ID   LFG2_MOUSE              Reviewed;         317 AA.
AC   Q8K097; Q3TY22; Q8K1F6; Q9D6K4;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Protein lifeguard 2;
DE   AltName: Full=Fas apoptotic inhibitory molecule 2;
DE   AltName: Full=Neural membrane protein 35;
GN   Name=Faim2; Synonyms=Kiaa0950, Lfg, Lfg2, Nmp35;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Sole C., Segura M.F., Bayascas J.R., Comella J.X.;
RT   "Cloning and characterization of the long form of mouse lifeguard (LFG-L),
RT   an anti Fas-apoptotic molecule.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17635665; DOI=10.1111/j.1471-4159.2007.04767.x;
RA   Fernandez M., Segura M.F., Sole C., Colino A., Comella J.X., Cena V.;
RT   "Lifeguard/neuronal membrane protein 35 regulates Fas ligand-mediated
RT   apoptosis in neurons via microdomain recruitment.";
RL   J. Neurochem. 103:190-203(2007).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19784873; DOI=10.1007/s10495-009-0402-2;
RA   Hu L., Smith T.F., Goldberger G.;
RT   "LFG: a candidate apoptosis regulatory gene family.";
RL   Apoptosis 14:1255-1265(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=21209208; DOI=10.1523/jneurosci.2188-10.2011;
RA   Reich A., Spering C., Gertz K., Harms C., Gerhardt E., Kronenberg G.,
RA   Nave K.A., Schwab M., Tauber S.C., Drinkut A., Harms K., Beier C.P.,
RA   Voigt A., Goebbels S., Endres M., Schulz J.B.;
RT   "Fas/CD95 regulatory protein Faim2 is neuroprotective after transient brain
RT   ischemia.";
RL   J. Neurosci. 31:225-233(2011).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=21957071; DOI=10.1073/pnas.1114226108;
RA   Hurtado de Mendoza T., Perez-Garcia C.G., Kroll T.T., Hoong N.H.,
RA   O'Leary D.D., Verma I.M.;
RT   "Antiapoptotic protein Lifeguard is required for survival and maintenance
RT   of Purkinje and granular cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:17189-17194(2011).
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.
CC       {ECO:0000269|PubMed:17635665, ECO:0000269|PubMed:21209208,
CC       ECO:0000269|PubMed:21957071}.
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:0000269|PubMed:17635665}.
CC       Postsynaptic cell membrane {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, LFG-L;
CC         IsoId=Q8K097-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, LFG-S;
CC         IsoId=Q8K097-2; Sequence=VSP_008994;
CC   -!- TISSUE SPECIFICITY: Brain. Highly expressed in cerebellum, also found
CC       in cortex, olfactory bulb, and hippocampus.
CC       {ECO:0000269|PubMed:17635665, ECO:0000269|PubMed:21957071}.
CC   -!- DISRUPTION PHENOTYPE: Mice show reduced cerebellar size and internal
CC       granular layer (IGL) thickness in early developmental stages, delayed
CC       Purkinje Cell (PC) development, with an abnormal morphology and reduced
CC       cellular density, increased caspase-8 and caspase-3 activity in PCs and
CC       higher sensitivity to Fas-mediated apoptosis.
CC       {ECO:0000269|PubMed:21957071}.
CC   -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98056.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF468028; AAM46781.1; -; mRNA.
DR   EMBL; AK013476; BAB28874.1; -; mRNA.
DR   EMBL; AK030513; BAC26999.1; -; mRNA.
DR   EMBL; AK129246; BAC98056.1; ALT_INIT; mRNA.
DR   EMBL; AK158960; BAE34742.1; -; mRNA.
DR   EMBL; BC032278; AAH32278.1; -; mRNA.
DR   CCDS; CCDS37203.1; -. [Q8K097-1]
DR   CCDS; CCDS88840.1; -. [Q8K097-2]
DR   RefSeq; NP_001033747.1; NM_001038658.2. [Q8K097-2]
DR   RefSeq; NP_082500.2; NM_028224.4. [Q8K097-1]
DR   RefSeq; XP_006521512.1; XM_006521449.3. [Q8K097-1]
DR   AlphaFoldDB; Q8K097; -.
