ZSC21_MOUSE
ID ZSC21_MOUSE Reviewed; 555 AA.
AC Q07231; Q921V2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 21;
DE AltName: Full=CtFIN51;
DE AltName: Full=Transcription factor RU49;
DE AltName: Full=Zinc finger protein 38;
DE Short=Zfp-38;
GN Name=Zscan21; Synonyms=Zfp-38, Zfp38, Zipro1, Znf38;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=BTBRTF; TISSUE=Spermatocyte;
RX PubMed=1397691; DOI=10.1016/0012-1606(92)90120-6;
RA Noce T., Fujiwara Y., Sezaki M., Fujimoto H., Higashinakagawa T.;
RT "Expression of a mouse zinc finger protein gene in both spermatocytes and
RT oocytes during meiosis.";
RL Dev. Biol. 153:356-367(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=1284028; DOI=10.1016/0925-4773(92)90040-q;
RA Chowdhury K.;
RT "The ubiquitous transactivator Zfp-38 is upregulated during spermatogenesis
RT with differential transcription.";
RL Mech. Dev. 39:129-142(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8625807; DOI=10.1242/dev.122.2.555;
RA Yang X.W., Zhong R., Heintz N.;
RT "Granule cell specification in the developing mouse brain as defined by
RT expression of the zinc finger transcription factor RU49.";
RL Development 122:555-566(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27492080; DOI=10.1530/rep-16-0225;
RA Yan Z., Fan D., Meng Q., Yang J., Zhao W., Guo F., Song D., Guo R., Sun K.,
RA Wang J.;
RT "Transcription factor ZFP38 is essential for meiosis prophase I in male
RT mice.";
RL Reproduction 152:431-437(2016).
CC -!- FUNCTION: Strong transcriptional activator (PubMed:1284028). Plays an
CC important role in spermatogenesis; essential for the progression of
CC meiotic prophase I in spermatocytes (PubMed:27492080).
CC {ECO:0000269|PubMed:1284028, ECO:0000269|PubMed:27492080}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1397691}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the spermatocytes and
CC spermatids of adult testes. It is also present at lower levels in the
CC ovary, brain, spleen, embryo and fetus. {ECO:0000269|PubMed:1284028,
CC ECO:0000269|PubMed:1397691, ECO:0000269|PubMed:27492080}.
CC -!- DEVELOPMENTAL STAGE: First detected between 2 and 3 weeks after birth,
CC in parallel with the onset and progression of meiosis. It is expressed
CC during oogenesis from the pachytene stage of meiotic prophase through
CC to postmeiotic cells. Expression in testis starts from postnatal day 7
CC (PND7) and expression remains constant until PND28 (PubMed:27492080).
CC {ECO:0000269|PubMed:1397691, ECO:0000269|PubMed:27492080}.
CC -!- DISRUPTION PHENOTYPE: Male germ-cell-specific conditional knockout
CC results in complete male infertility and meiotic arrest in
CC spermatocytes (PubMed:27492080). Spermatocytes show impaired
CC chromosomal synapsis and DNA double-strand breaks (DSB) repair and a
CC significantly reduced expression of DSB repair-associated genes
CC (PubMed:27492080). {ECO:0000269|PubMed:27492080}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; D10630; BAA01480.1; -; mRNA.
DR EMBL; X63747; CAA45280.1; -; mRNA.
DR EMBL; U41671; AAB03786.1; -; mRNA.
DR EMBL; AK146875; BAE27498.1; -; mRNA.
DR EMBL; CH466529; EDL19218.1; -; Genomic_DNA.
DR EMBL; BC010591; AAH10591.1; -; mRNA.
DR CCDS; CCDS19790.1; -.
DR PIR; A56560; A56560.
DR RefSeq; NP_001038168.1; NM_001044703.2.
DR RefSeq; NP_001038169.1; NM_001044704.2.
DR RefSeq; NP_001038170.1; NM_001044705.2.
DR RefSeq; NP_035887.2; NM_011757.3.
DR RefSeq; XP_011239244.1; XM_011240942.1.
DR AlphaFoldDB; Q07231; -.
DR SMR; Q07231; -.
DR BioGRID; 204660; 28.
DR IntAct; Q07231; 1.
DR STRING; 10090.ENSMUSP00000106584; -.
DR iPTMnet; Q07231; -.
DR PhosphoSitePlus; Q07231; -.
