PRD10_PONAB
ID PRD10_PONAB Reviewed; 1117 AA.
AC Q5RAX9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858882; CAH91081.1; -; mRNA.
DR RefSeq; NP_001125628.1; NM_001132156.1.
DR AlphaFoldDB; Q5RAX9; -.
DR SMR; Q5RAX9; -.
DR STRING; 9601.ENSPPYP00000004643; -.
DR GeneID; 100172546; -.
DR KEGG; pon:100172546; -.
DR CTD; 56980; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5RAX9; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 4.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..1117
FT /note="PR domain zinc finger protein 10"
FT /id="PRO_0000363964"
FT DOMAIN 182..300
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 329..351
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 530..552
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 558..580
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..609
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 614..636
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 642..665
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..720
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..765
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 804..827
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 96..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV6"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV6"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV6"
SQ SEQUENCE 1117 AA; 126746 MW; C84E0E1B4E1835F0 CRC64;
MDSKDESSHV WPTSAEHEQN AAQVHFVPDT GTVAQIVYTD DQVRPPQQVV YTADGASYTS
VDGPEHTLVY IHPVEAAQTL FTDPGQVAYV QQDATAQQTP LGGLEAKEEE DEDEDEDTEE
DEEEDGEDAD LDDWEPDPPR PFDPHDLWCE ECNNAHSSVC PKHGPLHPIP NRPVLTRARA
SLPLVLYIDR FLGGVFSKRR IPKRTQLGPV EGPLVRGSEL KDCYIHLKVS LDKGDRKDRD
LHEDLWFELS DETLCNWMMF VRPAQNHLEQ NLVAYQYGHH VYYTTIKNVE PKQELKVWYA
ASYAEFVNQK IHDISEEERK VLREQEKNWP CYECNRRFIS SEQLQQHLNS HDEKLDVFSR
TRGRGRGRGK RRFGPGRRPG RPPKFIRLEI TSENGEKSDD GTQDLLHFPT KEQFDEAEPA
TLNGLDQPEQ TTIPIPQLPQ ETQSSLEHEP ETHTLHLQPQ HEESVVPTQS TLTADDMRRA
KRIRNAALQH LFIRKSFRPF KCLQCGKAFR EKDKLDQHLR FHGREGNCPL TCDLCNKGFI
SSASLESHMK LHSDQKTYSC IFCPESFDRL DLLKDHVAIH INDGYFTCPT CKKRFPDFIQ
VKKHVRSFHS EKIYQCTECD KAFCRPDKLR LHMLRHSDRK DFLCSTCGKQ FKRKDKLREH
MQRMHNPERE AKKADRISRS KTFKPRITST DYDSFTFKCR LCMMGFRRRG MLVNHLSKRH
PDMKIEEVPE LTLPIIKPNR DYFCQYCDKV YKSASKRKAH ILKNHPGAEL PPSIRKLRPA
GPGEPDPMLS THTQLTGTIA TPPVCCPHCS KQYSSKTKMV QHIRKKHPEF AQLSSTIHTP
LTTAVISATP AVLTTDSATG ETVVTTDLLT QAMTELSQTL TTDYRTPQGD YQRIQYIPVS
QSASGLQQPQ HIQLQVVQVA PATSPHQSQQ STVDVGQLHD PQPYPQHAIQ VQHIQVSGQP
LSPSAQQAQQ GLSPSHIQGS SSTQGQALQQ QQQQQQNSSV QHTYLPSAWN SFRGYSSEIQ
MMTLPPGQFV ITDSGVATPV TTGQVKAVTS GHYVLSESQS DLEEKQTSAL SGGVQVQPPA
HSDSLDPQTT SQQQTTQYII TTTTNGNGSS EVHITKP
