BFAR_MOUSE
ID BFAR_MOUSE Reviewed; 450 AA.
AC Q8R079; Q8C1A7; Q9CXY3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bifunctional apoptosis regulator;
GN Name=Bfar;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 STRUCTURE BY NMR OF 170-247.
RG RIKEN structural genomics initiative (RSGI);
RT "Sterile alpha motif (SAM) domain of mouse bifunctional apoptosis
RT regulator.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Apoptosis regulator. Has anti-apoptotic activity, both for
CC apoptosis triggered via death-receptors and via mitochondrial factors
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CASP8, BCL2 and BCL2L1 through SAM domain and
CC also with HIP1, IFT57, ESRRBL1 and BCAP31. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R079-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R079-2; Sequence=VSP_016651;
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DR EMBL; AK013874; BAB29029.1; -; mRNA.
DR EMBL; AK028592; BAC26022.1; -; mRNA.
DR EMBL; BC027221; AAH27221.1; -; mRNA.
DR CCDS; CCDS27966.1; -. [Q8R079-1]
DR CCDS; CCDS49769.1; -. [Q8R079-2]
DR RefSeq; NP_001171023.1; NM_001177552.1. [Q8R079-2]
DR RefSeq; NP_080252.1; NM_025976.5.
DR PDB; 1V85; NMR; -; A=170-247.
DR PDBsum; 1V85; -.
DR AlphaFoldDB; Q8R079; -.
DR SMR; Q8R079; -.
DR BioGRID; 211952; 22.
DR STRING; 10090.ENSMUSP00000023365; -.
DR GlyGen; Q8R079; 2 sites.
DR iPTMnet; Q8R079; -.
DR PhosphoSitePlus; Q8R079; -.
DR EPD; Q8R079; -.
DR MaxQB; Q8R079; -.
DR PaxDb; Q8R079; -.
DR PRIDE; Q8R079; -.
DR ProteomicsDB; 273606; -. [Q8R079-1]
DR ProteomicsDB; 273607; -. [Q8R079-2]
DR Antibodypedia; 24873; 220 antibodies from 28 providers.
DR DNASU; 67118; -.
DR Ensembl; ENSMUST00000069281; ENSMUSP00000063371; ENSMUSG00000022684. [Q8R079-2]
DR GeneID; 67118; -.
DR KEGG; mmu:67118; -.
DR UCSC; uc007ygf.2; mouse. [Q8R079-1]
DR UCSC; uc007ygg.2; mouse. [Q8R079-2]
DR CTD; 51283; -.
DR MGI; MGI:1914368; Bfar.
DR VEuPathDB; HostDB:ENSMUSG00000022684; -.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00390000005386; -.
DR HOGENOM; CLU_057444_0_0_1; -.
DR InParanoid; Q8R079; -.
DR OrthoDB; 1332799at2759; -.
DR PhylomeDB; Q8R079; -.
DR TreeFam; TF332303; -.
DR BioGRID-ORCS; 67118; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Bfar; mouse.
DR EvolutionaryTrace; Q8R079; -.
DR PRO; PR:Q8R079; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8R079; protein.
DR Bgee; ENSMUSG00000022684; Expressed in myocardium of ventricle and 254 other tissues.
DR ExpressionAtlas; Q8R079; baseline and differential.
DR Genevisible; Q8R079; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0089720; F:caspase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Bifunctional apoptosis regulator"
FT /id="PRO_0000055823"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..249
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 34..74
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 89..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016651"
FT CONFLICT 184
FT /note="M -> T (in Ref. 1; BAB29029)"
FT /evidence="ECO:0000305"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:1V85"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1V85"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:1V85"
SQ SEQUENCE 450 AA; 52968 MW; 07B1122FAA9EF2BC CRC64;
MEEPQKNDLS MREQEEEHPV RSSGPQISVS EFSCHCCYDT LVNPTTLNCG HSFCRHCLAL
WWMSSKKTEC PECREKWEGF PKVNILLRDA IEKLFPDAIR MRVEDIQQNN DVVQSLAAFQ
KYGNDQNPLA PSTGRVNPQR GGGFFSGVLT ALTGVAVILL VYHWRSRESE HGLLVHKAVD
KWTMEEVVLW LEQLGPWASL YRDRFLSERV NGRLLLTLTE EEFSRAPYTI ENSSHRRVIL
TELERVRALG VKPPQNLWEY KAVNPGRSLF LLYALKSSPR LGLLYLYLFD YTDCFLPFIH
TICPLQENSS GEDIFTKLLD LREPTWKQWR EFLVKYSFLP YQLIAEFAWD WLEVHYWTSR
FLIVNAVLLS VLELFSFWRI WSRSELKTVP QRMWSHFWKV STQGLFMAMF WPLIPQFVCN
CLFYWALYFN PIINIDLVVK EVRRLETQVL
