ID   LFG2_BOVIN              Reviewed;         316 AA.
AC   Q1LZ71;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Protein lifeguard 2;
DE   AltName: Full=Fas apoptotic inhibitory molecule 2;
GN   Name=FAIM2; Synonyms=LFG2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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}.
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DR   EMBL; BC116167; AAI16168.1; -; mRNA.
DR   RefSeq; NP_001068886.1; NM_001075418.2.
DR   AlphaFoldDB; Q1LZ71; -.
DR   SMR; Q1LZ71; -.
DR   STRING; 9913.ENSBTAP00000063728; -.
DR   GlyCosmos; Q1LZ71; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000023267; -.
DR   Ensembl; ENSBTAT00000068256.1; ENSBTAP00000063728.1; ENSBTAG00000017504.4.
DR   GeneID; 509790; -.
DR   KEGG; bta:509790; -.
DR   CTD; 23017; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017504; -.
DR   VGNC; VGNC:28710; FAIM2.
DR   eggNOG; KOG2322; Eukaryota.
DR   GeneTree; ENSGT01050000244890; -.
DR   HOGENOM; CLU_058671_3_2_1; -.
DR   InParanoid; Q1LZ71; -.
DR   OMA; FTGWYVY; -.
DR   OrthoDB; 377780at2759; -.
DR   TreeFam; TF319996; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000017504; Expressed in prefrontal cortex and 100 other cell types or tissues.
DR   ExpressionAtlas; Q1LZ71; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
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:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   CDD; cd10428; LFG_like; 1.
DR   InterPro; IPR006214; Bax_inhibitor_1-related.
DR   PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR23291:SF18; PROTEIN LIFEGUARD 2; 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_0000326145"
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        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
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;  35184 MW;  64C0898AF6786E03 CRC64;
     MTQGKLSVAN KAPGTEGQQQ ANGEKKETPA VPSAPPSYEE ATSGEGLKAG AFPPAPSAVP
     LHPSWAYVDP NSSSSYESGF PTGDHEFFTT FSWDDQKVRR VFIRKVYTIL LIQLLVTLGV
     VALFTFCDPV KDYVQANPGW YWASYAVFFA TYLTLACCSG PRRHFPWNLI LLTIFTLSMA
     YLTGMLSSYY NTTSVLLCLS ITALVCLSVT VFSFQTKFDF TSCQGVLFVL LMTLFFSGLI
     LAILLPFQYV PWLHAVYAVL GAGVFTLFLA FDTQLLMGSR RHSLSPEEYI FGALNIYLDI
     IYIFTFFLQL FGTNRE
//