ID A0A3Q3CYS4_HAPBU Unreviewed; 1660 AA.
AC A0A3Q3CYS4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=SWI/SNF related BAF chromatin remodeling complex subunit ATPase 4a {ECO:0000313|Ensembl:ENSHBUP00000033823.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033823.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000033823.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSHBUP00000033823.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 8153.ENSHBUP00000033823; -.
DR Ensembl; ENSHBUT00000028013.1; ENSHBUP00000033823.1; ENSHBUG00000021172.1.
DR GeneTree; ENSGT00940000156887; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0060973; P:cell migration involved in heart development; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0021634; P:optic nerve formation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18062; DEXHc_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 1.20.5.170:FF:000008; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 1.20.920.10:FF:000004; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 3.40.5.120:FF:000001; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 3.40.50.300:FF:003020; SNF2-related domain-containing protein; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR030100; BRG1_ATP-bd.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 193..228
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 474..546
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 779..944
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1097..1258
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1459..1529
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..45
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..158
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..257
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..603
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..618
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1396
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1569
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1602
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1660 AA; 186327 MW; B24FFB350011BD04 CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGGMMGP SPGPSPGSAH SMMGPSPGPP GSGHPHPPQG
PSGYPQDNMH QMHKPMEAMH EKGVPDDPRY GQMKGMGMRP GGHSGMGPPP SPMDQHSQGY
PSPLGGSEHA PSPVPANGPP SGPMMPGGPS GPGAGPMEGS GDSNQGMGQP NRGGPQGPGG
PPVAAGGAGG PTPFNQNQLH QLRAQIMAYK MLARSQPLPE HLQMAVQGKR PMPGMQQQPM
PNMPPSTGPG GGPGAGPGPA PANYNRQHGM VGPNIAPPGP AGVPPGMQGQ PTNGPPKSWP
EGPMVNAAAP SNPPQKLIPP QPTGRPSPAP PSVPPAASPV MPPQTQSPGQ PAQPPPMMLH
QKQNRITPIQ KPRGLDPVEI LQEREYRLQA RISHRIQELE NLPGSLAGDL RTKATIELKA
LRLLNFQRQL RQEVVVCMRR DTALETALNA KAYKRSKRQS LREARITEKL EKQQKIEQER
KRRQKHQEYL NSILQHAKDF KEYHRSITAK IQKATKAVAT YHANTEREQK KENERIEKER
MRRLMAEDEE GYRKLIDQKK DKRLAYLLQQ TDEYVANLTE LVRAHKAAQA LKEKKKKKKK
KKKPEAPEGA APALGPDGEP LDETSQMSDL PVKVIHVDSG KILTGVEAPK AGQLEAWLEM
NPGYEVAPRS DSEGSGSEEE EEEEEEEDDQ PQTSSAPTEE KKKIPDPDSE DVSEVDVLHI
IEHAKQDVDD EYGSASFNRG LQSYYAVAHA VTEKVDKQSS LLVNGQLKQY QIKGLEWLVS
LYNNNLNGIL ADEMGLGKTI QTIALITYLM EYKRINGPFL IIVPLSTLSN WVYEFDKWAP
SVVKVSYKGS PAARRSFVPI LRSGKFNVLL TTYEYIIKDK QVLAKIRWKY MIVDEGHRMK
NHHCKLTQVL NTHYLAPRRL LLTGTPLQNK LPELWALLNF LLPTIFKSCS TFEQWFNAPF
AMTGEKVDLN EEETILIIRR LHKVLRPFLL RRLKKEVEAQ LPEKVEYVIK CDMSALQRVL
YRHMQAKGVL LTDGSEKDKK GKGGTKTLMN TIMQLRKICN HPFMFQHIEE SFSEHLGYSG
GIITGPDLYR ASGKFELLDR ILPKLRATNH KVLLFCQMTS LMTIMEDYFA YRNFKYLRLD
GTTKAEDRGM LLKTFNDPAS EYFVFLLSTR AGGLGLNLQS ADTVIIFDSD WNPHQDLQAQ
DRAHRIGQQN EVRVLRLCTV NSVEEKILAA AKYKLNVDQK VIQAGMFDQK SSGYERRAFL
QAILEHEEQD EEEDEVPDDE TVNQMIARSE EEFEQFMRMD LDRRREEARN PKRKPRLMEE
DDLPGWILKD DAEVERLTCE EEEEKMFGRG SRQRKEVDYS DSLTEKQWLK AIEEGNLEDI
EEEVRHKKTT RKRKRDRDHD GGPATPSSSS GRGRDKDDDG KKAKKRGRPP AEKLSPNPPS
LTKKMRKIVD AVIKYKDGNG RQLSEVFIQL PSRKELPEYY ELIRKPVDFR KIKERIRSHK
YRSLNDLEKD VMLLCQNAQT FNLEGSLIYE DSIVLQSVFT SVRQKIEKED ESEGEESEEE
EEEVDEGSES ECRSVKVKIK LGRKEKGERG GKGQRRRGRG ARAKPVVSDD DSEEEQEEVR
AEQENEHTHT HTPNLESSAF MLMYLNDRFS RHNDRALSSL
//
