ZFP60_MOUSE
ID ZFP60_MOUSE Reviewed; 707 AA.
AC P16374; Q61135;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Zinc finger protein 60;
DE Short=Zfp-60;
DE AltName: Full=Zinc finger protein Mfg-3;
GN Name=Zfp60; Synonyms=Mfg3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8674531; DOI=10.1016/0014-5793(96)00474-7;
RA Perez M., Rompato G., Corbi N., de Gregorio L., Dragani T.A.,
RA Passananti C.;
RT "Zfp60, a mouse zinc finger gene expressed transiently during in vitro
RT muscle differentiation.";
RL FEBS Lett. 387:117-121(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-629.
RC STRAIN=CD-1; TISSUE=Skeletal muscle;
RX PubMed=2512579; DOI=10.1073/pnas.86.23.9417;
RA Passananti C., Felsani A., Caruso M., Amati P.;
RT "Mouse genes coding for 'zinc-finger'-containing proteins: characterization
RT and expression in differentiated cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9417-9421(1989).
CC -!- FUNCTION: May have a role during differentiation processes.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed widely and evenly in most adult mouse
CC tissues.
CC -!- DEVELOPMENTAL STAGE: Expression is positively regulated upon
CC differentiation and is not related to the cell cycle.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U48721; AAB06876.1; -; Genomic_DNA.
DR EMBL; M28515; AAA39533.1; -; mRNA.
DR PIR; C39240; C39240.
DR PIR; S68858; S68858.
DR AlphaFoldDB; P16374; -.
DR SMR; P16374; -.
DR STRING; 10090.ENSMUSP00000103973; -.
DR iPTMnet; P16374; -.
DR PhosphoSitePlus; P16374; -.
DR MaxQB; P16374; -.
DR PaxDb; P16374; -.
DR PRIDE; P16374; -.
DR ProteomicsDB; 299549; -.
DR MGI; MGI:99207; Zfp60.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P16374; -.
DR PhylomeDB; P16374; -.
DR PRO; PR:P16374; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P16374; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..707
FT /note="Zinc finger protein 60"
FT /id="PRO_0000047304"
FT DOMAIN 14..86
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 173..195
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 201..223
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..282
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 456..478
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 512..534
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 540..562
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 596..618
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 624..646
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 652..674
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 680..702
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ SEQUENCE 707 AA; 82274 MW; 7E0E404C4F0911DE CRC64;
MANSSSQHMV CGSVTFRDVA VDFSQEEWAC LDATQKVLYR NIMLETYSNL VAVVGRCIPK
PDLIVLLEPE KEPWMAVKKE TGRPSQGLET GFEAENRSPK NHVYNKKLPK QTIQQLSKTS
DVQGVSVSNG PGYSVIKEPQ NYQEGDANRN ITNKKEMSTY TSKTLAHNKE KPYKCKDCGK
CFGCKSNLHQ HESIHTGEKP YECKDCGKTF RLPQMLSRHQ KSHSDERPFE CNICGKSFHL
PTLLQYHKNI HTGLKPFECE ECGKSFKSFN RISTLFQHRT IHAGMKPYKC NVCGKAFNRR
SNLLQHQKIH SEDRPFHCKV CGKAFTVLAQ LTRHENIHTE DKSFECKQCG KIFSNGSYLL
RHYDTHTNEK PFECNICGKA FRLHLYLSEH QKTHTDEKPF KCKLCESAFR RKYQLSEHQR
IHTDGKPYQC KDCWEFFRRR SNFIEHQSIH TGKKPFECKD CGKVFRLNIH LIRHQRFHSD
EKPFECKECG KAFHFSSQLN NHKTSHTGQT PFECKECGKS FKRVSSLVEH RIIHSGVKPY
KCNACGRAFN RRSNLMQHEK IHSDERPFEC KDCGKAFTVL AQLTRHQTIH NGKKSYECEQ
CGSAFRLPYQ LTQHQRIHYD VKPFQCKECG RAFVRSTGLR IHERIHTGEK PFQCKECGEA
FQYHYQFLGH FRIHTGKNPY ECSECGKYFT YGRDLKVHQS IHNLEKP
