ID A0A2I2YZ59_GORGO Unreviewed; 1190 AA.
AC A0A2I2YZ59;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Large proline-rich protein BAG6 {ECO:0000256|ARBA:ARBA00021614};
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000256|ARBA:ARBA00030033};
DE AltName: Full=HLA-B-associated transcript 3 {ECO:0000256|ARBA:ARBA00029739};
GN Name=BAG6 {ECO:0000313|Ensembl:ENSGGOP00000040281.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000040281.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000040281.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000040281.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000040281.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Released extracellularly via exosomes, it is a ligand of the
CC natural killer/NK cells receptor NCR3 and stimulates NK cells
CC cytotoxicity. It may thereby trigger NK cells cytotoxicity against
CC neighboring tumor cells and immature myeloid dendritic cells (DC).
CC {ECO:0000256|ARBA:ARBA00002067}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
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DR EMBL; CABD030044187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2YZ59; -.
DR STRING; 9593.ENSGGOP00000040281; -.
DR Ensembl; ENSGGOT00000061833.1; ENSGGOP00000040281.1; ENSGGOG00000005529.3.
DR GeneTree; ENSGT00390000016199; -.
DR InParanoid; A0A2I2YZ59; -.
DR OMA; NRITVAM; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000005529; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0071818; C:BAT3 complex; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; IEA:Ensembl.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:Ensembl.
DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0036506; P:maintenance of unfolded protein; IEA:Ensembl.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007130; P:synaptonemal complex assembly; IEA:Ensembl.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd01809; Ubl_BAG6; 1.
DR InterPro; IPR021925; BAG6.
DR InterPro; IPR048926; Bag6_BAGS.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR PANTHER; PTHR15204; LARGE PROLINE-RICH PROTEIN BAG6; 1.
DR PANTHER; PTHR15204:SF0; LARGE PROLINE-RICH PROTEIN BAG6; 1.
DR Pfam; PF12057; BAG6; 1.
DR Pfam; PF20960; Bag6_BAGS; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 45..105
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 115..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 125403 MW; C5DD25556A5BC3C6 CRC64;
MLGSLPGTLW SGQQRAFLPS FFFRDLSAME PNDSTSTVVE EPDSLEVLVK TLDSQTRTFI
VGAQMNVKEF KEHIAASVSI PSEKQRLIYQ GRVLQDDKKL QEYNVGGKVI HLVERAPPQT
HLPSGASSGT GSASATHGGG PPPGTRGPGA SVHDRNANSY VMVGTFNLPS DGSAVDVHIN
MEQAPIQSEP RVRLVMAQHM IRDIQTLLSR MECRGGPQPQ HSQPPPQPPA VTPEPVALSS
QTSEPVESEA PPREPMEAEE VEERAPAQNP ELTPGPASAG PTPAPETNAP NHPSPAEYVE
VLQELQRLES RLQPFLQRYY EVLGAAATTD YNNNHEGREE DQRLINLVGE SLRLLGNTFV
ALSDLRCNLA CTPPRHLHVV RPMSHYTTPM VLQQAAIPIQ INVGTTVTMT GNGTRPPPTP
NAEASPPGPG QASSVAPSST NVESSAEGAP PPGPAPPPAT SHPRVIRISH QSVEPVVMMH
MNIQDSGTQP GGVPSAPTGP LGPSGHGQTL GSTLIQLPSL PPEFMHAVAH QITHQAMVAA
VASAAAGQQV PGFPTAPTRV VIARPTPPQA RPSHPGGPPV SGTLQGAGLG TNASLAQMVS
GLVGQLLMQP VLVAQGTPGM APPPAPATAS ASAGTTNTAT TAGPAPGGPA QPPPAPQPST
ADLQFSQLLG NLLGPAGPGA GGPGVASPTI TVAMPGVPAF LQGMTDFLQA TQTAPPPPPP
PPPPPPAPEQ QTMPPPGSPS GGAGSPGGLG LESLSPEFFT SVVQGVLSSL LGSLGARAGS
SESIAAFIQR LSGSSNIFEP GADGALGFFG ALLSLLCQNF SMVDVVMLLH GHFQPLQRLQ
PQLRSFFHQH YLGGQEPTPS NIRMATHTLI TGLEEYVRES FSLVQVQPGV DIIRTNLEFL
QEQFNSIAAH VLHCTDSGFG ARLLELCNQG LFECLALNLH CLGGQQMELA AVINGRIRRM
SRGVNPSLVS WLTTMMGLRL QVVLEHMPVG PDAILRYVRR VGDPPQPLPE EPMEVQGAER
ASPEPQRENA SPAPGTTAEE AMSRGPPPAP EGGSRDEQDG ASAETEPWAA AVPPEWVPII
QQDIQSQRKV KPQPPLSDAY LSGMPAKRRK TMQGEGPQLL LSEAVSRAAK AAGARPLTSS
ESLSRDLEAP EVQESYRQQL RSDIQKRLQE DPNYSPQRFP NAQRAFADDP
//
