ID A0A1U8CS58_MESAU Unreviewed; 1133 AA.
AC A0A1U8CS58;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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|RefSeq:XP_012981295.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012981295.1};
RN [1] {ECO:0000313|RefSeq:XP_012981295.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_012981295.1; XM_013125841.2.
DR AlphaFoldDB; A0A1U8CS58; -.
DR OrthoDB; 3177594at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01809; Ubl_BAG6; 1.
DR InterPro; IPR021925; BAG6.
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; PF00240; ubiquitin; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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:UP000189706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 17..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 88..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 118254 MW; A9F0DB487CDD6DA6 CRC64;
MEPSDSASAA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI
YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTQLPSGASS GTGSASAPHG GAPLPGTRGP
GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPVQS EPRVRLVMAQ HMIRDIQTLL
SRMECRGPQA QASQPPPQTP TVASETVTLS SQTSEPVESE APPREPMESE EMGERTPAQT
PELAAAGPAP AGPTPAPDTN TPNHPSPAEH VEVLQELQRL QRRLQPFLQR YCEVLGAAAT
TDYNNNHEGR EEDQRLINLV GESLRLLGNT FVALSDLRCN LACAPPRHLH VVRPMSHYTT
PMVLQQAAIP IQINVGTTVT MTGNGARPPP APGSEAASPG SGQASSLPPS STAVDSSTEG
APPPAASHPR VIRISHQSVE PVVMMHMNIQ DPGSQPGGVP SAPTGPLGPP GHGQTLGSTL
IQLPSLPPEF MHAVAHQITH QAMVAAVASA AAGQQVPGFP TAPTRVVIAR PTPPQARPSH
PGGPPVSGTL GTGLGTNPSL AQMVSGLVGQ LLMQPVLVAQ GTPGMAPAPA AAPAPAPAPA
PAAAPAPAPA PAPAPAPAPA TASASAGTTN TATTAGPAPG GPAQPPPPQP SAADLQFSQL
LGNLLGPAGP GAAGPAMASP TITVAMPGVP AFLQGMTEFL QASQTAPPPP PPPPPPPPAP
EQQATPPPGS PSGGTGSTGG LGPESLPPEF FTSVVQGVLS SLLGSLGARA GSSESIAAFI
QRLSGSSNIF EPGADGALGF FGALLSLLCQ NFSMVDVVML LHGHFQPLQR LQPQLRSFFH
QHYLGGQEPT PGNIRMATHT LITGLEEYVR ESFSLVQVQP GVDIIRTNLE FLQEQFNSIA
AHVLHCTDSG FGARLLELCN QGLFECLALN LHCLGGQQME LAAVINGRIR RMSRGVNPSL
VSWLTTMMGL RLQVVLEHMP VGPDAILRYV RRVGDPPQAL PEEPMEVQGA ERTSPEPQRE
NASPAPGTTA EEAMSRGPPP APEGGSRDEQ DGASADAEPW AAAVPPEWVP IIQQDIQSQR
KVKPQPPLSD AYLSGMPAKR RKLRSDIQKR LQEDPNYSPQ RFPNAHRAFA DDP
//
