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Database: UniProt
Entry: A0A2Y9SX50_PHYMC
LinkDB: A0A2Y9SX50_PHYMC
Original site: A0A2Y9SX50_PHYMC 
ID   A0A2Y9SX50_PHYMC        Unreviewed;       553 AA.
AC   A0A2Y9SX50;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Heterochromatin protein 1-binding protein 3 {ECO:0000256|ARBA:ARBA00019297};
GN   Name=HP1BP3 {ECO:0000313|RefSeq:XP_007120691.1,
GN   ECO:0000313|RefSeq:XP_023981114.1, ECO:0000313|RefSeq:XP_023981115.1,
GN   ECO:0000313|RefSeq:XP_023981116.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023981115.1};
RN   [1] {ECO:0000313|RefSeq:XP_007120691.1, ECO:0000313|RefSeq:XP_023981114.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007120691.1,
RC   ECO:0000313|RefSeq:XP_023981114.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_007120691.1; XM_007120629.4.
DR   RefSeq; XP_007120692.1; XM_007120630.1.
DR   RefSeq; XP_007120693.1; XM_007120631.1.
DR   RefSeq; XP_023981114.1; XM_024125346.3.
DR   RefSeq; XP_023981115.1; XM_024125347.3.
DR   RefSeq; XP_023981116.1; XM_024125348.3.
DR   STRING; 9755.ENSPCTP00005018348; -.
DR   Ensembl; ENSPCTT00005020216; ENSPCTP00005018348; ENSPCTG00005013029.
DR   GeneID; 102995224; -.
DR   KEGG; pcad:102995224; -.
DR   CTD; 50809; -.
DR   OrthoDB; 3029985at2759; -.
DR   Proteomes; UP000248484; Chromosome 3.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0031491; F:nucleosome binding; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0070828; P:heterochromatin organization; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0097298; P:regulation of nucleus size; IEA:Ensembl.
DR   CDD; cd00073; H15; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 3.
DR   InterPro; IPR005818; Histone_H1/H5_H15.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR15832:SF1; HETEROCHROMATIN PROTEIN 1-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR15832; SHC (SRC HOMOLOGY DOMAIN C-TERMINAL) ADAPTOR HOMOLOG; 1.
DR   Pfam; PF00538; Linker_histone; 3.
DR   SMART; SM00526; H15; 3.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR   PROSITE; PS51504; H15; 3.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT   DOMAIN          157..232
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   DOMAIN          255..330
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   DOMAIN          337..413
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   REGION          29..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..447
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  61203 MW;  D904822F13AA890D CRC64;
     MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDNTMP IRRAVNSTRE TPPKSKLAEG
     EEEKPEPDVS SEESVSTVEE QENETPPATS SETEQPKGQP ENEEKEENKP SEETKKDEKD
     QSKEKEKKVK KTIPSWATLS ASQLARAQKQ TPMASSPRPK MDAILTEAIK ACFQKSGASV
     VAIRKYIIHK YPSLELERRG YLLKQALKRE LNRGVIKQVK GKGASGSFIV VQKSRKTPQK
     SRNRKNRSSA VDPEPQVKLE DILPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
     LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
     TTALKKYVLE NHPGTNSNYQ MHLLKKTLQR CEKNGWMEQI SGKGFSGTFQ LCFPYYPSPG
     VLFPKKEPDD SKDEAEDEDE SSEEDSEDEE PPPKRRLQKK TPAKSPGKAA SMKQRGSKPA
     PKVPAAQRGK ARPLPKKAPP KAKTPAKKAR PSPPVIKKPS GSSSKKPAAS VRKEVKLPGK
     GKSTMKKSFK AKK
//
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