LDHB_RAT
ID LDHB_RAT Reviewed; 334 AA.
AC P42123;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=L-lactate dehydrogenase B chain;
DE Short=LDH-B;
DE EC=1.1.1.27 {ECO:0000250|UniProtKB:P07195};
DE AltName: Full=LDH heart subunit;
DE Short=LDH-H;
GN Name=Ldhb; Synonyms=Ldh-2, Ldh2;
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 [MRNA].
RC TISSUE=Heart;
RX PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
RA Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
RT "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals,
RT birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from
RT Xenopus, pig, and rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 PROTEIN SEQUENCE OF 24-91; 120-127 AND 159-170, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC and lactate with concomitant interconversion of NADH and NAD(+).
CC {ECO:0000250|UniProtKB:P07195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000250|UniProtKB:P07195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC Evidence={ECO:0000250|UniProtKB:P07195};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC Evidence={ECO:0000250|UniProtKB:P07195};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P07195}.
CC -!- SUBUNIT: Homotetramer. Interacts with PTEN upstream reading frame
CC protein MP31; the interaction leads to inhibition of mitochondrial
CC lactate dehydrogenase activity, preventing conversion of lactate to
CC pyruvate in mitochondria. {ECO:0000250|UniProtKB:P07195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07195}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; U07181; AAA50439.1; -; mRNA.
DR EMBL; BC059149; AAH59149.1; -; mRNA.
DR PIR; I62761; I62761.
DR RefSeq; NP_001303262.1; NM_001316333.1.
DR RefSeq; NP_001303263.1; NM_001316334.1.
DR RefSeq; NP_036727.1; NM_012595.2.
DR AlphaFoldDB; P42123; -.
DR SMR; P42123; -.
DR BioGRID; 246687; 6.
DR IntAct; P42123; 4.
DR MINT; P42123; -.
DR STRING; 10116.ENSRNOP00000017965; -.
DR ChEMBL; CHEMBL2176834; -.
DR iPTMnet; P42123; -.
DR PhosphoSitePlus; P42123; -.
DR SwissPalm; P42123; -.
DR World-2DPAGE; 0004:P42123; -.
DR jPOST; P42123; -.
DR PaxDb; P42123; -.
DR PRIDE; P42123; -.
DR Ensembl; ENSRNOT00000017965; ENSRNOP00000017965; ENSRNOG00000013000.
DR GeneID; 24534; -.
DR KEGG; rno:24534; -.
DR UCSC; RGD:2997; rat.
DR CTD; 3945; -.
DR RGD; 2997; Ldhb.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000153525; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; P42123; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; P42123; -.
DR TreeFam; TF314963; -.
DR Reactome; R-RNO-70268; Pyruvate metabolism.
DR UniPathway; UPA00554; UER00611.
DR PRO; PR:P42123; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013000; Expressed in heart and 20 other tissues.
DR Genevisible; P42123; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:1990204; C:oxidoreductase complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:RGD.
DR GO; GO:0004457; F:lactate dehydrogenase activity; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0006089; P:lactate metabolic process; IDA:RGD.
DR GO; GO:0019674; P:NAD metabolic process; IDA:RGD.
DR GO; GO:0006090; P:pyruvate metabolic process; ISO:RGD.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT CHAIN 2..334
FT /note="L-lactate dehydrogenase B chain"
FT /id="PRO_0000168464"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
SQ SEQUENCE 334 AA; 36612 MW; AE9DE0AF5194CDE0 CRC64;
MATLKEKLIA PVADDETAVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
IIPQIVKYSP DCTIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVDSAY
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
LTSVINQKLK DDEVAQLRKS ADTLWDIQKD LKDL