DR EPD; Q07231; -.
DR MaxQB; Q07231; -.
DR PaxDb; Q07231; -.
DR PeptideAtlas; Q07231; -.
DR PRIDE; Q07231; -.
DR ProteomicsDB; 275246; -.
DR Antibodypedia; 16310; 416 antibodies from 30 providers.
DR DNASU; 22697; -.
DR Ensembl; ENSMUST00000062350; ENSMUSP00000053430; ENSMUSG00000037017.
DR Ensembl; ENSMUST00000080732; ENSMUSP00000079557; ENSMUSG00000037017.
DR Ensembl; ENSMUST00000110959; ENSMUSP00000106584; ENSMUSG00000037017.
DR Ensembl; ENSMUST00000110960; ENSMUSP00000106585; ENSMUSG00000037017.
DR Ensembl; ENSMUST00000110961; ENSMUSP00000106586; ENSMUSG00000037017.
DR GeneID; 22697; -.
DR KEGG; mmu:22697; -.
DR UCSC; uc009aem.2; mouse.
DR CTD; 7589; -.
DR MGI; MGI:99182; Zscan21.
DR VEuPathDB; HostDB:ENSMUSG00000037017; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161607; -.
DR HOGENOM; CLU_002678_49_4_1; -.
DR InParanoid; Q07231; -.
DR OMA; WEPLYIQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q07231; -.
DR TreeFam; TF338304; -.
DR BioGRID-ORCS; 22697; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q07231; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q07231; protein.
DR Bgee; ENSMUSG00000037017; Expressed in ear vesicle and 260 other tissues.
DR ExpressionAtlas; Q07231; baseline and differential.
DR Genevisible; Q07231; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
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 Activator; Developmental protein; Differentiation; DNA-binding;
KW Isopeptide bond; Meiosis; Metal-binding; Nucleus; Oogenesis;
KW Reference proteome; Repeat; Spermatogenesis; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..555
FT /note="Zinc finger and SCAN domain-containing protein 21"
FT /id="PRO_0000047296"
FT REPEAT 18..56
FT /note="1-1"
FT REPEAT 57..95
FT /note="1-2"
FT REPEAT 96..134
FT /note="1-3"
FT DOMAIN 122..204
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 359..381
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..409
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 415..436
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 526..548
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 18..134
FT /note="3 X 39 AA approximate tandem repeats"
FT REGION 102..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT CONFLICT 193
FT /note="A -> T (in Ref. 1; BAA01480)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="N -> S (in Ref. 3; AAB03786)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="S -> P (in Ref. 3; AAB03786)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..347
FT /note="ASLQDTGSRKGAEP -> PLFKTQVPGRGRA (in Ref. 3;
FT AAB03786)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="NL -> KV (in Ref. 3; AAB03786)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="S -> E (in Ref. 3; AAB03786)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="E -> K (in Ref. 2; CAA45280)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="F -> L (in Ref. 2; CAA45280)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="S -> N (in Ref. 2; CAA45280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 63012 MW; 39321721BBE3687D CRC64;
MTKVVGMATV LGPRPPQESM GPSPIKVEED EEKDKCCPTL ELSHKHFRQS GNQDTLEPMG
PSTIKAEEDE SKDKCRPNLE ISRKSFKQFG YQDTLEQLGP STIKAEEDDE KDKGHPSPEI
SRQRFRQFGY HDTPGPREAL SQLRVLCCEW LQPEIHTKEQ ILELLVLEQF LTILPRELQT
WVQQHCPESA EEAVTLLEDL EQELDEPGLQ VSSPPNEQKQ SWEKMSTSGT AMESLSSTET
QHVDASPKYE FWGPLYIQET GEEEVFTQDP RKRQGFKSNP QKEDSADEHR SSEEESHADG
LKRTVIPMIP ANKYGSRSER QWANNLERER GTKASLQDTG SRKGAEPAST RPAPGEKRYI
CAECGKAFSN SSNLTKHRRT HTGEKPYVCT KCGKAFSHSS NLTLHYRTHL VDRPYDCKCG
KAFGQSSDLL KHQRMHTEEA PYQCKDCGKA FSGKGSLIRH YRIHTGEKPY QCNECGKSFS
QHAGLSSHQR LHTGEKPYKC KECGKAFNHS SNFNKHHRIH TGEKPYWCSH CGKTFCSKSN
LSKHQRVHTG EGEVQ
