ZN394_MOUSE
ID ZN394_MOUSE Reviewed; 521 AA.
AC Q9Z1D9; B9EIZ4; Q3U4Z1; Q9CYV9; Q9CZG8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein 394;
DE AltName: Full=Zinc finger protein 94;
DE Short=Zfp-94;
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 14;
GN Name=Znf394; Synonyms=Zfp94, Zfp99, Zkscan14;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12860387; DOI=10.1016/s0014-5793(03)00669-0;
RA Weissig H., Narisawa S., Sikstrom C., Olsson P.G., McCarrey J.R.,
RA Tsonis P.A., Del Rio-Tsonis K., Millan J.L.;
RT "Three novel spermatogenesis-specific zinc finger genes.";
RL FEBS Lett. 547:61-68(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in testis.
CC {ECO:0000269|PubMed:12860387}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28368.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U62906; AAD00102.1; -; mRNA.
DR EMBL; AK012630; BAB28368.1; ALT_FRAME; mRNA.
DR EMBL; AK013258; BAB28752.1; -; mRNA.
DR EMBL; AK153972; BAE32289.1; -; mRNA.
DR EMBL; CH466529; EDL18989.1; -; Genomic_DNA.
DR EMBL; BC141244; AAI41245.1; -; mRNA.
DR CCDS; CCDS19860.1; -.
DR RefSeq; NP_075811.2; NM_023322.2.
DR AlphaFoldDB; Q9Z1D9; -.
DR SMR; Q9Z1D9; -.
DR BioGRID; 212036; 1.
DR IntAct; Q9Z1D9; 1.
DR STRING; 10090.ENSMUSP00000031632; -.
DR iPTMnet; Q9Z1D9; -.
DR PhosphoSitePlus; Q9Z1D9; -.
DR jPOST; Q9Z1D9; -.
DR PaxDb; Q9Z1D9; -.
DR PRIDE; Q9Z1D9; -.
DR ProteomicsDB; 302082; -.
DR Antibodypedia; 16184; 230 antibodies from 25 providers.
DR DNASU; 67235; -.
DR Ensembl; ENSMUST00000031632; ENSMUSP00000031632; ENSMUSG00000029627.
DR GeneID; 67235; -.
DR KEGG; mmu:67235; -.
DR UCSC; uc009amm.1; mouse.
DR CTD; 67235; -.
DR MGI; MGI:1914485; Zkscan14.
DR VEuPathDB; HostDB:ENSMUSG00000029627; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162347; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q9Z1D9; -.
DR OMA; EGDSKNN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Z1D9; -.
DR TreeFam; TF338304; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 67235; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Zkscan14; mouse.
DR PRO; PR:Q9Z1D9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z1D9; protein.
DR Bgee; ENSMUSG00000029627; Expressed in primary oocyte and 234 other tissues.
DR ExpressionAtlas; Q9Z1D9; baseline and differential.
DR Genevisible; Q9Z1D9; MM.
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: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 CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..521
FT /note="Zinc finger protein 394"
FT /id="PRO_0000047558"
FT DOMAIN 38..133
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 135..196
FT /note="KRAB"
FT ZN_FING 327..349
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..432
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CONFLICT 112
FT /note="G -> R (in Ref. 1; AAD00102)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="LA -> W (in Ref. 1; AAD00102)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..199
FT /note="AEPQAW -> QSHRSC (in Ref. 1; AAD00102)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="K -> R (in Ref. 2; BAB28368/BAB28752)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..486
FT /note="HQR -> NQS (in Ref. 2; BAE32289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59038 MW; BFA0C7F21761A2EB CRC64;
MAAGSGVVPP PLGAGLCTVK VEEDSPGNQE SSGSGDWQNP ETSRKQFRQL RYQEVAGPEE
ALSRLWELCR RWLRPELLSK EQIMELLVLE QFLTILPQEL QAYVRDHSPE SGEEAAALAR
TLQRALDRAS PQGFMTFKDV AESLTWEEWE QLAAARKGFC EESTKDAGST VVPGLETRTV
NTDVILKQEI LKEAEPQAWL QEVSQGMVPA LTKCGDPSED WEEKLPKAAV LLQLQGSEEQ
GRTAIPLLIG VSREERDSKN NESENSGSSV LGQHIQTAEG LGTNSQCGDD HKQGFHVKCH
SVKPHSSVDS AVGLLETQRQ FQEDKPYKCD SCEKGFRQRS DLFKHQRIHT GEKPYQCQEC
GKRFSQSAAL VKHQRTHTGE KPYACPECGE CFRQSSHLSR HQRTHASEKY YKCEECGEIV
HVSSLFRHQR LHRGERPYKC GDCEKSFRQR SDLFKHQRTH TGEKPYACVV CGRRFSQSAT
LIKHQRTHTG EKPYKCFQCG ERFRQSTHLV RHQRIHQNSV S
