ID A0A2K6BXY8_MACNE Unreviewed; 1123 AA.
AC A0A2K6BXY8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=MDS1 and EVI1 complex locus {ECO:0000313|Ensembl:ENSMNEP00000016269.1};
GN Name=MECOM {ECO:0000313|Ensembl:ENSMNEP00000016269.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000016269.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000016269.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6BXY8; -.
DR STRING; 9545.ENSMNEP00000016269; -.
DR Ensembl; ENSMNET00000040484.1; ENSMNEP00000016269.1; ENSMNEG00000032164.1.
DR GeneTree; ENSGT00940000157208; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032164; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24393:SF161; LOW QUALITY PROTEIN: MDS1 AND EVI1 COMPLEX LOCUS PROTEIN EVI1-RELATED; 1.
DR PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR Pfam; PF13912; zf-C2H2_6; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 93..121
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 147..174
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 175..202
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 203..231
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 232..259
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 260..287
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 289..316
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 805..832
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 833..861
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 862..889
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..978
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 126523 MW; 2763B39F74F8A078 CRC64;
MRTSATATKI LDEFYNVKFC IDASQPDVGS WLKYIRFAGC YDQHNLVACQ INDQIFYRVV
ADIAPGEELL LFMKSEDYPH ETMAPDIHEE RQYRCEDCDQ LFESKADLAD HQKFPCSTPH
SAFSMVEEDF QQKLESENDL QEIHTIQECK ECDQVFPDLQ SLEKHMLSHT EEREYKCDQC
PKAFNWKSNL IRHQMSHDSG KHYECENCAK VFTDPSNLQR HIRSQHVGAR AHACPECGKT
FATSSGLKQH KHIHSSVKPF ICEVCHKSYT QFSNLCRHKR MHADCRTQIK CKDCGQMFST
TSSLNKHRRF CEGKNHFAAG GFFGQGISLP GTPAMDKTSM VNMSHANPGL ADYFGANRHP
AGLTFPTAPG FSFSFPGLFP SGLYHRPPLI PASSPVKGLS STEQTNKSQS PLMTHPQILP
ATQDILKALS KHPSVGDNKP VELQPERSSE ERPLEKISDQ SESSDLDDVS TPSGSDLETT
SGSDLESDIE SDKEKFKENG KMFKDKVSPL QNLASINNKK EYSNHSIFSP SLEEQTAVSG
AVNDSIKAIA SIAEKYFGST GLVGLQDKKV GALPYPSMFP LPFFPAFSQS MYPFPDRDLR
SLPLKMEPQS PGEVKKLQKG SSESPFDLTT KRKDEKPLTP VPSKPPVTPA TSQDQPLDLS
MGSRSRASGT KLTEPRKNHV FGEKKGSNVE SRPASDGSLQ HARPTPFFMD PIYRVEKRKL
TDPLEALKEK YLRPSPGFLF HPQFQLPDQR TWMSAIENMA EKLESFSALK PEASELLQSV
PSMFNFRAPP SALPENLLRK GKERYTCRYC GKIFPRSANL TRHLRTHTGE QPYRCKYCDR
SFSISSNLQR HVRNIHNKEK PFKCHLCDRC FGQQTNLDRH LKKHENGNMS GTATSSPHSE
LESTGAILDD KEDAYFTEIR NFIGNSNHSS QSPRNVEERM NGSHFKDEKA LVTSQNSDLL
DDEEVEDEVL LDEEDEDNDI TGKTGKEPVT SNLHEGNPED DYEETSALEM SCKTSPVRYK
EEEYKSGLSA LDHIRHFTDS LKMRKMEDNQ YSEAELSSFS TSHVPEELKQ PLHRKSKSQA
YAMMLSLSDK ESLHSTSHSS SNVWHSMARA AAESSAIQSI SHV
//