MBLC1_MOUSE
ID MBLC1_MOUSE Reviewed; 260 AA.
AC Q8BWY4; Q8CHU7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein 1;
DE EC=3.1.27.- {ECO:0000250|UniProtKB:A4D2B0};
DE AltName: Full=Endoribonuclease MBLAC1 {ECO:0000250|UniProtKB:A4D2B0};
GN Name=Mblac1 {ECO:0000312|MGI:MGI:2679717};
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;
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].
RC STRAIN=FVB/N-3; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endoribonuclease that catalyzes the hydrolysis of histone-
CC coding pre-mRNA 3'-end. Involved in histone pre-mRNA processing during
CC the S-phase of the cell cycle, which is required for
CC entering/progressing through S-phase. Cleaves histone pre-mRNA at a
CC major and a minor cleavage site after the 5'-ACCCA-3' and the 5'-
CC ACCCACA-3' sequence, respectively, and located downstream of the stem-
CC loop. May require the presence of the HDE element located at the
CC histone pre-RNA 3'-end to avoid non-specific cleavage.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end
CC ribonucleotide-RNA + a 5'-end (5'-phospho)-ribonucleoside-RNA + H(+);
CC Xref=Rhea:RHEA:68096, Rhea:RHEA-COMP:15179, Rhea:RHEA-COMP:17355,
CC Rhea:RHEA-COMP:17428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:138282, ChEBI:CHEBI:173118;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68097;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:A4D2B0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A4D2B0}. Nucleus {ECO:0000250|UniProtKB:A4D2B0}.
CC Note=Localizes in the nucleus during early S-phase of the cell cycle.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- DOMAIN: Contains four of the five characteristic MBL-fold metal-binding
CC motifs, with two waters completing metal coordination.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AK049381; BAC33723.1; -; mRNA.
DR EMBL; BC038925; AAH38925.1; -; mRNA.
DR CCDS; CCDS19796.1; -.
DR RefSeq; NP_808546.1; NM_177878.3.
DR AlphaFoldDB; Q8BWY4; -.
DR SMR; Q8BWY4; -.
DR STRING; 10090.ENSMUSP00000052869; -.
DR PhosphoSitePlus; Q8BWY4; -.
DR EPD; Q8BWY4; -.
DR MaxQB; Q8BWY4; -.
DR PaxDb; Q8BWY4; -.
DR PRIDE; Q8BWY4; -.
DR ProteomicsDB; 293416; -.
DR Antibodypedia; 71061; 16 antibodies from 9 providers.
DR Ensembl; ENSMUST00000057773; ENSMUSP00000052869; ENSMUSG00000049285.
DR GeneID; 330216; -.
DR KEGG; mmu:330216; -.
DR UCSC; uc009afa.2; mouse.
DR CTD; 255374; -.
DR MGI; MGI:2679717; Mblac1.
DR VEuPathDB; HostDB:ENSMUSG00000049285; -.
DR eggNOG; KOG4736; Eukaryota.
DR GeneTree; ENSGT00390000016193; -.
DR HOGENOM; CLU_030571_2_6_1; -.
DR InParanoid; Q8BWY4; -.
DR OMA; FPGQPYS; -.
DR OrthoDB; 1139836at2759; -.
DR PhylomeDB; Q8BWY4; -.
DR TreeFam; TF316508; -.
DR BioGRID-ORCS; 330216; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8BWY4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BWY4; protein.
DR Bgee; ENSMUSG00000049285; Expressed in rostral migratory stream and 147 other tissues.
DR Genevisible; Q8BWY4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0008334; P:histone mRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR039344; MBLAC1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR23200; PTHR23200; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..260
FT /note="Metallo-beta-lactamase domain-containing protein 1"
FT /id="PRO_0000337028"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT CONFLICT 19
FT /note="S -> T (in Ref. 2; AAH38925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 26923 MW; EE08CB1E9E323756 CRC64;
MNGPVRTEPL HGEIPLLASS GSYSVVVLLR GYAEPQGAGD AVRADGTVTL VLPRGWASDS
SRGLAPSADG GSKTALEEAV RGPILVDTGG PWARGALLEA LATQGVAPED VTLVVGTHGH
SDHIGNLGLF PEAALLVSHD FCLPEGLYLP HGLCETQPLI LGSGLQVWAT PGHGGQRDVS
VVVEGTSLGT VVVAGDVFER LGDEDSWQAL SEDPVAQQRS RERILSVADV VVPGHGAPFR
VVRETVKSSE DLICEGKAVA
