ID   LFG2_PONAB              Reviewed;         316 AA.
AC   Q5R4I4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein lifeguard 2;
DE   AltName: Full=Fas apoptotic inhibitory molecule 2;
GN   Name=FAIM2; Synonyms=LFG2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Antiapoptotic protein which protects cells uniquely from Fas-
CC       induced apoptosis. Regulates Fas-mediated apoptosis in neurons by
CC       interfering with caspase-8 activation. Plays a role in cerebellar
CC       development by affecting cerebellar size, internal granular layer (IGL)
CC       thickness, and Purkinje cell (PC) development (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FAS/TNFRSF6 and BAX. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Membrane raft {ECO:0000250}. Postsynaptic cell
CC       membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR861264; CAH93332.1; -; mRNA.
DR   RefSeq; NP_001126961.1; NM_001133489.1.
DR   AlphaFoldDB; Q5R4I4; -.
DR   SMR; Q5R4I4; -.
DR   STRING; 9601.ENSPPYP00000005137; -.
DR   GeneID; 100173980; -.
DR   KEGG; pon:100173980; -.
DR   CTD; 23017; -.
DR   eggNOG; KOG2322; Eukaryota.
DR   InParanoid; Q5R4I4; -.
DR   OrthoDB; 1290306at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0021681; P:cerebellar granular layer development; ISS:UniProtKB.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISS:UniProtKB.
DR   GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   InterPro; IPR006214; Bax_inhibitor_1-related.
DR   PANTHER; PTHR23291; PTHR23291; 1.
DR   Pfam; PF01027; Bax1-I; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell membrane; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="Protein lifeguard 2"
FT                   /id="PRO_0000326146"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   316 AA;  35094 MW;  269D351BADD84481 CRC64;
     MTQGKLSVAN KAPGTEGQQQ VHGEKKEAPA VPSAPPSYEE ATSGEGMKAG AFPPAPTAVP
     LHPSWAYVDP SSSSSYDNGF PTGDHELFTT FSWDDQKVRR VFVRKVYTIL LIQLLVTLAV
     VALFTFCDPV KDYVQANPGW YWASYAVFFA TYLTLACCSG PRRHFPWNLI LLTVFTLSMA
     YLTGMLSSYY NTTSVLLCLG ITALVCLSVT VFSFQTKFDF TSCQGVLFVL PMTLFFSGLI
     LAILLPFQYV PWLHAVYAAL GAGVFTLFLA LDTQLLMGNR RHSLSPEEYI FGALNIYLDI
     IYIFTFFLQL FGTNRE