FAIM3_RAT
ID FAIM3_RAT Reviewed; 426 AA.
AC Q5M871;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Fas apoptotic inhibitory molecule 3 {ECO:0000250|UniProtKB:O60667};
DE AltName: Full=IgM Fc fragment receptor {ECO:0000250|UniProtKB:O60667, ECO:0000312|RGD:1359282};
DE AltName: Full=Regulator of Fas-induced apoptosis Toso {ECO:0000250|UniProtKB:O60667};
DE Flags: Precursor;
GN Name=Fcmr {ECO:0000250|UniProtKB:O60667, ECO:0000312|RGD:1359282};
GN Synonyms=Faim3, Toso;
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 [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: May play a role in the immune system processes. Protects
CC cells from FAS-, TNF alpha- and FADD-induced apoptosis without
CC increasing expression of the inhibitors of apoptosis BCL2 and BCLXL.
CC Seems to activate an inhibitory pathway that prevents CASP8 activation
CC following FAS stimulation, rather than blocking apoptotic signals
CC downstream. May inhibit FAS-induced apoptosis by preventing CASP8
CC processing through CFLAR up-regulation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60667}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The Ig-like domain is required for the anti-apoptotic ability.
CC {ECO:0000250}.
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DR EMBL; BC088197; AAH88197.1; -; mRNA.
DR RefSeq; NP_001014843.1; NM_001014843.2.
DR AlphaFoldDB; Q5M871; -.
DR SMR; Q5M871; -.
DR STRING; 10116.ENSRNOP00000036615; -.
DR iPTMnet; Q5M871; -.
DR PhosphoSitePlus; Q5M871; -.
DR PaxDb; Q5M871; -.
DR GeneID; 548326; -.
DR KEGG; rno:548326; -.
DR UCSC; RGD:1359282; rat.
DR CTD; 9214; -.
DR RGD; 1359282; Fcmr.
DR eggNOG; ENOG502S6XH; Eukaryota.
DR HOGENOM; CLU_059565_0_0_1; -.
DR InParanoid; Q5M871; -.
DR OrthoDB; 1378301at2759; -.
DR PhylomeDB; Q5M871; -.
DR TreeFam; TF338713; -.
DR PRO; PR:Q5M871; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q5M871; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0070229; P:negative regulation of lymphocyte apoptotic process; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..426
FT /note="Fas apoptotic inhibitory molecule 3"
FT /id="PRO_0000284423"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 33..104
FT /note="Ig-like"
FT REGION 178..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT DISULFID 37..103
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 48055 MW; B8CE97B14EE46EA1 CRC64;
MNLWLWLLYF LPVSGTLKVL PEVRLEVELG GSVFIECPLP QTHVRMYLCR QMTNPAICAT
VVSNIFVKKE YKRRVTLKPS LNKKLFLVEM TQLTKDDEGI YACGVGTNTD LGKTQKVTLN
VRNEFPEYPE PFWDDEPTSE PSPRWWLHRY PEELPWLKMG EHASPSGFID KVTTLSPKTE
APPVHQPSTN TSVSRHPRVY GASSETPTKP SALLPATTAF KTSARQASRL LEASYSHHTR
LHGERTPHYG SQYGREDRGL HISIPEFHIL IPTFLGFLLL VLLGLVVKRA IQRRRAFSRR
VGRMARRMRG RGPSRQIPTQ RRDAPQRPRS QNNVYSACPR RAREPDNVGS AEALLLNAPA
SAPPALPLVI ETSWPHTPSL KMSCEYVSLG HQPAVNVEDQ DSNDYINIPG LPHLPSKPPG
PRPSRQ
