ID G1KM96_ANOCA Unreviewed; 1193 AA.
AC G1KM96;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSACAP00000012170.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012170.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000012170.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012170.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000012170.3}
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 RefSeq; XP_008103892.1; XM_008105685.2.
DR RefSeq; XP_016847297.1; XM_016991808.1.
DR AlphaFoldDB; G1KM96; -.
DR STRING; 28377.ENSACAP00000012170; -.
DR Ensembl; ENSACAT00000012418.4; ENSACAP00000012170.3; ENSACAG00000012381.4.
DR GeneID; 100555197; -.
DR KEGG; acs:100555197; -.
DR CTD; 7917; -.
DR eggNOG; KOG4248; Eukaryota.
DR GeneTree; ENSGT00390000016199; -.
DR HOGENOM; CLU_012159_0_0_1; -.
DR InParanoid; G1KM96; -.
DR OrthoDB; 3177594at2759; -.
DR TreeFam; TF328437; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000012381; Expressed in kidney and 13 other cell types or tissues.
DR GO; GO:0071818; C:BAT3 complex; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 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; 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:UP000001646};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 7..67
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 76..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 126164 MW; FE0A75D854C2BF43 CRC64;
MADPENLEVM VKTLDSQTRT FTVEEEITVK EFKEHIASSV NIPAEKQRLI YQGRVLQDDK
KLKEYNVGGK VIHLVERAPP QTQSPSSGGP SGVGSSSVPH NGAGPRGTGP TVHDRNANSY
VMVGTFNLPV SIMDPQPPTQ SDGSSVDVHI NMDQAPIQSE PRIRLVMAQH MLRDVQGILN
RLEGRTNGQA PSGSEEMPSA SPTEREPMEG AESEPSSEPT AAEETPPSGT EPPPAPDAAT
PNHPSPSEYV EVLGELRGVE NRLQPFLQRY EEILGTAGSA DYNNNTEGRE EDQRIINLVG
ESLRLLGNTF VTLSDLRCNL SCNAPRHLHV VRPMSHYTAP MVLQQAAIPI QINVGTTVTM
TGNGSRGAQT SSEGSTASQT SPPAQPGTST PPDAGRPTEG SPPAASSPGA APTQTQGSQT
GHPRVIRISH QTVEPVVMMH MNIQDSSSPM GGSGTGGAPP AGTPGPIGHT PGMGGAPHMP
LPSLPPEFMQ AVAHQITQQA MAAAASAAAG QQVPSFQSAP TRVMIARPSA PSVRPTHPGS
PQAPGQGPPS LGGNASLAQM ISGLVGQLLM QPVIVAQGSG TTASAPSSVN TQATFSTSNS
ASPPTASASA GTTNTATTAA GGSSAGAPGG PIPSSQPPTA GAELQLSQLS QLLGNFFGAT
GSTMAGMAGV GSPTITVAMP GVPAFLQGMT DFLQATQMGA APPHPPEQSP PPPPPQPEAT
PPPPPPPSAP QSGTEAPSGS VGGSGVRGGA SSADAPPPEF FTSVVQGVLS SMMGSLSAQQ
CSTESIADFI QRLSGTSNIF EPGTEGALGF FGDLLSLICQ NFSMVDMVML LHGQFQPLKR
IQPQLNRFFR EEYLHGQEPT DRNIQMATYN LINGLEDYIR ESFASVRVRD GVDITRTNLE
FLQEQFNRIA THILRCTDNT FGYRLLELCN QGLFECLALN LYCLRGEQGA LTAVINDRIR
RMSADMNPSL VSWLTTMMSM RLQVILEHMP VTEEQVLQYV RRVGDPPQPA PEEPMDLQTV
EQAPETLQRD SVASPAPATT AEEAMPQQRG EPEHEEPQQA EPPAPEAEPW AAAVPPEWVP
IIREDIQTQR KLKQQPPLSD AYLSGMPAKR RKTMQGDGPQ LLLSEAVNKA AKAAGVKPLT
STESLSRDLA EPALQEGYRQ QLKSDLQKRL QADPSFTPQR FPNAQQVFVA EDP
//
