ID A0A2B4RMQ5_STYPI Unreviewed; 3201 AA.
AC A0A2B4RMQ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Transcription activator BRG1 {ECO:0000313|EMBL:PFX18089.1};
GN Name=SMARCA4 {ECO:0000313|EMBL:PFX18089.1};
GN ORFNames=AWC38_SpisGene17562 {ECO:0000313|EMBL:PFX18089.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX18089.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX18089.1}.
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DR EMBL; LSMT01000431; PFX18089.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4RMQ5; -.
DR EnsemblMetazoa; XM_022946766.1; XP_022802501.1; LOC111340007.
DR EnsemblMetazoa; XM_022946769.1; XP_022802504.1; LOC111340010.
DR EnsemblMetazoa; XM_022946772.1; XP_022802507.1; LOC111340011.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd00112; LDLa; 12.
DR CDD; cd18793; SF2_C_SNF; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 14.
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 Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF67; PROLOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1-LIKE PROTEIN; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00057; Ldl_recept_a; 14.
DR Pfam; PF00058; Ldl_recept_b; 7.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00192; LDLa; 15.
DR SMART; SM00135; LY; 9.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 14.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 15.
DR PROSITE; PS51120; LDLRB; 8.
DR PROSITE; PS51666; QLQ; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 127..162
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 421..493
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 700..865
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1018..1180
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1385..1455
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REPEAT 1651..1693
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1694..1736
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1737..1782
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1783..1826
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1924..1961
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2173..2291
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REPEAT 2925..2968
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2969..3013
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 3014..3059
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 3060..3103
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..625
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1951..1960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2053..2068
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2178..2239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 2186..2232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 2253..2277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 2329..2344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2348..2360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2355..2373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2367..2382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2408..2423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2450..2465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2491..2506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2533..2548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2573..2588
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2613..2628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2653..2668
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2693..2708
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2713..2725
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2720..2738
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2732..2747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2754..2766
