PRD10_DANRE
ID PRD10_DANRE Reviewed; 1121 AA.
AC A2BID7; Q1LV64;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=PR domain zinc finger protein 10;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 10;
GN Name=prdm10; ORFNames=si:ch211-151h10.3, si:dkey-11k4.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC methyltransferase activity.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM13007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX908391; CAK04147.1; -; Genomic_DNA.
DR EMBL; BX908399; CAM13007.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2BID7; -.
DR SMR; A2BID7; -.
DR ZFIN; ZDB-GENE-050419-74; prdm10.
DR InParanoid; A2BID7; -.
DR PhylomeDB; A2BID7; -.
DR PRO; PR:A2BID7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19194; PR-SET_PRDM10; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044403; PRDM10_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 3: Inferred from homology;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1121
FT /note="PR domain zinc finger protein 10"
FT /id="PRO_0000363965"
FT DOMAIN 173..290
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 319..341
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 500..522
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 529..551
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 557..579
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..608
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 613..635
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..664
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 696..719
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 741..764
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 803..826
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 401
FT /note="E -> D (in Ref. 1; CAK04147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 126179 MW; 13D642EEA8FD6C2B CRC64;
MEAKQESSTV WSTASNNDTG NTPQVHFEAG AVAQIVYSGD QSDRTQQQVV YAADGSSYTS
VESAEHTLVY IHPADGTQSQ LAVTNAALPT LTEASSSPLG ATDSTVDSED EEEDNDSEDS
EMDDWEPRAL QPFTPQNLWC EDCNNANPAA CIKHGPLHPI LNRPVMSKAR ASLPLVLYID
RFLGGVFTKR RIPKRTQFGP LEGPLVRQSE LLDTHIHLKL YMLDPEKEGE RAQDLWFDLS
DEERCNWMMF VRPAQNHLEQ NLVAYQYGSD IFYTSIKNIQ PKQELKVWYA ASYAEFVNQK
VHDVTEEERK VLREQEKNWP CYECNRRFMS SEQLQQHLNM HDDKLNLIQR PKSRGRGRGR
KRFGGARRPG RRTKFLCPQT PVESADKTQE LLASVDKLQF EERTDGALNG LKVVEMAAES
METETEDALD PPPIHTESLQ DEEDSVTPPP VTEIPESAKD DLSHTSPIDP HLTPQDMRRA
RRIRNAALKH LFIRKSFRPF KCPQCGKAFR DKEKLEQHMR FHGRDGCRHV CHQCGKGFLS
STSLEDHLVL HSDQRNYSCL FCAESYDRLE LLKVHVGIHM VNGCFLCPSC KKSFTDFIQV
KKHVRSFHSE KVFQCSECDK AFCRPDKLRL HMLRHSDRKD FLCSTCGKQF KRKDKLREHM
QRMHNPEREA KKADRIHRTK ALKQKEPTTD FESFMFKCRL CMMGFRRRGM LVNHLSKRHP
EMRLEEVPEL TLPIIKPNRD YYCQYCDKVY KSASKRKAHI LKNHPGAELP PSIRKLRPAG
PGEPDPMLST HTQLTGTIAT APVCCPHCAK QYSSKTKMVQ HIRKKHPEYQ YNSSSNIQAP
LAATVISSTP AVITTDGTTA EAVVTTDLLT QAMTELSQTL TTDYRTAQGD FQRIQYIPVS
QAGGGLSQPQ HIQLQVVQVA PASSPHSQHS TVDVSQLHDP HSYSQHSIQV QHIQVAEPTA
AVQANAQVSG QPLSPSSQQA AQELSTAQLT PVTLAQQTLQ TSSNQTQGAT QHAYLPSNWN
YRSYPSEIQM MALPHTQYVI AEASTPVTAA VNSSQVKTTH YVISDGQTEL DGKQVSVPST
ATQGHPDPLE QPAGGQQATT QYIITTTTNG AGASEVHITK P
