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Database: UniProt
Entry: H0UY50_CAVPO
LinkDB: H0UY50_CAVPO
Original site: H0UY50_CAVPO 
ID   H0UY50_CAVPO            Unreviewed;      1051 AA.
AC   H0UY50;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 {ECO:0000313|Ensembl:ENSCPOP00000002050.2};
GN   Name=SMARCA5 {ECO:0000313|Ensembl:ENSCPOP00000002050.2};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000002050.2, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000002050.2}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002050.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; AAKN02012070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02012071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003477037.1; XM_003476989.3.
DR   AlphaFoldDB; H0UY50; -.
DR   STRING; 10141.ENSCPOP00000002050; -.
DR   Ensembl; ENSCPOT00000002291.3; ENSCPOP00000002050.2; ENSCPOG00000002259.4.
DR   GeneID; 100729120; -.
DR   KEGG; cpoc:100729120; -.
DR   CTD; 8467; -.
DR   VEuPathDB; HostDB:ENSCPOG00000002259; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00940000156733; -.
DR   HOGENOM; CLU_000315_0_3_1; -.
DR   InParanoid; H0UY50; -.
DR   OMA; KIAGDNW; -.
DR   OrthoDB; 5482994at2759; -.
DR   TreeFam; TF300674; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002259; Expressed in pituitary gland and 12 other cell types or tissues.
DR   GO; GO:0016590; C:ACF complex; IEA:Ensembl.
DR   GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR   GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl.
DR   GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0090536; C:NoRC complex; IEA:Ensembl.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0016589; C:NURF complex; IEA:Ensembl.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0031213; C:RSF complex; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0090535; C:WICH complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR   GO; GO:0140751; F:histone octamer slider activity; IEA:Ensembl.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:Ensembl.
DR   GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IEA:Ensembl.
DR   GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR   GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR   CDD; cd18064; DEXHc_SMARCA5; 1.
DR   CDD; cd00167; SANT; 2.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   DOMAIN          191..356
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          486..637
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          839..891
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  121591 MW;  92AD7F02F1CAD3D8 CRC64;
     MSTAAEPPPP PPPESAPSKP AALAGGASSS GNKGGSEGAA ALAVPAAAGA GPADAEVEEV
     FDDASPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL FAHFIQPAAQ KTPTSPLKMK
     PGRPRVKKDE KQNLLSVGDY RHRRTEQEED EELLTESSKA TNICTRFEDS PSYVKWGKLR
     DYQVRGLNWL ISLYENGING ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL
     HNWMSELKRW VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
     WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL NFLLPDVFNS
     ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE KSLPPKKEVK IYVGLSKMQR
     EWYTRILMKD IDILNSAGKM DKMRLLNILM QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN
     SGKMVVLDKL LPKLKEQGSR VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS
     INAYNEPNST KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
     VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML QMIRHGATHV
     FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR NFTMDTESSV YNFEGEDYRE
     KQKIAFTEWI EPPKRERKAN YAVDAYFREA LRVSEPKAPK APRPPKQPNV QDFQFFPPRL
     FELLEKEILY YRKTIGYKVP RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG
     FTNWNKRDFN QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
     AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE DRFLICMLHK
     LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC NTLITLIERE NMELEEKEKA
     EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK L
//
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