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2761..2779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2773..2788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2804..2816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2811..2829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2823..2838
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 3201 AA; 358632 MW; 8926A767AD9D89BE CRC64;
MRMFFIRFVC FDHLLFAEKE TLTKKMASIA GFQYTPENMQ RLEKALQTMQ ERGMESDPRY
AQLMSLLRAK PASVDMQDAR HGLQLPPPSM SMGLGNIPPG TGVGGDMQTR NSPAPNLLSQ
ASQKAHSFSS PQLLQLRAQI MAYKLLARSQ PLPEHIRIAI QGKSPSAKPA GSGIPSSGVP
PQSSQLPSRT QNQPGNQSAP QSQANIGAGS STTSPAVPVP NQTAYNVPGM TAAQQLQSKQ
ATGTSQSTTP ASWEAAKGAA ASAIAAATQQ HKLKEQQRQA LAQQQQQQQQ QQRKVQTPGT
TQGGIQMPSK PRLAPVAKPV GLDPVTILKE RENRIQARIV QRIRDLEGLP GSIPDDLRMK
AMIELRALRL LNFQKQLRAE VVACTRRDTT LETALNSKAY KRSKKQSLRE ARITEKLEKQ
QKMEQERKRR QKHQEYLNTI LQHARDFREY HRSIQSKVVK LNRAVMSYHS ITDREKKKEE
ERIEKERMRR LMAEDEEGYR KLIDQKKDKR LAYLLGQTDE YVASLTKMVQ QHKREQRKKQ
MKENRKRRKS DYDDDETPEG NRHVPVVDTE TGMVLKGDDA PIADNLDSWL ESHPGYQVAP
RQEQESDDEE EEEGSVEDAE GDEEADKEAD EKKTEKEKKR EEYGKDEEDV EEEADDPTVL
ESRQYYRIAH SFQEDITEQP TILIGGKLKE YQMRGLEWLV SLHNNALNGI LADEMGLGKT
IQTIALFAYL IEVKKLNGPF LVIVPLSTLS NWLLEFEKWT PSIIVVSYKG SPNMRRSAAS
QIRGGKFNVV LTTYEYVMKD KSVLSKVRWR YMVVDEGHRM KNHHCKLTQI LNTHYAAPHR
VLLTGTPLQN RLPELWALLN FLLPTIFKSC STFEQWFNAP FAMTGEKVEL NGEETLLIIR
RLHKVLRPFL LRRLKKEVES QLPEKVEYVV KCDMSSLQRI LYNHMHKAGV LLTDGSEKDK
KGRGGTKTLM NTIMQLRKIC NHPFLFQHIE ESMAEHLGFP SGIVQGPDVV RVSGKFDLLD
RILPKLKRKN HRVLLFSQMT QLMTILEDYF NWKGFPYLRL DGTTKSEDRG QLLSLFNAKD
SPYFIFLLST RAGGLGLNLQ AADTVVIFDS DWNPHQDLQA QDRAHRIGQK NEVRVLRLMT
VNSVEEKILA AARYKLNVDE KVIQAGMFNQ NSTSSERRAF LMAILDTEND EDETSLLGDE
ISRPQRQEKE ESEVPDDETI NQMIARTEDE FELYQRMDIE RRRQEVREAG SIRRRPRLMQ
TNELPRWIVK DDAEVERLTW EEESEKIFGR GSRVRKDVVY CEHLTERQWL KAIEDGRLDE
VEEKQKVKKL SKKRKHDPGE EGDVPKVKKK RGRPPAVKLA PNPPELTKQM KKLMKYIVRY
VDDSTSRNLA EIFMVLPTRK ELPDYYQIIK QPVDIRKIRE RINSHKYRTL DDLEEDFTLM
CKNAQTYNIE GSIIYEDSIK LQSIFTHARQ KIQGGEDLQL AHSSAAEPEV ESEKEASEGE
EEDDGNDSDG EEAESVGSDI EGGSSQSSLK MRIKLGKQSV EKAKVELGGV KKKRRGRPPR
IRQEPSDNEI ESYPPSEKGY SSEGEGSDRE DYPGSSQEMA ASPSQKKHTP GFLLVANRKD
ILRVELDPVA HKTLVPRQMA AVAIDFDFGT GFVFWTDVAE GNIQRVPVDN GGNTEVLIDG
LVSPEGLAVD WMNKKLYWTD TGTDTIEVAG FDGGHRMVLI NTGLKKPRAL VVHPSAGYMF
WSDWGNAAKI EKCGMDGEST SRKVLVSNNI VWPNGLTIDY NDDRIWWSDA RLGTIESIDL
NGGDRRVTLR SNRARYTFGI SLFQDSVYVA KRQGGRRILK MDKSGSKRPM TILRHLYGPR
GIVVYHSSRQ PGTGNNPCSD SVDSGGCSHI CLLAPKDLAP KGYSCHCPPG LVMLQDQKTC
MSSDGLKCSE RMCLNGGTCI EKAKTLPRCS CPSDYKGPRC QEIIPTLAPM QVSTTTSPST
RKASNGSCGA DQIMCKDTGV CVDKASVCGG DDGDCRELSE EELCGNATVI SKCGSKLFKC
RETGHCLKNF HVCDGSYDCD DKSDEEGCNS TVPCGASEFK CRDSGACMPE IVSCEKFPQI
GEKACIAVNP TAPISLPAAS LETYALMCTK ESCFRGGTCI EGFKPFPSCS CKCEEIIKTL
PPAHISTTIS PSTKQDSCEP LTLPLCRSMP YNTTIFPNLL NHATQDEAAL DVQLFYPLVK
YACSEHLEFF LCAVYAPVCS VLKAAVPPCR SLCNGARLGC GDVMKRFGFK WPETLNCERF
PLEGASNCVG VNGSMGPTSL PQTTSSRSCL TSQFICNSTK ECIDKSLLCD GNDDCGDNSD
EDSCGNECDN NEFQCDDRSC ILISAVCDGK IDCVDKSDET RCNYTQACTS NQFQCRSTGV
CINKVFVCDG SNDCGDMSDE EKCNTTALCS ITDQFQCGAF ERCIEKVLVC DGNDDCGDNS
DEVDCEDDRL CNADEFKCNT TRRCIPAKWV CDGISHCPDS SDEANCNNTE CVGEDRFRCK
SRAGACIPTT WICDGQDDCG DDSDEVNCTL PQCETGEFIC KPSKSCMPVR WKCDGESDCP
DESDEADCPE FLCKREYFKC KSVEKCIPEK WVCDSDDDCD DKSDEVNCAN NTCEAWLFSC
ETSGKCLRKT WVCDGQDDCS DGSDEKNCTR SKCEDEEFSC SASGTCIPKK QRCNGVNDCH
DNSDELNCTL PVCEEGQFLC GSRGCAPNAW RCDGDSDCPG NSDEVNCPTV AAKCSNREFQ
CKDSSCIHVG WVCDGDPDCE DNSDEFNCTS PRECPGNICG DGLCETNQFI CENGRCIDVQ
ERCDGKDDCS DGTDEADCDQ EVCKIRGNCS QGCSVDGDVY ICKCTEGYEL TSDNKTCRAL
GPEGFVFAAN RKDIRRFSMN TLTPELVVTS DQTNSFFLDF NFDTKHIYWS DMVHDNIRRA
PIDNGSDIEV VIEGNLNRPE GITVDWINKK LYWIDANSTE SEIEVADLSG KNRLSLIQGD
MQEPRAIAVH PLLGYLFWTD WGKPSKIERC AMNGDSATRK AIITENIGWP NGITIDYTLN
RIWWTDAKLH TIESADLNGK HRKVFLKARP LKRPFGISVF LDSVFWTDWQ TSKLHVANKF
TGRVVNAVVL QMPMDVVVFH RQRQPIGSNP CNVTALLGGC SHICLLAPVD SYPQGFSCRC
PPGLTLLADQ KTCNPQAQPQ L
//
