ID L5LJ83_MYODS Unreviewed; 598 AA.
AC L5LJ83;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Hypermethylated in cancer 2 protein {ECO:0000313|EMBL:ELK26277.1};
GN ORFNames=MDA_GLEAN10020136 {ECO:0000313|EMBL:ELK26277.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26277.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB111160; ELK26277.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LJ83; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR CDD; cd18334; BTB_POZ_ZBTB30_HIC2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF22; HYPERMETHYLATED IN CANCER 2 PROTEIN; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 28..91
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 425..452
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 488..515
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 516..543
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 544..571
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 572..598
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 160..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 64618 MW; 3FCBD51099D6B8BC CRC64;
MGPDMELPSH SKQLLLQLNQ QRTKGFLCDV IIMVENSIFR AHKNVLAASS IYFKSLVLHD
NLINLDTDMV SSTVFQQILD FIYTGKLLPS DQPAEPNFST LLTAASYLQL PELAALCRRK
LKRAGKPFGS GRVGAAGMGR PPRSQRLSTA SVIQARYPGL MDGRKGAHTP QELPQAKGSD
DELFLGSSNQ ESAHSLGRAI CPASGEAGLG SCSTNGSSGG CEQELGLDLS KKSPPLPPAT
PGPPLTPDDP AQLSDSQHGS PLSASAPPVA NSASYADLGG TPSEPMDLEG PEDNHLSLLE
GPGGQPRKSL RHSARKKEWS KKEPMAGSPF ERREVGPKGS CPGEESEGLG DRVPNGILAS
GVAGGGPSGP YREPPYPCKE EEENGKDGSE DSGQSESEGG SGHASAHYMY RQEGYETVSY
GDNLYVCIPC AKGFPSSEQL NAHVETHTEE ELFIKEEGAY ETGSGGAEEE AEDLSTPSAA
YAAEPRPFKC SVCEKTYKDP ATLRQHEKTH WLTRPFPCNI CGKMFTQRGT MTRHMRSHLG
LKPFACDECG MRFTRQYRLT EHMRVHSGEK PYECQLCGGK FTQQRNLISH LRMHTSPS
//