ID G9K718_MUSPF Unreviewed; 785 AA.
AC G9K718;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Lysine-specific demethylase 5C {ECO:0000313|EMBL:AES00693.1};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES00693.1};
RN [1] {ECO:0000313|EMBL:AES00693.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES00693.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
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DR EMBL; JP012095; AES00693.1; -; mRNA.
DR AlphaFoldDB; G9K718; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF43; LYSINE-SPECIFIC DEMETHYLASE 5C; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:AES00693.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AES00693.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..65
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 616..681
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 744..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES00693.1"
FT NON_TER 785
FT /evidence="ECO:0000313|EMBL:AES00693.1"
SQ SEQUENCE 785 AA; 87470 MW; 4FFEA8DCE10C5395 CRC64;
PTPSCPMVYQ WSAVVRTNQC AGEFVITFPR AYHSGFNQGY NFAEAVNFCT ADWLPAGRQC
IEHYRRLRRY CVFSHEELIC KMAACPEKLD LNLAAAVHKE MFIMVQEERR LRKALLEKGI
TEAEREAFEL LPDDERQCIK CKTTCFLSAL ACYDCPDGLV CLSHINDLCK CSSSRQYLRY
RYTLDELPAM LHKLKVRAES FDTWANKVRV ALEVEDGRKR SLEELRALES EARERRFPNS
ELLQRLKNCL SEAEACVSQA LGLVSGQEAG PHRAAGLQMT LAELRAFLDQ MNNLPCAMHQ
IGDVKGILEQ VEAYQAEVRE ALASLPSSPG LLQSLLERGQ QLGVEVPEAQ QLQRQVEQAR
WLDEVKRTLA PSARRGTLAV MRGLLVAGAS VAPSPAVDKA RAELQELLTI AERWEEKAHL
CLEARQKHPP ATLEAIIHEA ENIPVHLPNI QALKEALAKA RAWIADVDEI QNGDHYPCLD
DLEGLVAVGR DLPVGLEELR QLELQVLTAH SWREKASKTF LKKNSCYTLL EVLCPCADAG
SDSTKRSRWM EKELGLYKSD TELLGLSAQD LRDPGSVIVA FKEGEQKEKE GILQLRRTNS
AKPSPLASSA TASSATSVCV CGQVPAGGGA LQCDLCQDWF HGRCVSVPRL LSSPRPSLTT
SPLLAWWEWD TKFLCPLCMR SRRPRLETIL ALLVALQRLP VRLPEGEALQ CLTERAINWQ
GRARQALASE DVTALLGRLA ELRQRLQAEP KPEEPPTYPS APASDPLREG SGKDMPKVPG
LLENG
//
