OSR2_MOUSE
ID OSR2_MOUSE Reviewed; 312 AA.
AC Q91ZD1; Q8BPV6; Q91V54;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein odd-skipped-related 2;
GN Name=Osr2;
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] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Mammary gland;
RX PubMed=11520675; DOI=10.1016/s0925-4773(01)00457-9;
RA Lan Y., Kingsley P.D., Cho E.-S., Jiang R.;
RT "Osr2, a new mouse gene related to Drosophila odd-skipped, exhibits dynamic
RT expression patterns during craniofacial, limb, and kidney development.";
RL Mech. Dev. 107:175-179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Jiang R., Cho E.-S., Lan Y.;
RT "Alternative splicing of the mouse Osr2 mRNA produces two protein isoforms
RT differing in the zinc finger region.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP STRUCTURE BY NMR OF 162-252 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of three ZF-C2H2 domains from mouse protein odd-
RT skipped-related 2 splicing isoform 2.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=OSR2A;
CC IsoId=Q91ZD1-1; Sequence=Displayed;
CC Name=2; Synonyms=OSR2B;
CC IsoId=Q91ZD1-2; Sequence=VSP_017122;
CC -!- DEVELOPMENTAL STAGE: First detected at 9.25 dpc, specifically in the
CC mesonephric vesicles. By 10.0 dpc expression is also observed in the
CC rostro-lateral mandibular mesenchyme immediately adjacent to the
CC maxillary processes. In the developing limb buds it is expressed in a
CC unique mesenchymal domain and the onset of the expression follows a
CC distinct dorsal to ventral developmental time sequence beginning in the
CC forelimb and then in the hindlimb. It exhibits a dynamic expression
CC pattern during craniofacial development, in the mandibular and
CC maxillary processes as well as the developing palate. It is also
CC expressed at sites of epithelial-mesenchymal interactions during tooth
CC and kidney development. {ECO:0000269|PubMed:11520675}.
CC -!- SIMILARITY: Belongs to the Odd C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF370121; AAL07364.1; -; mRNA.
DR EMBL; AY038074; AAK74068.1; -; mRNA.
DR EMBL; AK052147; BAC34859.1; -; mRNA.
DR EMBL; BC013504; AAH13504.1; -; mRNA.
DR CCDS; CCDS27422.1; -. [Q91ZD1-2]
DR CCDS; CCDS88748.1; -. [Q91ZD1-1]
DR RefSeq; NP_473390.1; NM_054049.2. [Q91ZD1-2]
DR RefSeq; XP_006520076.1; XM_006520013.3.
DR PDB; 2EE8; NMR; -; A=162-252.
DR PDBsum; 2EE8; -.
DR AlphaFoldDB; Q91ZD1; -.
DR SMR; Q91ZD1; -.
DR IntAct; Q91ZD1; 3.
DR STRING; 10090.ENSMUSP00000022952; -.
DR iPTMnet; Q91ZD1; -.
DR PhosphoSitePlus; Q91ZD1; -.
DR PaxDb; Q91ZD1; -.
DR PRIDE; Q91ZD1; -.
DR ProteomicsDB; 295477; -. [Q91ZD1-1]
DR ProteomicsDB; 295478; -. [Q91ZD1-2]
DR Antibodypedia; 26083; 145 antibodies from 29 providers.
DR DNASU; 107587; -.
DR Ensembl; ENSMUST00000022952; ENSMUSP00000022952; ENSMUSG00000022330. [Q91ZD1-2]
DR Ensembl; ENSMUST00000228152; ENSMUSP00000154286; ENSMUSG00000022330. [Q91ZD1-1]
DR GeneID; 107587; -.
DR KEGG; mmu:107587; -.
DR UCSC; uc007vma.1; mouse. [Q91ZD1-2]
DR UCSC; uc007vmb.1; mouse. [Q91ZD1-1]
DR CTD; 116039; -.
DR MGI; MGI:1930813; Osr2.
DR VEuPathDB; HostDB:ENSMUSG00000022330; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160530; -.
DR HOGENOM; CLU_051854_0_0_1; -.
DR InParanoid; Q91ZD1; -.
DR OMA; HTPHQDY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q91ZD1; -.
DR TreeFam; TF350876; -.
DR BioGRID-ORCS; 107587; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Osr2; mouse.
DR EvolutionaryTrace; Q91ZD1; -.
DR PRO; PR:Q91ZD1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91ZD1; protein.
DR Bgee; ENSMUSG00000022330; Expressed in undifferentiated genital tubercle and 158 other tissues.
DR Genevisible; Q91ZD1; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IGI:BHF-UCL.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:BHF-UCL.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEP:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:BHF-UCL.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IGI:BHF-UCL.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IGI:BHF-UCL.
DR GO; GO:0072498; P:embryonic skeletal joint development; IGI:BHF-UCL.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:BHF-UCL.
DR GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IGI:BHF-UCL.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0060322; P:head development; IMP:BHF-UCL.
DR GO; GO:0001823; P:mesonephros development; IEP:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IEP:UniProtKB.
DR GO; GO:0042474; P:middle ear morphogenesis; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0042476; P:odontogenesis; IMP:UniProtKB.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IGI:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0001655; P:urogenital system development; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..312
FT /note="Protein odd-skipped-related 2"
FT /id="PRO_0000047008"
FT ZN_FING 172..194
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 253..312
FT /note="ESPHKCPTCGRTFNQRSNLKTHLLTHTDIKPYSCEQCGKVFRRNCDLRRHSL
FT THTPRQNF -> TSSPTAASSAAKCSGETAICGGTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11520675,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_017122"
FT CONFLICT 142
FT /note="G -> W (in Ref. 3; BAC34859)"
FT /evidence="ECO:0000305"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2EE8"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:2EE8"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2EE8"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2EE8"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2EE8"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2EE8"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2EE8"
SQ SEQUENCE 312 AA; 35454 MW; 33B4B92B1FA11D20 CRC64;
MGSKALPAPI PLHPSLQLTN YSFLQAVNTF PAAVDHLQGL YGLSAVQTMH MNHWTLGYPS
VHEITRSTIT EMAAAQGLVD ARFPFPSLPF ATHLFHPKQG AIAHVLPALH KDRPRFDFAN
LAVAATQEDP PKMGDLSKLS PGLGSPISGL SKLNPDRKPS RGRLPSKTKK EFICKFCGRH
FTKSYNLLIH ERTHTDERPY TCDICHKAFR RQDHLRDHRY IHSKEKPFKC QECGKGFCQS
RTLAVHKTLH MQESPHKCPT CGRTFNQRSN LKTHLLTHTD IKPYSCEQCG KVFRRNCDLR
RHSLTHTPRQ NF
