ZFP13_MOUSE
ID ZFP13_MOUSE Reviewed; 512 AA.
AC P10754; Q80WS0; Q8CDD0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger protein 13;
DE Short=Zfp-13;
DE AltName: Full=Zinc finger protein Krox-8;
GN Name=Zfp13; Synonyms=Krox-8, Zfp-13;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 400-481 (ISOFORMS 1/2).
RX PubMed=2452975; DOI=10.1128/mcb.8.3.1319-1326.1988;
RA Chavrier P., Lemaire P., Revelant O., Bravo R., Charnay P.;
RT "Characterization of a mouse multigene family that encodes zinc finger
RT structures.";
RL Mol. Cell. Biol. 8:1319-1326(1988).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10754-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10754-2; Sequence=VSP_016902;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK030240; BAC26860.1; -; mRNA.
DR EMBL; BC052082; AAH52082.1; -; mRNA.
DR EMBL; M19440; AAA39388.1; -; Genomic_DNA.
DR CCDS; CCDS28450.1; -. [P10754-2]
DR CCDS; CCDS89003.1; -. [P10754-1]
DR PIR; E29942; E29942.
DR RefSeq; NP_035877.1; NM_011747.2. [P10754-2]
DR RefSeq; XP_006524272.1; XM_006524209.3.
DR RefSeq; XP_006524273.1; XM_006524210.3. [P10754-1]
DR RefSeq; XP_006524274.1; XM_006524211.3. [P10754-2]
DR AlphaFoldDB; P10754; -.
DR SMR; P10754; -.
DR STRING; 10090.ENSMUSP00000111178; -.
DR iPTMnet; P10754; -.
DR PhosphoSitePlus; P10754; -.
DR PaxDb; P10754; -.
DR PRIDE; P10754; -.
DR ProteomicsDB; 274982; -. [P10754-1]
DR ProteomicsDB; 274983; -. [P10754-2]
DR Antibodypedia; 822; 106 antibodies from 17 providers.
DR DNASU; 22654; -.
DR Ensembl; ENSMUST00000057029; ENSMUSP00000054595; ENSMUSG00000062012. [P10754-2]
DR Ensembl; ENSMUST00000115516; ENSMUSP00000111178; ENSMUSG00000062012. [P10754-1]
DR GeneID; 22654; -.
DR KEGG; mmu:22654; -.
DR UCSC; uc008ash.2; mouse. [P10754-1]
DR UCSC; uc008asi.1; mouse. [P10754-2]
DR CTD; 22654; -.
DR MGI; MGI:99159; Zfp13.
DR VEuPathDB; HostDB:ENSMUSG00000062012; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161865; -.
DR HOGENOM; CLU_002678_9_2_1; -.
DR InParanoid; P10754; -.
DR OMA; EWRGAYT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P10754; -.
DR TreeFam; TF338003; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22654; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Zfp13; mouse.
DR PRO; PR:P10754; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P10754; protein.
DR Bgee; ENSMUSG00000062012; Expressed in embryonic brain and 113 other tissues.
DR ExpressionAtlas; P10754; baseline and differential.
DR Genevisible; P10754; MM.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
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; IDA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI.
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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..512
FT /note="Zinc finger protein 13"
FT /id="PRO_0000047284"
FT DOMAIN 124..196
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 266..288
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..344
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..428
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 84..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016902"
FT CONFLICT 400..401
FT /note="HT -> PH (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56054 MW; 5A56713302C37D07 CRC64;
MSADSQSIAA TENEEKSHEV PGNVQHCGDM LSGQEETVPL GTSQESTHIK AEPEEPHSEG
ASREDRTPGT QRWMSPCPGP KDKGPFLPGG VVPSPWTPVL SRGGRTRERK MAAALLTAWS
QMPVTFEDVA LYLSQEEWGR LDHTQQNFYR DVLQGKNGLA LGAVEMGKVV PALAVATLED
TKSIRTRARW APGEDPKCGQ HVASGPGTKL TRDTGKAGQL KPAPSESRPL KTPEDSGPEK
PSEGEEALKS GEEGLVPDGD TGKKTYKCEQ CGKGFSWHSH LVTHRRTHTG EKPYTCTDCG
KRFGRSSHLI QHQIIHTGEK PYTCPSCWKS FSHHSTLIQH QRIHTGEKPY VCDRCAKRFT
RRSDLVTHQG THTGAKPHKC PICSKCFTQS SALVTHQRTH TGVKPYPCPE CGKCFSQRSN
LIAHNRTHTG EKPYHCLDCG KSFSHSSHLT AHQRTHRGVR PYSCPLCGKS FSRRSNLHRH
EKIHTTGPKA LAMLMLGAAA AGALTAPPPA ST
