | 30400 |
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| FASTA Sequence |
Download |
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| Gene Name | ITM2B |
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| Gene ID | 510575 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein 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. |
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| Biochemical Properties | The type II integral membrane protein (Itm2) family consists of Itm2a, Itm2b, and Itm2c. The homology of amino acid sequences in Itm2 family members between mouse and human was very high, up to 91%–94%. Itm2a is 38% identical to Itm2b and 49% identical to Itm2c, and Itm2b is 49% identical to Itm2c. All three members of the Itm2 family show different expression patterns. |
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| PTMs | Disulfide bond formation,N-Linked Glycosylation at Asn |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q3T0P7|ITM2B_BOVIN Integral membrane protein 2B OS=Bos taurus OX=9913 GN=ITM2B PE=2 SV=1
MVKVTFNSALAQKEAKKDESKSGEEALIIPPDAVAVDCKDPDEVVPVGQRRAWCWCMCFG
LAFMLAGVILGGAYLYKYFAFQPDDVYYCGIKYIKDDVILNEPSADAPASRYQTIEENIK
IFEEDEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLN*170TSIVMPPKNL
LELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFYIYRLCHDKETYKLQRRETIKGI
QKRSADVCVTIRHFENRFAVETLICP
|
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (52-74) |
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| Significance of PTMs | 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.Glycosylation at Asn-170 is important for cell surface localization, but doesn't affect furin- and ADAM10-induced proteolytic processing. |
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| Additional Comments | Itm2b expression in epididymis and vas deferens was significantly decreased after the Leydig cells were destroyed by ethylene dimethane sulfonate. |
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| Bibliography | 1.Rengaraj D, Liang XH, Gao F, Deng WB, Mills N, Yang ZM. Differential expression and regulation of integral membrane protein 2b in rat male reproductive tissues. Asian J Androl. 2008 May;10(3):503-11.doi:10.1111/j.1745-7262.2008.00360.x. Epub 2007 Dec 20. PMID: 18097506. 2. Pittois K, Deleersnijder W, Merregaert J. cDNA sequence analysis, chromosomal assignment and expression pattern of the gene coding for integral membrane protein 2B. Gene 1998;217: 141–9. 3.Choi SC, Kim J, Kim TH, Cho SY, Park SS, Kim KD, et al. Cloning and characterization of a type II integral transmembrane protein gene, Itm2c, that is highly expressed in the mouse brain. Mol Cells 2001; 12: 391–7. 4.Deleersnijder W, Hong G, Cortvrindt R, Poirier C, Tylzanowski
P, Pittois K, et al. Isolation of markers for chondro-osteogenic
differentiation using cDNA library subtraction – molecular
cloning and characterization of a gene belonging to a novel
multigene family of integral membrane proteins. J Biol Chem
1996; 271: 19475–82. |
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