FAIM3_MOUSE
ID FAIM3_MOUSE Reviewed; 422 AA.
AC A1KXC4; A1KXC6; A1KXC8; A1KXC9; Q148B9; Q9D8T1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 82.
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|MGI:MGI:1916419};
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|MGI:MGI:1916419};
GN Synonyms=Faim3, Toso;
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].
RC STRAIN=129/Sv, BALB/cJ, C3H/HeJ, C57BL/6J, NOD, NZB, NZM2328, NZW/LacJ, and
RC SJL/J; TISSUE=Spleen;
RA Song Y., Jacob C.O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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; AY227385; AAP51723.1; -; mRNA.
DR EMBL; AY227386; AAP51724.1; -; mRNA.
DR EMBL; AY227387; AAP51725.1; -; mRNA.
DR EMBL; AY227388; AAP51726.1; -; mRNA.
DR EMBL; AY227389; AAP51727.1; -; mRNA.
DR EMBL; AY227390; AAP51728.1; -; mRNA.
DR EMBL; AY227391; AAP51729.1; -; mRNA.
DR EMBL; AY227392; AAP51730.1; -; mRNA.
DR EMBL; AY227393; AAP51731.1; -; mRNA.
DR EMBL; AK007714; BAB25207.1; -; mRNA.
DR EMBL; AK155943; BAE33514.1; -; mRNA.
DR EMBL; BC118505; AAI18506.1; -; mRNA.
DR EMBL; BC116674; AAI16675.1; -; mRNA.
DR RefSeq; NP_081252.1; NM_026976.2.
DR AlphaFoldDB; A1KXC4; -.
DR SMR; A1KXC4; -.
DR STRING; 10090.ENSMUSP00000048303; -.
DR iPTMnet; A1KXC4; -.
DR PhosphoSitePlus; A1KXC4; -.
DR PaxDb; A1KXC4; -.
DR PRIDE; A1KXC4; -.
DR ProteomicsDB; 271722; -.
DR DNASU; 69169; -.
DR GeneID; 69169; -.
DR KEGG; mmu:69169; -.
DR UCSC; uc007cmn.1; mouse.
DR CTD; 9214; -.
DR MGI; MGI:1916419; Fcmr.
DR eggNOG; ENOG502S6XH; Eukaryota.
DR InParanoid; A1KXC4; -.
DR OrthoDB; 1378301at2759; -.
DR PhylomeDB; A1KXC4; -.
DR TreeFam; TF338713; -.
DR BioGRID-ORCS; 69169; 4 hits in 71 CRISPR screens.
DR PRO; PR:A1KXC4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A1KXC4; protein.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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; IDA:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0070229; P:negative regulation of lymphocyte apoptotic process; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 2: Evidence at transcript 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..422
FT /note="Fas apoptotic inhibitory molecule 3"
FT /id="PRO_0000284422"
FT TOPO_DOM 18..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..104
FT /note="Ig-like"
FT REGION 290..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5M871"
FT DISULFID 37..103
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="A -> T (in Ref. 1; AAP51725/AAP51727/AAP51728/
FT AAP51729 and 2; BAE33514/BAB25207)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="P -> L (in Ref. 1; AAP51728)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="K -> R (in Ref. 1; AAP51728)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="S -> P (in Ref. 1; AAP51723/AAP51724/AAP51725/
FT AAP51726/AAP51730/AAP51731 and 3; AAI16675/AAI18506)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="P -> Q (in Ref. 2; BAE33514/BAB25207 and 3;
FT AAI16675/AAI18506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47471 MW; 24270D3B50AD871E CRC64;
MDFWLWLLYF LPVSGALRVL PEVQLNVEWG GSIIIECPLP QLHVRMYLCR QMAKPGICST
VVSNTFVKKE YERRVTLTPC LDKKLFLVEM TQLTENDDGI YACGVGMKTD KGKTQKITLN
VHNEYPEPFW EDEWTSERPR WLHRFLQHQM PWLHGSEHPS SSGVIAKVTT PAPKTEAPPV
HQPSSITSVT QHPRVYRAFS VSATKSPALL PATTASKTST QQAIRPLEAS YSHHTRLHEQ
RTRHHGPHYG REDRGLHIPI PEFHILIPTF LGFLLLVLLG LVVKRAIQRR RASSRRAGRL
AMRRRGRGAS RPFPTQRRDA SQRPRSQNNV YSACPRRARG PDSLGPAEAP LLNAPASASP
ASPQVLEAPW PHTPSLKMSC EYVSLGYQPA VNLEDPDSDD YINIPDPSHL PSYAPGPRSS
CP
