ZN322_MOUSE
ID ZN322_MOUSE Reviewed; 410 AA.
AC Q8BZ89; Q8K0A0; Q91W42;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein 322;
DE AltName: Full=Zinc finger protein 322A;
GN Name=Znf322; Synonyms=Zfp322a, Znf322a;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Kidney;
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 [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=16325481; DOI=10.1016/j.modgep.2005.06.003;
RA Yoshikawa T., Piao Y., Zhong J., Matoba R., Carter M.G., Wang Y.,
RA Goldberg I., Ko M.S.;
RT "High-throughput screen for genes predominantly expressed in the ICM of
RT mouse blastocysts by whole mount in situ hybridization.";
RL Gene Expr. Patterns 6:213-224(2006).
RN [5]
RP FUNCTION, INTERACTION WITH POU5F1, AND SUBCELLULAR LOCATION.
RX PubMed=24550733; DOI=10.1371/journal.pgen.1004038;
RA Ma H., Ng H.M., Teh X., Li H., Lee Y.H., Chong Y.M., Loh Y.H.,
RA Collins J.J., Feng B., Yang H., Wu Q.;
RT "Zfp322a Regulates mouse ES cell pluripotency and enhances reprogramming
RT efficiency.";
RL PLoS Genet. 10:E1004038-E1004038(2014).
CC -!- FUNCTION: Transcriptional activator. Important for maintenance of
CC pluripotency in embryonic stem cells. Binds directly to the POU5F1
CC distal enhancer and the NANOG proximal promoter, and enhances
CC expression of both genes. Can also bind to numerous other gene
CC promoters and regulates expression of many other pluripotency factors,
CC either directly or indirectly. Promotes inhibition of MAPK signaling
CC during embryonic stem cell differentiation.
CC {ECO:0000269|PubMed:24550733}.
CC -!- SUBUNIT: Interacts with POU5F1. {ECO:0000269|PubMed:24550733}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550733}. Cytoplasm
CC {ECO:0000269|PubMed:24550733}. Note=Mainly found in the nucleus.
CC {ECO:0000269|PubMed:24550733}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the inner cell mass of the blastocyst
CC during preimplantation stage embryonic development.
CC {ECO:0000269|PubMed:16325481}.
CC -!- MISCELLANEOUS: Significantly enhances POU5F1/OCT4-SOX2-KLF4-MYC (OSKM)
CC mediated reprogramming of mouse embryonic fibroblasts into induced
CC pluripotent stem cells, and can also substitute for SOX2 in this
CC process. {ECO:0000269|PubMed:24550733}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32268.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK036302; BAC29377.1; -; mRNA.
DR EMBL; AK162608; BAE36986.1; -; mRNA.
DR EMBL; AK170525; BAE41858.1; -; mRNA.
DR EMBL; AL669819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017143; AAH17143.1; -; mRNA.
DR EMBL; BC032268; AAH32268.1; ALT_INIT; mRNA.
DR EMBL; BC043711; AAH43711.1; -; mRNA.
DR CCDS; CCDS26337.1; -.
DR RefSeq; NP_001104577.1; NM_001111107.2.
DR RefSeq; NP_001273084.1; NM_001286155.1.
DR RefSeq; NP_001273085.1; NM_001286156.1.
DR RefSeq; NP_766174.1; NM_172586.4.
DR AlphaFoldDB; Q8BZ89; -.
DR SMR; Q8BZ89; -.
DR STRING; 10090.ENSMUSP00000061524; -.
DR iPTMnet; Q8BZ89; -.
DR PhosphoSitePlus; Q8BZ89; -.
DR PaxDb; Q8BZ89; -.
DR PRIDE; Q8BZ89; -.
DR ProteomicsDB; 275281; -.
DR Antibodypedia; 11103; 122 antibodies from 19 providers.
DR DNASU; 218100; -.
DR Ensembl; ENSMUST00000050101; ENSMUSP00000061524; ENSMUSG00000046351.
DR GeneID; 218100; -.
DR KEGG; mmu:218100; -.
DR UCSC; uc007ptn.3; mouse.
DR CTD; 218100; -.
DR MGI; MGI:2442566; Zfp322a.
DR VEuPathDB; HostDB:ENSMUSG00000046351; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162956; -.
DR HOGENOM; CLU_002678_44_10_1; -.
DR InParanoid; Q8BZ89; -.
DR OMA; MHAGKKF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BZ89; -.
DR TreeFam; TF338126; -.
DR BioGRID-ORCS; 218100; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Zfp322a; mouse.
DR PRO; PR:Q8BZ89; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BZ89; protein.
DR Bgee; ENSMUSG00000046351; Expressed in embryonic post-anal tail and 269 other tissues.
DR ExpressionAtlas; Q8BZ89; baseline and differential.
DR Genevisible; Q8BZ89; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IDA:UniProtKB.
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; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..410
FT /note="Zinc finger protein 322"
FT /id="PRO_0000047531"
FT ZN_FING 81..103
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 109..131
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 137..159
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 165..187
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..215
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 221..243
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..271
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 277..299
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 303..325
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..383
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6U7Q0"
FT CONFLICT 1
FT /note="M -> V (in Ref. 3; AAH32268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 48492 MW; 27E5668CC383FAA7 CRC64;
MENHLGENHR RCTLQKRNVT RELKKGKHTM YALKRVKKIY IRVHEITQID NQTYQCLERE
QNFCENLARM CERTYTEEKP YRCDMCEKTF IQSSDLISHQ RIHNYEKPYK CSKCEKSFWH
HLALSGHQRT HAGKKFYTCD ICGKNFGQSS DLLVHQRSHT GEKPYLCNEC DKCFSRSTNL
IRHRRTHTGE KPFKCLECEK AFSGKSDLIS HQRTHTGERP YKCNKCEKSY RHRSAFIVHK
RVHTGEKPYK CGACEKCFGQ KSDLIVHQRV HTGEKPYKCL ECMRSFTRSA NLIRHQATHT
HTFKCLEYEK SFNCSSDFIV HQRIHMEEKP HQWSMCESDF LLGMDFVAQQ KMRAQTEELH
YKYSVCDKTF HHSSALLQHQ TVHIDDEYIC NMSEKGLDLS SHASETSRVS
