ID   ZFP37_RAT               Reviewed;         601 AA.
AC   O88553;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Zinc finger protein 37;
DE            Short=Zfp-37;
GN   Name=Zfp37;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9772206; DOI=10.1006/taap.1998.8478;
RA   Vanden Heuvel J.P., Holden P., Tugwood J., Ingle C., Yen W., Galjart N.,
RA   Greenlee W.F.;
RT   "Identification of a novel peroxisome proliferator responsive cDNA isolated
RT   from rat hepatocytes as the zinc-finger protein ZFP-37.";
RL   Toxicol. Appl. Pharmacol. 152:107-118(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3 AND SER-9, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in testes, brain, kidney, spleen, thymus,
CC       lung, and at low levels in liver.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF072439; AAC24590.1; -; mRNA.
DR   AlphaFoldDB; O88553; -.
DR   SMR; O88553; -.
DR   STRING; 10116.ENSRNOP00000018209; -.
DR   iPTMnet; O88553; -.
DR   PhosphoSitePlus; O88553; -.
DR   PRIDE; O88553; -.
DR   UCSC; RGD:620723; rat.
DR   RGD; 620723; Zfp37.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; O88553; -.
DR   PhylomeDB; O88553; -.
DR   PRO; PR:O88553; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR   GO; GO:0008283; P:cell population proliferation; IEP:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; 11.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..601
FT                   /note="Zinc finger protein 37"
FT                   /id="PRO_0000047295"
FT   DOMAIN          1..70
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         257..279
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         285..303
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         314..337
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         343..365
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         371..393
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         399..421
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         427..449
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         455..477
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         483..505
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         511..533
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         539..561
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         570..592
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          30..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   601 AA;  68098 MW;  1CFCB55B595B7C9E CRC64;
     MATPEPAESD AEWEQLEPGQ RNLYKDTKLE TCSNPASMGN QDPKQGLVSK LDGEEERWSS
     VRANKNSSSS LHRLKKTGTS AKVQQDGAQT EGKQKFQRKL TSEVTFRKKS SNSKKSSECT
     LLEKKNVHSK HDPSEKRLHK SNLYGKNLNQ NLDLPSQIKI SAKKKPDTAN EYRKSLSHSA
     SDVNRDEIST RKKCDKSPNN KLFGKGDKNQ TGKKCEKVCR HTASHTKEDK IHTGEKRKSP
     CRSPSKSDKA PGSGKPYECN QCGKVLSHKQ GLLDHQRTHA GEEPYECYEC GIAFSQKSHL
     VVHQKTPTGE KAPYECVQCG KAHGHKHALT DHLRISHTGE KPYKCNECGK TFRHSSNLMQ
     HIRSHTGEKP YECKECGKSF RYNSSFTEHV RTHTGEIPYE CNECGKAFKY GSSLTKHMRI
     HTGEKPFECT ECGKTFSKKS HLVIHQRTHT KEKPYKCKEC GKAFGHSSSL TYHMRTHTGD
     CPFECNKCGK AFKQIEGLTQ HQRVHTGEKP YECVECGKAF SQKSHLIVHQ RTHTGEKPFE
     CYECGKAFNA KSQLVIHQRS HTGEKPYKPY ECVECGKAFK QNASLTRHMK THSEEQSQEE
     D