BFAR_RAT
ID BFAR_RAT Reviewed; 450 AA.
AC Q5PQN2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Bifunctional apoptosis regulator;
GN Name=Bfar;
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=Heart;
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: 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}.
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DR EMBL; BC087103; AAH87103.1; -; mRNA.
DR RefSeq; NP_001013143.1; NM_001013125.2.
DR AlphaFoldDB; Q5PQN2; -.
DR SMR; Q5PQN2; -.
DR STRING; 10116.ENSRNOP00000004217; -.
DR GlyGen; Q5PQN2; 1 site.
DR PaxDb; Q5PQN2; -.
DR Ensembl; ENSRNOT00000004217; ENSRNOP00000004217; ENSRNOG00000003151.
DR GeneID; 304709; -.
DR KEGG; rno:304709; -.
DR UCSC; RGD:1304791; rat.
DR CTD; 51283; -.
DR RGD; 1304791; Bfar.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00390000005386; -.
DR HOGENOM; CLU_057444_0_0_1; -.
DR InParanoid; Q5PQN2; -.
DR OMA; FWRLWSR; -.
DR OrthoDB; 1332799at2759; -.
DR PhylomeDB; Q5PQN2; -.
DR PRO; PR:Q5PQN2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003151; Expressed in heart and 20 other tissues.
DR Genevisible; Q5PQN2; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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:RGD.
DR GO; GO:0089720; F:caspase binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:RGD.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
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 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Bifunctional apoptosis regulator"
FT /id="PRO_0000055824"
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
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"
SQ SEQUENCE 450 AA; 53024 MW; F089F94F8DE354DD CRC64;
MEEPQKNDLS MRGQEEDHPV RSSGPQISVS EFSCHCCYDT LVNPTTLNCG HSFCRHCLAL
WWMSSKKTEC PECREKWEGF PKVNILLRDA IEKLFPDAIK MRVEDIQQNN DVVQSLAAFQ
KYGNDQNPLA PSTGRVNQQR GGGFFSGVLT ALTGVAVILL VYHWRSRESE HGLLVHKAVD
KWTTEEVVLW LEQLGPWASL YRDRFLSERV NGRLLLTLTE EEFSRAPYTI ENSSHRRVIL
MELERVRALG VKPPQNLWEY KAVNPGRSLF LLYALKSSPR LGLLYLYLFD YTDSFLPFIH
TICPLQEDSF GEDIFTKLLD LREPTWKQWR EFLIKYSFLP YQLIAEFAWD WLEVHYWTSR
FLIVNAMLLS VLELFSFWRI WSRSELKTVP QRMWSHFWKV STQGLFMAMF WPLIPQFVCN
CLFYWALYFN PIINIDLVVK EIRRLETQVF
