ID G1LAI8_AILME Unreviewed; 266 AA.
AC G1LAI8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Integral membrane protein 2 {ECO:0000256|RuleBase:RU367061};
GN Name=ITM2B {ECO:0000313|Ensembl:ENSAMEP00000003911.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000003911.1, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000003911.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000003911.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_002919158.1; XM_002919112.2.
DR AlphaFoldDB; G1LAI8; -.
DR STRING; 9646.ENSAMEP00000003911; -.
DR Ensembl; ENSAMET00000004069.2; ENSAMEP00000003911.1; ENSAMEG00000003662.2.
DR GeneID; 100475802; -.
DR KEGG; aml:100475802; -.
DR CTD; 9445; -.
DR eggNOG; KOG4681; Eukaryota.
DR GeneTree; ENSGT00950000183115; -.
DR HOGENOM; CLU_074596_0_0_1; -.
DR InParanoid; G1LAI8; -.
DR OMA; YFAFQQD; -.
DR OrthoDB; 3664639at2759; -.
DR TreeFam; TF317770; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
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 3: Inferred from homology;
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:UP000008912};
KW Signal-anchor {ECO:0000256|RuleBase:RU367061};
KW Transmembrane {ECO:0000256|RuleBase:RU367061};
KW Transmembrane helix {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; 30447 MW; FC2DC321B558F9FD CRC64;
MVKVTFNSAL AQKETKKDEP KCGEEALIIP PDAVAVDCKD PDEVVPVGQR RAWCWCMCFG
LAFMLAGVIL GGAYLYKYFA LQPDDVYYCG IKYIKDDVIL NEPSADAPAA RYQTIEENIK
IFEEDEVEFI SVPVPEFADS DPANIVHDFN KKLTAYLDLN LDKCYVIPLN TSIVMPPRNL
LELLINIKAG TYLPQSYLIH EHMVITDRIE NVDHLGFFIY RLCHDKETYK LQRRETIRGI
QKREVSNCVT IRHFENKFAV ETVICP
//