DR   SMR; Q8K097; -.
DR   BioGRID; 215353; 1.
DR   STRING; 10090.ENSMUSP00000023750; -.
DR   GlyCosmos; Q8K097; 1 site, No reported glycans.
DR   GlyGen; Q8K097; 1 site.
DR   iPTMnet; Q8K097; -.
DR   PhosphoSitePlus; Q8K097; -.
DR   SwissPalm; Q8K097; -.
DR   PaxDb; 10090-ENSMUSP00000023750; -.
DR   PeptideAtlas; Q8K097; -.
DR   ProteomicsDB; 291940; -. [Q8K097-1]
DR   ProteomicsDB; 291941; -. [Q8K097-2]
DR   Antibodypedia; 14095; 288 antibodies from 32 providers.
DR   DNASU; 72393; -.
DR   Ensembl; ENSMUST00000023750.9; ENSMUSP00000023750.8; ENSMUSG00000023011.9. [Q8K097-1]
DR   Ensembl; ENSMUST00000231171.2; ENSMUSP00000155195.2; ENSMUSG00000023011.9. [Q8K097-2]
DR   GeneID; 72393; -.
DR   KEGG; mmu:72393; -.
DR   UCSC; uc007xpp.2; mouse. [Q8K097-2]
DR   UCSC; uc007xpq.2; mouse. [Q8K097-1]
DR   AGR; MGI:1919643; -.
DR   CTD; 23017; -.
DR   MGI; MGI:1919643; Faim2.
DR   VEuPathDB; HostDB:ENSMUSG00000023011; -.
DR   eggNOG; KOG2322; Eukaryota.
DR   GeneTree; ENSGT01050000244890; -.
DR   HOGENOM; CLU_058671_3_2_1; -.
DR   InParanoid; Q8K097; -.
DR   OMA; FTGWYVY; -.
DR   OrthoDB; 377780at2759; -.
DR   PhylomeDB; Q8K097; -.
DR   TreeFam; TF319996; -.
DR   BioGRID-ORCS; 72393; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Faim2; mouse.
DR   PRO; PR:Q8K097; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8K097; Protein.
DR   Bgee; ENSMUSG00000023011; Expressed in superior frontal gyrus and 94 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0021681; P:cerebellar granular layer development; IMP:UniProtKB.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:UniProtKB.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:UniProtKB.
DR   GO; GO:0021549; P:cerebellum development; IMP:UniProtKB.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
DR   GO; GO:0002931; P:response to ischemia; IMP:MGI.
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.
DR   Genevisible; Q8K097; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Cell membrane; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..317
FT                   /note="Protein lifeguard 2"
FT                   /id="PRO_0000179088"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         72..84
FT                   /note="SGSSGYEGGFPAG -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008994"
FT   CONFLICT        256
FT                   /note="A -> T (in Ref. 2; BAC98056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="F -> Y (in Ref. 1; AAM46781)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  35258 MW;  A62D51BA49BCDB15 CRC64;
     MTQGKLSVAN KAPGTEGQQH QANGEKKDAP AVPSAPPSYE EATSGEGLKA GTFPQGPTAV
     PLHPSWAYVD PSGSSGYEGG FPAGHHEHFT TFSWDDQKVR RLFIRKVYTI LLVQLLVTLA
     VVALFTFCDV VKDYVQANPG WYWASYAVFF ATYLTLACCS GPRRHFPWNL ILLTIFTLSM
     AYLTGMLSSY YNTTSVLLCL VITALVCLSV TIFSFQTKFD FTSCQGVLFV LLMTLFFSGL
     LLAVLLPFQY VPWLHAVYAV LGAGVFTLFL AFDTQLLMGN RRHSLSPEEY IFGALNIYLD
     IIYIFTFFLQ LFGTNRE
//