LFG2_RAT
ID LFG2_RAT Reviewed; 316 AA.
AC O88407;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=Lfg, Lfg2, Nmp35;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9698393; DOI=10.1006/mcne.1998.0697;
RA Schweitzer B., Taylor V., Welcher A.A., McClelland M., Suter U.;
RT "Neural membrane protein 35 (NMP35): a novel member of a gene family which
RT is highly expressed in the adult nervous system.";
RL Mol. Cell. Neurosci. 11:260-273(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12414123; DOI=10.1016/s0169-328x(02)00445-x;
RA Schweitzer B., Suter U., Taylor V.;
RT "Neural membrane protein 35/Lifeguard is localized at postsynaptic sites
RT and in dendrites.";
RL Brain Res. Mol. Brain Res. 107:47-56(2002).
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:0000269|PubMed:12414123};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12414123}. Membrane
CC raft {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:12414123}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels on dendrites and to a
CC lesser extent on the soma and axons of neurons in various regions of
CC brain. {ECO:0000269|PubMed:12414123}.
CC -!- DEVELOPMENTAL STAGE: Low expression was detected in brain and spinal
CC cord at birth, increasing with age to highest levels in postnatal days
CC 60 (P60). {ECO:0000269|PubMed:9698393}.
CC -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
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DR EMBL; AF044201; AAC32463.1; -; mRNA.
DR EMBL; BC087606; AAH87606.1; -; mRNA.
DR RefSeq; NP_653357.1; NM_144756.2.
DR AlphaFoldDB; O88407; -.
DR SMR; O88407; -.
DR BioGRID; 251568; 1.
DR STRING; 10116.ENSRNOP00000039775; -.
DR GlyGen; O88407; 1 site.
DR iPTMnet; O88407; -.
DR PhosphoSitePlus; O88407; -.
DR PaxDb; O88407; -.
DR PRIDE; O88407; -.
DR Ensembl; ENSRNOT00000072309; ENSRNOP00000064487; ENSRNOG00000045554.
DR GeneID; 246274; -.
DR KEGG; rno:246274; -.
DR UCSC; RGD:628744; rat.
DR CTD; 23017; -.
DR RGD; 628744; Faim2.
DR eggNOG; KOG2322; Eukaryota.
DR GeneTree; ENSGT01050000244890; -.
DR HOGENOM; CLU_058671_3_2_1; -.
DR InParanoid; O88407; -.
DR OMA; YPGDTEM; -.
DR OrthoDB; 1290306at2759; -.
DR PhylomeDB; O88407; -.
DR TreeFam; TF319996; -.
DR PRO; PR:O88407; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000053258; Expressed in frontal cortex and 7 other tissues.
DR Genevisible; O88407; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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:0007417; P:central nervous system development; IEP:RGD.
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; ISO:RGD.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
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; ISO:RGD.
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_0000179089"
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..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
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; 35036 MW; 8A0FA4E4312A14F7 CRC64;
MTQGKLSVAN KAPGTEGQQQ ANGEKKDAPA VPSAPPSYEE ATSGEGLKAG AFPQGPTAVP
LHPSWAYVDP SSSSGYEGGF PAGHHELFST FSWDDQKVRQ LFIRKVYTIL LVQLLVTLAV
VALFTFCDVV KDYVQANPGW YWASYAVFFA TYLTLACCSG PRRHFPWNLI LLTIFTLSMA
YLTGMLSSYY NTTSVLLCLG ITALVCLSVT IFSFQTKFDF TSCHGVLFVL LMTLFFSGLL
LAILLPFQYV PWLHAVYAVL GAGVFTLFLA FDTQLLMGNR RHSLSPEEYI FGALNIYLDI
IYIFTFFLQL FGTNRE
