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Database: UniProt
Entry: F7B0D0_MACMU
LinkDB: F7B0D0_MACMU
Original site: F7B0D0_MACMU 
ID   F7B0D0_MACMU            Unreviewed;       266 AA.
AC   F7B0D0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Integral membrane protein 2 {ECO:0000256|RuleBase:RU367061};
GN   Name=ITM2B {ECO:0000313|EMBL:AFH34711.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000010359.2,
GN   ECO:0000313|VGNC:VGNC:73799};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000010359.2, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000010359.2, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000010359.2,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFH34711.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Orbital {ECO:0000313|EMBL:AFJ70944.1}, Testis
RC   {ECO:0000313|EMBL:AFI33588.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH34711.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000010359.2}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000010359.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta
CC       protein 42 into toxic oligomers. {ECO:0000256|ARBA:ARBA00037053}.
CC   -!- FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the amyloid-
CC       beta A4 precursor protein (APP) processing leading to a strong
CC       reduction in the secretion of secretase-processed amyloid-beta protein
CC       40 and amyloid-beta protein 42. {ECO:0000256|ARBA:ARBA00037187}.
CC   -!- FUNCTION: Plays a regulatory role in the processing of the amyloid-beta
CC       A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta
CC       peptide aggregation and fibrils deposition. Plays a role in the
CC       induction of neurite outgrowth. Functions as a protease inhibitor by
CC       blocking access of secretases to APP cleavage sites.
CC       {ECO:0000256|ARBA:ARBA00037249}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Endosome membrane {ECO:0000256|ARBA:ARBA00004639}; Single-pass type II
CC       membrane protein {ECO:0000256|ARBA:ARBA00004639}. Golgi apparatus
CC       membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU367061}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU367061}.
CC   -!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000256|ARBA:ARBA00006794,
CC       ECO:0000256|RuleBase:RU367061}.
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DR   EMBL; JU477907; AFH34711.1; -; mRNA.
DR   EMBL; JV043517; AFI33588.1; -; mRNA.
DR   EMBL; JV635604; AFJ70944.1; -; mRNA.
DR   RefSeq; NP_001244984.1; NM_001258055.1.
DR   SMR; F7B0D0; -.
DR   STRING; 9544.ENSMMUP00000010359; -.
DR   PaxDb; 9544-ENSMMUP00000010359; -.
DR   Ensembl; ENSMMUT00000011048.4; ENSMMUP00000010359.2; ENSMMUG00000007888.4.
DR   GeneID; 709896; -.
DR   KEGG; mcc:709896; -.
DR   CTD; 9445; -.
DR   VEuPathDB; HostDB:ENSMMUG00000007888; -.
DR   VGNC; VGNC:73799; ITM2B.
DR   eggNOG; KOG4681; Eukaryota.
DR   GeneTree; ENSGT00950000183115; -.
DR   HOGENOM; CLU_074596_0_0_1; -.
DR   OMA; YFAFQQD; -.
DR   OrthoDB; 3664639at2759; -.
DR   TreeFam; TF317770; -.
DR   Proteomes; UP000006718; Chromosome 17.
DR   Bgee; ENSMMUG00000007888; Expressed in cerebellum and 22 other cell types or tissues.
DR   ExpressionAtlas; F7B0D0; baseline.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007084; BRICHOS_dom.
DR   InterPro; IPR040145; ITM2.
DR   PANTHER; PTHR10962:SF4; INTEGRAL MEMBRANE PROTEIN 2B; 1.
DR   PANTHER; PTHR10962; INTEGRAL TRANSMEMBRANE PROTEIN 2; 1.
DR   Pfam; PF04089; BRICHOS; 1.
DR   SMART; SM01039; BRICHOS; 1.
DR   PROSITE; PS50869; BRICHOS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367061};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Signal-anchor {ECO:0000256|RuleBase:RU367061};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367061};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367061}.
FT   TRANSMEM        52..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367061"
FT   DOMAIN          137..231
FT                   /note="BRICHOS"
FT                   /evidence="ECO:0000259|PROSITE:PS50869"
SQ   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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