ID A0A1S3GDA5_DIPOR Unreviewed; 1725 AA.
AC A0A1S3GDA5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protein polybromo-1 isoform X1 {ECO:0000313|RefSeq:XP_012886214.1};
GN Name=Pbrm1 {ECO:0000313|RefSeq:XP_012886214.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012886214.1};
RN [1] {ECO:0000313|RefSeq:XP_012886214.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012886214.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_012886214.1; XM_013030760.1.
DR STRING; 10020.ENSDORP00000017356; -.
DR GeneID; 105996597; -.
DR KEGG; dord:105996597; -.
DR CTD; 55193; -.
DR InParanoid; A0A1S3GDA5; -.
DR OrthoDB; 2878065at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd04717; BAH_polybromo; 2.
DR CDD; cd05524; Bromo_polybromo_I; 1.
DR CDD; cd05517; Bromo_polybromo_II; 1.
DR CDD; cd05520; Bromo_polybromo_III; 1.
DR CDD; cd05518; Bromo_polybromo_IV; 1.
DR CDD; cd05515; Bromo_polybromo_V; 1.
DR CDD; cd05526; Bromo_polybromo_VI; 1.
DR CDD; cd21984; HMG-box_PB1; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037968; PBRM1_BD5.
DR InterPro; IPR037382; Rsc/polybromo.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 5.
DR PROSITE; PS50014; BROMODOMAIN_2; 6.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 85..155
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 221..291
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 421..491
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 574..644
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 712..782
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 853..898
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 992..1110
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1192..1308
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1415..1483
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1415..1483
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 22..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1725 AA; 197106 MW; D23110C6199E1136 CRC64;
MRRLAFRGAG CALVKLKKLD SMGSKRRRAT SPSSSVSGDF DDGHHSIPTP GPSRKRRRLS
NLPTVDPIAV CHELYNTIRD YKDEQGRLLC ELFIRAPKRR NQPDYYEVVS QPIDLMKIQQ
KLKMEEYDDV NLLTADFQLL FNNAKAYYKP DSPEYKAACK LWDLYLRTRN EFVQKGEADD
EDDDDDGQDN RGTVTEGSSP SYLKEILEQL LEAIVVATNP SGRLISELFQ KLPSKVQYPD
YYAIIKEPID LKTIAQRIQN GSYKSIHAMA KDIDLLAKNA KTYNEPGSQV FKDANSIKKI
FYMKKAEIEH HEMAKSSLRI RTASNLAAAR LTGPSHSKGS LGEERNPTSK YYRNKRAVQG
GRLSAITMAL QYGSESEEDA ALAAARYEEG ESEAESITSF MDVSNPFYQL YDTVRNCRNN
QGQLIAEPFF HLPSKKKYPD YYQQIKMPIS LQQIRTKLKN QEYETLDHLE CDLNLMFENA
KRYNVPNSAI YKRVLKLQQV MQAKKKELAR RDDIEDGDSM ISSATSDTGS AKRKRNTHDS
EMLGLRRLSS KKNIRKQRMK ILFNVVLEAR EPGSGRRLCD LFMVKPSKKD YPDYYKIILE
PMDLKIIEHN IRNDKYSGEE GMIEDMKLMF RNARHYNEEG SQVYNDAHIL EKLLKDKRKE
LGPLPDDDDM ASPKLKLSRK SGVSPKKSKY MTPMQQKLNE VYEAVKNYTD KRGRRLSAIF
LRLPSRSELP DYYLTIKKPM DMEKIRSHMM ANKYQDIDSM VEDFVMMFNN ACTYNEPESL
IYKDALVLHK VLLETRRDLE GDEDSHVPNV TLLIQELIHN LFVSVMSHQD DEGRCYSDSL
AEIPAVDPNF PNKPPLTFDI IRKNVENNRY RRLDLFQEHM FEVLERARRM NRTDSEIYED
AVELQQFFIK IRDELCKNGE ILLSPALSYT TKHLHNDVEK EKKEKLPKEI EEDKLKREEE
KREAEKSEDS SGATGLSGLH RTYSQDCSFK NSMYHVGDYV YVEPAEANLQ PHIVCIERLW
EDSAGEKWLY GCWFYRPNET FHLATRKFLE KEVFKSDYYN KVPVSKILGK CVVMFVKEYF
KLCPENFRDE DVFVCESRYS AKTKSFKKIK LWTMPISSVR FVPRDVPLPV VRVASVFANA
DKGDDEKNTD ISEDSRVEDN FNLEKEKEDV PVEMSNGEPG CHYFEQLHYN DMWLKVGDCV
FIKSHGLVRP RVGRIEKVWV RDGAAYFYGP IFIHPEETEH EPTKMFYKKE VFLSNLEETC
PMTCILGKCA VLSFKDFLSC RPTEIPENDI LLCESRYNES DKQMKKFKGL KRFSLSAKVV
DDEIYYFRKP IVPQKEPSPL LEKKIQLLEA KFAELEGGDD DIEEMGEEDN EVIEPPSLPQ
LQTPLASELD LMPYTPPQST PKSAKGSAKK EGSKRKINMS GYILFSSEMR AVIKAQHPDY
SFGELSRLVG TEWRNLETAK KAEYEERAAK VAEQQERERA AQQQQPSASP RAGTPVGALM
GVVPPPTPMG MLNQQLTPVA GMMGGYPPGL PPLQGPVDGL VSMGSMQPLH PGGPPPHHLP
PGVPGLPGIP PPGVMNQGVA PMVGTPAPGG SPYGQQVGVL GPPGQQAPPP YPSPHPAGPP
VIQQPTTPIF VAPPPKTQRL LHSEAYLKYI EGLSAESNSI SKWDQTLAAR RRDIHLSKEQ
ESRLPSHWLK SKGAHTTMAD ALWRLRDLML RDTLNIRQAY NLENV
//