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ZCPW2_MOUSE
ID   ZCPW2_MOUSE             Reviewed;         331 AA.
AC   Q08EN7; A0A5F8MP94;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Zinc finger CW-type PWWP domain protein 2 homolog;
GN   Name=Zcwpw2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Histone methylation reader which binds to non-methylated
CC       (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and
CC       trimethylated (H3K4me3) 'Lys-4' on histone H3 (By similarity). The
CC       order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0
CC       (By similarity). {ECO:0000250|UniProtKB:Q504Y3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08EN7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08EN7-2; Sequence=VSP_060790, VSP_060791;
CC   -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC       histone H3K4me3. {ECO:0000250|UniProtKB:Q504Y3}.
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DR   EMBL; AC157475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC104378; AAI04379.1; -; mRNA.
DR   AlphaFoldDB; Q08EN7; -.
DR   SMR; Q08EN7; -.
DR   PaxDb; Q08EN7; -.
DR   PRIDE; Q08EN7; -.
DR   ProteomicsDB; 302119; -. [Q08EN7-1]
DR   Ensembl; ENSMUST00000187803; ENSMUSP00000159064; ENSMUSG00000032443. [Q08EN7-2]
DR   Ensembl; ENSMUST00000191100; ENSMUSP00000159110; ENSMUSG00000032443. [Q08EN7-2]
DR   Ensembl; ENSMUST00000238919; ENSMUSP00000158867; ENSMUSG00000032443. [Q08EN7-1]
DR   MGI; MGI:1921888; Zcwpw2.
DR   VEuPathDB; HostDB:ENSMUSG00000032443; -.
DR   GeneTree; ENSGT00560000077278; -.
DR   InParanoid; Q08EN7; -.
DR   OMA; AFVGHYS; -.
DR   PhylomeDB; Q08EN7; -.
DR   PRO; PR:Q08EN7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q08EN7; protein.
DR   Bgee; ENSMUSG00000032443; Expressed in spermatid and 35 other tissues.
DR   ExpressionAtlas; Q08EN7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR042778; ZCWPW1/ZCWPW2.
DR   InterPro; IPR011124; Znf_CW.
DR   PANTHER; PTHR15999; PTHR15999; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF07496; zf-CW; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS51050; ZF_CW; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..331
FT                   /note="Zinc finger CW-type PWWP domain protein 2 homolog"
FT                   /id="PRO_0000415849"
FT   DOMAIN          83..147
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   ZN_FING         9..64
FT                   /note="CW-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   REGION          264..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   VAR_SEQ         96..125
FT                   /note="SWPGILCPDPFKGKYVTYDQDGNVEKYYVE -> RQQTVRRRRGGIEVPSRK
FT                   HTNSTGVPQSKD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_060790"
FT   VAR_SEQ         126..331
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_060791"
SQ   SEQUENCE   331 AA;  37519 MW;  073465FC27887ABA CRC64;
     MGPAPESSEF VHRTWVQCEN ESCLKWRLLS PAAAAAVNPS EPWYCFMNTD PSYSSCSVSE
     EDFPEESQFL ENGYKFVYSQ LPLGSLVLVK LRNWPSWPGI LCPDPFKGKY VTYDQDGNVE
     KYYVEFLGDP HSTAWMSAAF VGHFSLTLEA ADCTKKKRWY RSALEEAYQL YRCSAEQRLE
     VCCLSKPNRA KTDTKAAVVT KKGMQVSKIN TEKKRPRVRK RKRDAALKCS VEIFCSDEAL
     SKENMVVSET EGLLKELEKM LQQIQEPTAR EDESQGEQLS QCSPESPTGS PFQSYHEEDY
     IVPDGAGLKA GEYIEIITNN LKKIDALISE F
 
 
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