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Database: UniProt
Entry: A0A2Y9GM82_NEOSC
LinkDB: A0A2Y9GM82_NEOSC
Original site: A0A2Y9GM82_NEOSC 
ID   A0A2Y9GM82_NEOSC        Unreviewed;      1207 AA.
AC   A0A2Y9GM82;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Bromodomain and PHD finger-containing protein 3 {ECO:0000313|RefSeq:XP_021540353.1};
GN   Name=BRPF3 {ECO:0000313|RefSeq:XP_021540353.1};
OS   Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Neomonachus.
OX   NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021540353.1};
RN   [1] {ECO:0000313|RefSeq:XP_021540353.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_021540353.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_021540353.1; XM_021684678.2.
DR   AlphaFoldDB; A0A2Y9GM82; -.
DR   STRING; 29088.A0A2Y9GM82; -.
DR   KEGG; nsu:110575675; -.
DR   InParanoid; A0A2Y9GM82; -.
DR   OrthoDB; 163389at2759; -.
DR   Proteomes; UP000248481; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd05512; Bromo_brd1_like; 1.
DR   CDD; cd15703; ePHD_BRPF3; 1.
DR   CDD; cd15572; PHD_BRPF; 1.
DR   CDD; cd20158; PWWP_BRPF3; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR042005; BRPF3_ePHD.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13793:SF19; BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248481};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          212..262
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          266..387
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          607..677
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1078..1161
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          566..593
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        75..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..435
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..865
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..954
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1207 AA;  135594 MW;  9AD9A2D72B3E1CCB CRC64;
     MRKPRRKSRQ NAEGRRSPSP YSLKCSPTRE TLTYAQAQRI VEVDIDGRLH RISIYDPLKI
     ITEDELTAQD ITECNSNKEN SEQPQFPGKS KKPSSKGKKK ESCSKHASGT SFHLPQPSFR
     MVDSGSQPEA PPLPAAYYRY IEKPPEDLDA EVEYDMDEED LAWLDMVNEK RRVDGHSLVS
     ADTFELLVDR LEKESYLESR SSGAQQSLID EDAFCCVCLD DECHNSNVIL FCDICNLAVH
     QECYGVPYIP EGQWLCRCCL QSPSRPVDCV LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC
     FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM
     KIEPMRETSL NGTIFTVRKT AYCEAHSPPG AATARRKGDS PGNLSEAGEE EGLKEGCGEE
     EEKEDIEEEE EDEGQGGVGG PLKGVPKKNK MTLKQKIKKE PEEVGRDTPS TVPMVTVPQI
     PSYRLNKICS GLSFQRKNQF IQRLHNYWLL KRQARNGVPL IRRLHSHLQS QRNAEQREQD
     EKTSAVKEEL KYWQKLRHDL ERARLLIELI RKREKLKREQ VKVQQAAMEL ELMPFNVLLR
     TTLDLLQEKD PAHIFAEPVN LSEVPDYLEF ISKPMDFSTM RRKLESHLYR TLEEFEEDFN
     LIVTNCMKYN AKDTIFHRAA VRLRDLGGAI LRHARRQAEN IGYDPERGTH LPESPKLEDF
     YRFSWEDVDN ILIPENRAHL SPEVQLKELL EKLDLVSAMR SSGARTRRVR LLRREINALR
     QKLAQPSPPP QPPSLNKTVS NGELPAGPQG DAAVLEQAPQ GEPEDDGDRD DSKLPPPPTL
     EPTGPAPSLS EQDSPPDPPT LKPINDSKPP SRFLKPRKVE EDELLEKSPL QIGSEPLQRL
     LSDNGINRVS LMAPDAPAGA PLSGVGRRTS VLFKKAKNGV KLQRSPDRAL ENGEDHGAVG
     SPASPASIED ERHPQKRPRS RSCSESEGER SPRQEEETGV TNGFGKHTES GSDSECSLGL
     SGGLAFEACS GLTPPKRSRG KPALSRVPFL EGVNGDSDYS SSGRSLLMPF EDRGDLEPLE
     LVWAKCRGYP SYPALIIDPK MPREGLLHNG VPIPVPPLDV LKLGEQKQAE AGEKLFLVLF
     FDNKRTWQWL PRDKVLPLGV EDTVDKLKML EGRKTSIRKS VQVAYDRAMI HLSRVRGPHS
     FVTSSYL
//
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