ID A0A3Q1HVN6_ANATE Unreviewed; 1225 AA.
AC A0A3Q1HVN6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=BCL2-associated athanogene 6 {ECO:0000256|ARBA:ARBA00030033};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000009103.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000009103.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
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DR AlphaFoldDB; A0A3Q1HVN6; -.
DR STRING; 64144.ENSATEP00000009103; -.
DR Ensembl; ENSATET00000009262.2; ENSATEP00000009103.1; ENSATEG00000006414.2.
DR GeneTree; ENSGT00390000016199; -.
DR InParanoid; A0A3Q1HVN6; -.
DR OMA; RCTDDTF; -.
DR Proteomes; UP000265040; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 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; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 8..68
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 202..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 129698 MW; 1DBB9F0C4097E1C3 CRC64;
MEEQTADIEV TVKTLDSQSR TYTVDAQLTV KQFKEHIAPS VSIPVDKQRL IYQGRVLQDE
RTLADYNVGG KVIHLVERAP PPPSQPGSGS GGTSADSGPS SSAQGTSQVP PHDRNANSYV
MLGTVNLPVN IMDPQQIQMS VQQMVSGMGE NARNARITTS TGSNGSVNVH IDMDQPVQSE
PRLRLVLAEN LLRDINDVIH RMEGRPSDSS SQTETTSAAA PPPPSSSSTT STPSPSAQPM
DTSPPPTTPP PAPTSSAQSE GPTPHPGPNH PSPAELAEML TELRRVEERL QPFIQRAHTI
LETATTAEYN NNTEREEDQR TLVLTWECLR LLGNALVALS DLRLNLMSPV PRHLHVVRPF
SHYATPVTLP GAVHHHIPVQ MNLGATVTVA ANSTEGQAPP TQSASQSEQT GQGQTSPPQT
SPSNQQAGQG QAGPRVIRIS HQAVPVVMMQ MNTDGPGANP AAAGQQMPGQ PGSLPPDFMR
NLMQQISQYA AAVATSAATA AATGQPAPPQ PTPPGYSSTA NSSTTTTGPN TPTTTPTAPP
PPPQTGTQPQ ARVVFTRPPF APNMPPPAFG TRGTTINVRA AMPGQQPGQA FNPAALNQMI
SGLVGQLLLP GQMAGQTVTS SSSTSSSSSS SSFSSSSSSS HTTSSSSSFS FSTSSPTPPP
TANTTSPPSQ PDTNTSEPQA QEMPPDLSQL LGSLLGVAGV AGAGPGGAPS VTVTTSGVPA
FIQGVSEFMQ QAQPIFSPPQ PPSGTTPAPS SAPNPTPNAP AAAEALNPEL FTGIVRGVLS
TMMGSLGQAQ NDTESIAQFM QRLSQATNIF ISPEDPTGFF GELLMLVCQT FTMSDLVMLL
HGQHQPLSRI QPQLSQFFTQ NYLNGREPTD QNIADAADSL VNELEEYISE SFRESSVTVL
EGVDITQTNM SFFRQQLTHI ATHILRCTDE SFGPRLLQMC NQALFECLAL NLHCLRGDQR
ALTAVINHRI RRMSSDISPS LVNWMTSMMT MRLQVILEHI PVTQEQIQNY IIHTQRDQSS
ATGTQEPERA QSAAIGDTLS PAAATTAEEA MSVSHDTRAP SRDTRVLPGD LGATGGAVPI
GGDRAAAGAE GGSEESAGES EAWAAAVPPE WVPIIRCDMI TQKKMKAQPP LSDAYLHGMP
AKRRKTGPGS GSLLSLSDAV SQAARTAGVK PITSAERLQD DLESQELKEA YAEQVKSDLK
KRVREDPDFN SQQFPNSNRA FSSDS
//
