GenomeNet

Database: UniProt
Entry: J9NWV6_CANLF
LinkDB: J9NWV6_CANLF
Original site: J9NWV6_CANLF 
ID   J9NWV6_CANLF            Unreviewed;       196 AA.
AC   J9NWV6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   05-JUN-2019, entry version 40.
DE   RecName: Full=Bcl-2-like protein 11 {ECO:0000256|PIRNR:PIRNR037827};
DE            Short=Bcl2-L-11 {ECO:0000256|PIRNR:PIRNR037827};
DE   AltName: Full=Bcl2-interacting mediator of cell death {ECO:0000256|PIRNR:PIRNR037827};
GN   Name=BCL2L11 {ECO:0000313|Ensembl:ENSCAFP00000037767,
GN   ECO:0000313|VGNC:VGNC:54922};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000037767, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000037767, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000037767,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000037767}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000037767};
RG   Ensembl;
RL   Submitted (SEP-2012) to UniProtKB.
CC   -!- FUNCTION: Induces apoptosis and anoikis.
CC       {ECO:0000256|PIRNR:PIRNR037827}.
CC   -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
CC       proteins including MCL1, BCL2, BCL2L1 isoform Bcl-X(L),
CC       BCL2A1/BFL-1. {ECO:0000256|PIRNR:PIRNR037827}.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC       {ECO:0000256|PIRNR:PIRNR037827}.
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DR   EMBL; AAEX03010902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03010903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005630482.1; XM_005630425.2.
DR   RefSeq; XP_005630483.1; XM_005630426.1.
DR   RefSeq; XP_005630485.1; XM_005630428.2.
DR   STRING; 9612.ENSCAFP00000037767; -.
DR   PaxDb; J9NWV6; -.
DR   Ensembl; ENSCAFT00000045409; ENSCAFP00000037767; ENSCAFG00000030412.
DR   GeneID; 612867; -.
DR   KEGG; cfa:612867; -.
DR   CTD; 10018; -.
DR   VGNC; VGNC:54922; BCL2L11.
DR   eggNOG; ENOG410IZKS; Eukaryota.
DR   eggNOG; ENOG410Y8GB; LUCA.
DR   GeneTree; ENSGT00390000003178; -.
DR   InParanoid; J9NWV6; -.
DR   KO; K16341; -.
DR   OMA; IRLVWRM; -.
DR   OrthoDB; 1460067at2759; -.
DR   TreeFam; TF335898; -.
DR   Reactome; R-CFA-111446; Activation of BIM and translocation to mitochondria.
DR   Reactome; R-CFA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR   Reactome; R-CFA-193648; NRAGE signals death through JNK.
DR   Proteomes; UP000002254; Chromosome 17.
DR   Bgee; ENSCAFG00000030412; Expressed in 3 organ(s), highest expression level in liver.
DR   GO; GO:0097136; C:Bcl-2 family protein complex; IEA:Ensembl.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0001783; P:B cell apoptotic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:UniProtKB-UniRule.
DR   GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
DR   GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
DR   GO; GO:0043583; P:ear development; IEA:Ensembl.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0060139; P:positive regulation of apoptotic process by virus; IEA:Ensembl.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
DR   GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0032464; P:positive regulation of protein homooligomerization; IEA:Ensembl.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
DR   GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
DR   GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR   InterPro; IPR014771; Apoptosis_Bim_N.
DR   InterPro; IPR017288; Bcl-2-like_11.
DR   InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
DR   Pfam; PF08945; Bclx_interact; 1.
DR   Pfam; PF06773; Bim_N; 1.
DR   PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|PIRNR:PIRNR037827};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037827};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR037827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254}.
FT   DOMAIN        4     39       Bim_N. {ECO:0000259|Pfam:PF06773}.
FT   DOMAIN      128    164       Bclx_interact. {ECO:0000259|Pfam:
FT                                PF08945}.
FT   REGION        1     68       Disordered. {ECO:0000256|MobiDB-lite:
FT                                J9NWV6}.
SQ   SEQUENCE   196 AA;  21892 MW;  8BCEE2748A9ADF69 CRC64;
     MAKQPSDVSS ECDREGGQLQ PAERPPQLRP GAPTSLQTEQ QGNPEGEGDR CPQGSPQGPL
     APPASPGPFA TRSPLFIFVR RSSLLSRSSS GYFSFDTDRS PAPMSCDKST QTPSPPCQAF
     NHYLSAMASM RQSQAVPADM RPEIWIAQEL RRIGDEFNAY YPRRVFLNNY QAAEAHPQMI
     ILRLLRYIVR LVWRLQ
//
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