ID A0A093FAT4_TYTAL Unreviewed; 226 AA.
AC A0A093FAT4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Integral membrane protein 2 {ECO:0000256|RuleBase:RU367061};
DE Flags: Fragment;
GN ORFNames=N341_02541 {ECO:0000313|EMBL:KFV53655.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV53655.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV53655.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV53655.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of amyloid-beta peptide production. May
CC inhibit the processing of APP by blocking its access to alpha- and
CC beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal
CC fragment is negligible, suggesting that ITM2C is a poor gamma-secretase
CC cleavage inhibitor. May play a role in TNF-induced cell death and
CC neuronal differentiation. {ECO:0000256|ARBA:ARBA00037782}.
CC -!- SUBUNIT: Interacts with BACE1. Interacts with APP. Interacts with
CC STMN2. {ECO:0000256|ARBA:ARBA00038611}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00037874}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00037874}. Membrane
CC {ECO:0000256|RuleBase:RU367061}; Single-pass type II membrane protein
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; KK389671; KFV53655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FAT4; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.150; -; 1.
DR InterPro; IPR007084; BRICHOS_dom.
DR InterPro; IPR040145; ITM2.
DR PANTHER; PTHR10962:SF5; INTEGRAL MEMBRANE PROTEIN 2C; 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|RuleBase:RU367061};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367061};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Signal-anchor {ECO:0000256|RuleBase:RU367061};
KW Transmembrane {ECO:0000256|RuleBase:RU367061};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367061}.
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367061"
FT DOMAIN 95..189
FT /note="BRICHOS"
FT /evidence="ECO:0000259|PROSITE:PS50869"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV53655.1"
FT NON_TER 226
FT /evidence="ECO:0000313|EMBL:KFV53655.1"
SQ SEQUENCE 226 AA; 26257 MW; F941FE8AAF373DF2 CRC64;
EELAPAVQGR RSSLSGVCYL TMGLLVLLLG LVFASMYVYR YFFITQLPRE SVFHCGVLYE
DSLYSPFKGQ LELHEDVKIY IEENYEQINV PVPQFGGSDP ADIIHDFQRG LTAYHDITLD
KCYVIELNTT IVMPPRNLWE LLVNVKKGTY LPQTYIIQEE MIATEHVSDM EQLGSFIYRL
CSGKETYRLK RRSARRRISR REAGNCHRIR HFENTFVVET VICKKS
//
