MB211_MOUSE
ID MB211_MOUSE Reviewed; 359 AA.
AC O70299;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative nucleotidyltransferase MAB21L1;
DE EC=2.7.7.- {ECO:0000305};
DE AltName: Full=Protein mab-21-like 1;
GN Name=Mab21l1; Synonyms=Mab21;
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, AND DEVELOPMENTAL STAGE.
RX PubMed=10349626; DOI=10.1016/s0925-4773(98)00180-4;
RA Mariani M., Corradi A., Baldessari D., Malgaretti N., Pozzoli O., Fesce R.,
RA Martinez S., Boncinelli E., Consalez G.G.;
RT "Mab21, the mouse homolog of a C. elegans cell-fate specification gene,
RT participates in cerebellar, midbrain and eye development.";
RL Mech. Dev. 79:131-135(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11857508; DOI=10.1002/tera.10018;
RA Wong R.L.Y., Chow K.L.;
RT "Depletion of Mab21l1 and Mab21l2 messages in mouse embryo arrests axial
RT turning, and impairs notochord and neural tube differentiation.";
RL Teratology 65:70-77(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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].
RC TISSUE=Eye;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10556287; DOI=10.1093/hmg/8.13.2397;
RA Mariani M., Baldessari D., Francisconi S., Viggiano L., Rocchi M.,
RA Zappavigna V., Malgaretti N., Consalez G.G.;
RT "Two murine and human homologs of mab-21, a cell fate determination gene
RT involved in Caenorhabditis elegans neural development.";
RL Hum. Mol. Genet. 8:2397-2406(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=12642482; DOI=10.1242/dev.00399;
RA Yamada R., Mizutani-Koseki Y., Hasegawa T., Osumi N., Koseki H.,
RA Takahashi N.;
RT "Cell-autonomous involvement of Mab21l1 is essential for lens placode
RT development.";
RL Development 130:1759-1770(2003).
RN [7]
RP INDUCTION.
RX PubMed=17167770; DOI=10.1002/jcp.20933;
RA Kim Y.-J., Kim B.-G., Lee S.-J., Lee H.-K., Lee S.-H., Ryoo H.-M.,
RA Cho J.-Y.;
RT "The suppressive effect of myeloid Elf-1-like factor (MEF) in osteogenic
RT differentiation.";
RL J. Cell. Physiol. 211:253-260(2007).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=29156428; DOI=10.1016/j.diff.2017.11.001;
RA Nguyen D., Yamada R., Yoshimitsu N., Oguri A., Kojima T., Takahashi N.;
RT "Involvement of the Mab21l1 gene in calvarial osteogenesis.";
RL Differentiation 98:70-78(2017).
CC -!- FUNCTION: Putative nucleotidyltransferase required for several aspects
CC of embryonic development including normal development of the eye,
CC notochord, neural tube and other organ tissues, and for embryonic
CC turning (PubMed:11857508, PubMed:12642482). It is unclear whether it
CC displays nucleotidyltransferase activity in vivo (By similarity). Binds
CC single-stranded RNA (ssRNA) (By similarity).
CC {ECO:0000250|UniProtKB:Q13394, ECO:0000269|PubMed:11857508,
CC ECO:0000269|PubMed:12642482}.
CC -!- SUBUNIT: Monomer. Homodecamer; composed of 2 back to back
CC homopentamers. The protein may exist as monomer in solution and
CC oiligomerizes upon ligand binding. {ECO:0000250|UniProtKB:Q13394}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556287}.
CC -!- TISSUE SPECIFICITY: Expressed in the adult cerebellum and eye, with
CC lower levels in the adult forebrain. {ECO:0000269|PubMed:10349626,
CC ECO:0000269|PubMed:10556287}.
CC -!- DEVELOPMENTAL STAGE: At 10 dpc, expressed in the temporal aspect of the
CC retina and the anterior portion of the alar midbrain. At 10.5 dpc this
CC retinal pattern of expression persists, with expression also beginning
CC in the lens. Also expressed in the spinal cord, the optic cup, the
CC presumptive lens and the genital ridge. Expressed in the dorsal
CC midline, somites, and interdigital tissues from 9.5 dpc to 13.5 dpc.
