LACB2_RAT
ID LACB2_RAT Reviewed; 288 AA.
AC Q561R9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Endoribonuclease LACTB2 {ECO:0000250|UniProtKB:Q53H82};
DE AltName: Full=Beta-lactamase-like protein 2;
DE EC=3.1.27.- {ECO:0000250|UniProtKB:Q53H82};
GN Name=Lactb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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).
CC -!- FUNCTION: Endoribonuclease; cleaves preferentially 3' to purine-
CC pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage
CC product contains a free 3' -OH group. Has no activity with double-
CC stranded RNA or DNA. Required for normal mitochondrial function and
CC cell viability. {ECO:0000250|UniProtKB:Q53H82}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q53H82};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q53H82};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q53H82}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q53H82}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; BC093378; AAH93378.1; -; mRNA.
DR RefSeq; NP_001019418.1; NM_001024247.1.
DR AlphaFoldDB; Q561R9; -.
DR SMR; Q561R9; -.
DR IntAct; Q561R9; 11.
DR STRING; 10116.ENSRNOP00000010369; -.
DR iPTMnet; Q561R9; -.
DR PhosphoSitePlus; Q561R9; -.
DR jPOST; Q561R9; -.
DR PaxDb; Q561R9; -.
DR PRIDE; Q561R9; -.
DR Ensembl; ENSRNOT00000112393; ENSRNOP00000084220; ENSRNOG00000007829.
DR GeneID; 297768; -.
DR KEGG; rno:297768; -.
DR UCSC; RGD:1307876; rat.
DR CTD; 51110; -.
DR RGD; 1307876; Lactb2.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00390000001710; -.
DR HOGENOM; CLU_048478_1_2_1; -.
DR InParanoid; Q561R9; -.
DR OMA; EFYLAHR; -.
DR OrthoDB; 576967at2759; -.
DR PhylomeDB; Q561R9; -.
DR TreeFam; TF314297; -.
DR PRO; PR:Q561R9; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007829; Expressed in kidney and 20 other tissues.
DR Genevisible; Q561R9; RN.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR041516; LACTB2_WH.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF17778; BLACT_WH; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endonuclease; Hydrolase; Metal-binding; Mitochondrion;
KW Nuclease; Phosphoprotein; Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..288
FT /note="Endoribonuclease LACTB2"
FT /id="PRO_0000315745"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 273
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 282
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
SQ SEQUENCE 288 AA; 32484 MW; 23113B051EAA3835 CRC64;
MAAALQRIEQ LSSRVVRVLG CNPGPMTLQG TNTYLVGTGS RRILIDTGEP SVPEYISCLK
QALAEFDTAI QEILVTHWHR DHSGGIVDIC KNISNDATYC IKKLRRNPQK EEIIGSGEQQ
YVYIEDGDLI KTEGATLRVL YTPGHTDDHM ALLLEEENAI FSGDCILGEG TTIFEDLSDY
MNSLKDLLKV KANIIYPGHG PVIHNAEAKI LEYISHRNNR EEQIITVFRD NLEESFSVSE
LRKMIYKNVP ENLHKMAEHN LLLHLRKLEK DGKIFSIASP AKKWRASL
