ID V9KMD1_CALMI Unreviewed; 599 AA.
AC V9KMD1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Metal-response element-binding transcription factor 2-like protein {ECO:0000313|EMBL:AFO99326.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO99326.1};
RN [1] {ECO:0000313|EMBL:AFO99326.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:AFO99326.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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DR EMBL; JW866809; AFO99326.1; -; mRNA.
DR AlphaFoldDB; V9KMD1; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IEA:UniProt.
DR CDD; cd15578; PHD1_MTF2; 1.
DR CDD; cd15580; PHD2_MTF2; 1.
DR CDD; cd20450; Tudor_MTF2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.90.980.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR042014; MTF2_PHD1.
DR InterPro; IPR042015; MTF2_PHD2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12628:SF12; METAL-RESPONSE ELEMENT-BINDING TRANSCRIPTION FACTOR 2; 1.
DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF14061; Mtf2_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 103..158
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 68083 MW; 41708E48AE0BB56D CRC64;
MDRDTTGAGN SSLHKRSPSR RNQKTPVSSV HLSLRDGPKG KQTVCKFEEG QDVLARWSDG
LFYLGTVKKV NKQKESCFVI FEDSSKSWVL WKDIQTGASG SGEMVCTICQ EEYSEAPNEM
VICDKCGQGY HQKCHIPNID SSVIASDAKW LCRQCVFATT TKRGGALKKG PNAKALQVMK
QTLPYQLEDL QWDLGHKTNH QQCYCYCGGP GDWYLKMLQC WRCKQWFHEA CIQCLQKPML
YGDRFYLFIC SVCNSGPEYL KRLPLRWVDI AHLSLYNLSV IHKKKYFDSE LELMTYINEN
WDRLQPGELI DTLKTERYDH ILEALNENKC MFMSGKEIKK KKHLFGLRIR VPPIPPNTAL
KTEESNEEVS HEFKIKGRKS SKSTVLPVSI RSSLSNGIEK KGKKKCSVDL AEQYTKLKKV
RRFSDTTVDQ STVLDTLALD LPGPKRRLVE KTAQSSNTSD VESIGAASTA ETTSTSVSRQ
SSLSGPRRRT RTGRSWPLTL QRLKKRRGRT STRTFQPQTS ESGNDNEEKD DCQYEGLDPE
IIDINDQDMH LNHLKSSITN YFGAAGRLAC GEKYRILARR VTLDGKVQYL VEWEGITAS
//