ID A0A087WNX7_MOUSE Unreviewed; 3114 AA.
AC A0A087WNX7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Snf2-related CREBBP activator protein {ECO:0000313|Ensembl:ENSMUSP00000139536.2};
GN Name=Srcap {ECO:0000313|Ensembl:ENSMUSP00000139536.2,
GN ECO:0000313|MGI:MGI:2444036};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000139536.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000139536.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139536.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000139536.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139536.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR SMR; A0A087WNX7; -.
DR jPOST; A0A087WNX7; -.
DR ProteomicsDB; 368125; -.
DR Ensembl; ENSMUST00000186954.5; ENSMUSP00000139536.2; ENSMUSG00000053877.13.
DR AGR; MGI:2444036; -.
DR MGI; MGI:2444036; Srcap.
DR VEuPathDB; HostDB:ENSMUSG00000053877; -.
DR GeneTree; ENSGT00940000157457; -.
DR ChiTaRS; Srcap; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000053877; Expressed in undifferentiated genital tubercle and 181 other cell types or tissues.
DR ExpressionAtlas; A0A087WNX7; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 3.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 124..196
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 642..807
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1887..2040
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2201..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2498..2521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2562..2638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2653..2859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2879..2966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3000..3114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2170..2197
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2253..2272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2277..2341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2500..2521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2586..2601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2668..2731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2799..2816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2819..2834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2939..2964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3114 AA; 333620 MW; 84C77F956155A25E CRC64;
MQSSPSTAHP QLPILQTQMV SDGMTGSNPV SPASSSSPDS SGAGGISPQH IAQDSSLDGP
PGPQDGTTVP LEGFSLSHAA DLVNRGQKWE KSHAEIAEQA KHEAEIETRI AELRKEGFWS
LKRLPKVPEP PRPKGHWDYL CEEMQWLSAD FAQERRWKRG VARKVVRMVI RHHEEQRQKE
ERARREEQAK LRRIASTMAK DVRQFWSNVE KVVQFKQQSR LEEKRKKALD LHLDFIVGQT
EKYSDLLSQS LNQPPASSKA GSSPCLGSSS AASSPPPPVS RLDDEDGDFQ PQEEEEEDDE
ETIEVEEQQE GNDAETQRRE IELLRHEGEL PLEELLRSLP PQLLGGPFSP SQTPSHDSDT
QDGPEENIEE EPSQDLEVHP PSSAVTQCNK QRWHPDEDDE EFTANEDEAE DEEDTIAAEE
QLEGEVDHAM ELSELAREGE LSMEELLQQY AGAYACDASA PASGDSEDED EVEANSSDGE
