ZN667_RAT
ID ZN667_RAT Reviewed; 608 AA.
AC Q5MYW4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein 667;
DE AltName: Full=Myocardial ischemic preconditioning up-regulated protein 1;
GN Name=Znf667; Synonyms=Mip1, Mipu1, Zfp667;
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=Wistar;
RA Yuan C., Zhang H., Liu Y., Wang Q., Xiao X.;
RT "Cloning and characterization of a new gene Mip1 up-regulated during
RT myocardial ischemia-reperfusion.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:231-236(2004).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY221750; AAO67708.1; -; mRNA.
DR RefSeq; NP_001008557.1; NM_001008557.1.
DR RefSeq; XP_006228251.1; XM_006228189.3.
DR AlphaFoldDB; Q5MYW4; -.
DR SMR; Q5MYW4; -.
DR STRING; 10116.ENSRNOP00000061115; -.
DR Ensembl; ENSRNOT00000063956; ENSRNOP00000061115; ENSRNOG00000033906.
DR GeneID; 308326; -.
DR KEGG; rno:308326; -.
DR UCSC; RGD:1359114; rat.
DR CTD; 384763; -.
DR RGD; 1359114; Zfp667.
DR GeneTree; ENSGT00390000021477; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q5MYW4; -.
DR OMA; HQNSHSE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5MYW4; -.
DR TreeFam; TF341817; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q5MYW4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000033906; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q5MYW4; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..608
FT /note="Zinc finger protein 667"
FT /id="PRO_0000251899"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 144..166
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 172..194
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..275
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..603
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 75..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 70038 MW; 99BB8EB373514ED5 CRC64;
MPAARGKSKS KAPVTFGDLA IYFSQEEWEW LSPNQKDLYE DVMLENYHNL VSVGLACRRP
NIIALLEKGK APWMVEPSRK RRGPELGSKD ETKKLPPSQC NKSGPSICKK PDSSQQKVPT
EKAKHNKNAV PRKNKKGHSG KKSLKCNSCG KTFFRSLSLK LHQGFHTGER SYECSTCGQV
FRQILSLILH QRVHTQNKSY ECDKCGDIFN KKLTLMIHRR SHNGKENFHH EKTSDSCPSL
SPHHNNHAID SIHQCRKCGK VFSRMSSLLL HKKIHNRKRI QKYSACGRGF KKKPVLVHKR
ICIGKKTHEN KALIQSLRQR TYQSENPFTC RKCRKSFSRI SALMLHQRAH TSGNPYKCDK
CQKDFGRLST LILHLRIHSG EKQFKCNKCE KVCNRLSSFI QHKKIHKRKK KLIECKECGK
MFGGMKNLKV HLNIHSEEKP FKCNKCSKVF GRQSFLSEHQ RIHTGEKPYQ CEECGKAFSH
RISLTRHKRI HSEDRPYECD LCGKAFSQSA HLAQHERIHT GEKPYACKIC KKSFTQRISL
ILHERSHTGE KPYECNECGK AFSSGSDLIR HQRSHSSEKP YECSKCGKAY SRSSSLIRHQ
SIHSEEMS