CC {ECO:0000269|PubMed:10349626, ECO:0000269|PubMed:10556287,
CC ECO:0000269|PubMed:12642482}.
CC -!- INDUCTION: Expression is down-regulated by BMP2.
CC {ECO:0000269|PubMed:17167770}.
CC -!- DISRUPTION PHENOTYPE: Mice show eye and preputial gland defects
CC (PubMed:12642482). Most male mice are sterile, but they can reproduce
CC by in vitro fertilization (PubMed:12642482). Mice display calvarial
CC ossification characterized by an unclosed calvarial region with
CC impaired growth of fontanelle and parietal bones during postnatal
CC development (PubMed:29156428). {ECO:0000269|PubMed:12642482,
CC ECO:0000269|PubMed:29156428}.
CC -!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
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DR EMBL; AF040945; AAC15636.1; -; mRNA.
DR EMBL; AF228913; AAF67140.1; -; mRNA.
DR EMBL; AK032114; BAC27711.1; -; mRNA.
DR EMBL; BC014750; AAH14750.1; -; mRNA.
DR CCDS; CCDS17360.1; -.
DR RefSeq; NP_034880.1; NM_010750.3.
DR AlphaFoldDB; O70299; -.
DR SMR; O70299; -.
DR STRING; 10090.ENSMUSP00000074878; -.
DR PhosphoSitePlus; O70299; -.
DR PaxDb; O70299; -.
DR PeptideAtlas; O70299; -.
DR PRIDE; O70299; -.
DR ProteomicsDB; 295835; -.
DR TopDownProteomics; O70299; -.
DR Antibodypedia; 23045; 68 antibodies from 16 providers.
DR Ensembl; ENSMUST00000075422; ENSMUSP00000074878; ENSMUSG00000056947.
DR GeneID; 17116; -.
DR KEGG; mmu:17116; -.
DR UCSC; uc008pgv.2; mouse.
DR CTD; 4081; -.
DR MGI; MGI:1333773; Mab21l1.
DR VEuPathDB; HostDB:ENSMUSG00000056947; -.
DR eggNOG; KOG3963; Eukaryota.
DR GeneTree; ENSGT01050000244827; -.
DR HOGENOM; CLU_045315_0_0_1; -.
DR InParanoid; O70299; -.
DR OMA; AVDKCKY; -.
DR OrthoDB; 771781at2759; -.
DR PhylomeDB; O70299; -.
DR TreeFam; TF315012; -.
DR BioGRID-ORCS; 17116; 3 hits in 71 CRISPR screens.
DR PRO; PR:O70299; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O70299; protein.
DR Bgee; ENSMUSG00000056947; Expressed in epithelium of lens and 131 other tissues.
DR Genevisible; O70299; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR InterPro; IPR024810; Mab-21_dom.
DR Pfam; PF03281; Mab-21; 1.
DR SMART; SM01265; Mab-21; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="Putative nucleotidyltransferase MAB21L1"
FT /id="PRO_0000312782"
FT BINDING 23..24
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:Q13394"
FT BINDING 63..66
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:Q13394"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 248
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:Q13394"
FT BINDING 252..255
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:Q13394"
SQ SEQUENCE 359 AA; 40956 MW; A27C53FBC997A049 CRC64;
MIAAQAKLVY HLNKYYNEKC QARKAAIAKT IREVCKVVSD VLKEVEVQEP RFISSLNEMD
NRYEGLEVIS PTEFEVVLYL NQMGVFNFVD DGSLPGCAVL KLSDGRKRSM SLWVEFITAS
GYLSARKIRS RFQTLVAQAV DKCSYRDVVK MVADTSEVKL RIRDRYVVQI TPAFKCTGIW
PRSAAHWPLP HIPWPGPNRV AEVKAEGFNL LSKECHSLAG KQSSAESDAW VLQFAEAENR
LQMGGCRKKC LSILKTLRDR HLELPGQPLN NYHMKTLVSY ECEKHPRESD WDESCLGDRL
NGILLQLISC LQCRRCPHYF LPNLDLFQGK PHSALENAAK QTWRLAREIL TNPKSLEKL