LEETVEEAAQ EDSSSQSDSA EECSEDEEDE HSEEEMSGSS QSEESESDES EDAQSQSQAD
EEQDDEGEDD DVDDDDDDGF GVEYLLARDD ERSEVDGGSG PPTPGPTTTL GPKKEITDIA
AAAESLQPKG YTLATTQVKT PIPLLLRGQL REYQHIGLDW LVTMYEKKLN GILADEMGLG
KTIQTISLLA HLACEKGNWG PHLIIVPTSV MLNWEMELKR WCPSFKILTY YGAQKERKLK
RQGWTKPNAF HVCITSYKLV LQDHQAFRRK NWRYLILDEA QNIKNFKSQR WQSLLNFNSQ
RRLLLTGTPL QNSLMELWSL MHFLMPHVFQ SHREFKEWFS NPLTGMIEGS QEYNEGLVKR
LHKVLRPFLL RRVKVDVEKQ MPKKYEHVIR CRLSKRQRCL YDDFMAQTTT KETLATGHFM
SVINILMQLR KVCNHPNLFD PRPVTSPFIT PGICFSTASL VLRATEVHPL QRIDMGRFDL
IGLEGRVSRY EADTFLPRHR LSHRILLEIA TAPDPPPRPK PVKMKVNRML QPVPKQEGRT
VVVVNSPRPP LGPVPVRPPP GPEVSAQPAL GPVPPVLPAP LMVSASPAGT PVVPASRPPG
PVLLSPLQPN TGPLPQAGEV VSIGQLASLA QRPVTSAGGS KPLTFQIQGN KLTLTGAQVR
QLAVGQPRPL QMPPSMVNNT GVVKIVVRQA PRDGLTPVPP LAPAPRPSSS GLPAVLTSRP
TLTPSRLSSP TLGTTRTPIP TPTLVRPLLK LVHSPSPEVS ASAPGAAPMT ISSSLHMPSS
LPGPASSPMT IHNSSPLSSP VSSTVSVPVS SSLPISVPTT LPVPTSAPLP IPITAPLPVS
DLGPALLTSV TPALAVVSAA SGPPLASAGV SPSMSALALG LATTPALSPP QTSGHSLLLA
TTSSHVPGLN SAVAPACSPV LVSASALTSP FPVSPSSAPA QASLLAAAPS TSQALATSLA
PMAASQTAIL GPSPTPPLAP LPVLAASQTP LPAMTPPSMS GTPLPSSSLV SAPTSVLAPS
STQTLVSTPV SSPLSSLAST QTLTLAPTLA PTLGGLSPSQ THSLGTGSPQ GPFPIQTLSL
TPASSLVPTP AQTLSLAPGG PVGPTQTLSL APVPPLPPSS PVGPAPGHTL TLAPAASSAS
LLVPTSVQTL TLSPAPVPVP TLDLSATQTL ALAPALTQAP ASQASSLVSA SGAASLPVTM
VNRLPVPKDE PETLTLRSGP PSPLPTATSF SGPRPRRQPP PPPRSPFYLD SLEEKRKQQR
SERLDRIFQL SEAHGALAPV YGTEVLDFCT LPQPVASPIG PRSPGPSHPI FWTYTEAARR
AVLFPQQRLE QLSEIIERFI FVMPPVEAPP PSLHACHPPP WLAPHQAAFQ EQLACELWPR
ARPLHRIVCN MRTQFPDLRL IQYDCGKLQT LAVLLRQLKA EGHRVLIFTQ MTRMLDVLEQ
FLTYHGHLYL RLDGSTRVEQ RQALMERFNA DKRIFCFILS TRSGGVGVNL TGADTVVFYD
SDWNPTMDAQ AQDRCHRIGQ TRDVHIYRLI SERTVEENIL KKANQKRMLG DMAIEGGNFT
TAYFKQQTIR ELFDMPLEEP PGSSVSSVPE DEEEAVASKQ THILEQALCR AEDEEDIRAA
TQAKAEQVAE LAEFNENDGF PAGEGEEANR PGPGAEDEEM SRAEQEIAAL VEQLTPIERY
AMKFLEASLE EVSREELKQA EEQVEAARKD LDQAKEEVFR LPHEEEEGPG AGDEMSCGSS
GASHRRSKKI RAPERLGTRV SERLRGARAE TQGANHTPVT SSHHTCNTFV PPQCSPVRER
IPRPVPRPRP PPPPPAPPPP PAPPASPSPA PPPPPAPASP APPAPPASPP AASPSPAPLP
PAASVASAIT SALATAPIPI SAPNPVTILP VHILPTPPLL QLPPSSSPAS TPPSACTPLP
TCTPLQAQTS VLTSSSPAPL DSLSVPISPG VTNLPLDSGE VGLCAQELAP VESLELPGMT
NSEASLASLV SPKDLLPVAV DILPESEKTL PCIPAPSSTL EAESIPNGQQ QEVPGPVEGT
NTTLLPGSEE LTMSLNESNG LELPPSAASA EPLDELLETH RNSGETREVQ IPISNSEKPQ
ELVRAEVTAP STSSSATSSP EGPLPARPPR RRTSADVEIR GQGSGRTGQL PGPKVLRKLP
GRLVTVVEEK ELVKRRRHRA PASTLVPGVS EVSASPRSPS IHSMSGPESS PPSSGPCEAA
PTSSLSTPTQ STFIACRHNE LGTTTGGSPE NGEGTELAIT PPAVKRRRGR PPKKNRSPAD
AGRGVDEVPS SISKGKTNGV DPVPGPETVT VAEPDLRPQF VPGPQPPGPQ PVHRPEPTIL
SPVEKRRRGR PPKARDLPIP GTISSPGGGN LESRTQSLPF PAPLTPLLAC PTAVTNTVTT
VTISTSPPKR KRGRPPKNPP SPRPSQHPVL DPDSSSILES CGLGVQRQPL GQAESEGSSS
DEDGSRPLTR LARLRLEAEG MRGRKSEGSM VMAVIQDDLD LADSGPSGLE LTPPVVSLTP
KFRSTRLRPG SLVPPLETEK MPRKRSGAPV GSSGMAKRGR LQPPSPLGPE GSVEESEVEA
SGDEEEGDGT PRRRTGPRRL VGTTNQGDQR ILRSSAPPHL CIPTISHRGR KAKT
//
