MTNB_MOUSE
ID MTNB_MOUSE Reviewed; 241 AA.
AC Q9WVQ5; Q8BP46;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03116};
DE AltName: Full=APAF1-interacting protein {ECO:0000255|HAMAP-Rule:MF_03116};
DE AltName: Full=Monocyte/macrophage protein 19;
GN Name=Apip {ECO:0000255|HAMAP-Rule:MF_03116}; Synonyms=Mmrp19;
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].
RC TISSUE=Macrophage, and Monocyte;
RA Sha S., Aoki Y., Nishi Y.;
RT "A cDNA sequence from murine monocyte-macrophage.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15262985; DOI=10.1074/jbc.m405747200;
RA Cho D.-H., Hong Y.-M., Lee H.-J., Woo H.-N., Pyo J.-O., Mak T.W.,
RA Jung Y.-K.;
RT "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-
RT interacting protein.";
RL J. Biol. Chem. 279:39942-39950(2004).
RN [5]
RP FUNCTION.
RX PubMed=17086211; DOI=10.1038/sj.onc.1210080;
RA Cho D.-H., Lee H.-J., Kim H.-J., Hong S.-H., Pyo J.-O., Cho C., Jung Y.-K.;
RT "Suppression of hypoxic cell death by APIP-induced sustained activation of
RT AKT and ERK1/2.";
RL Oncogene 26:2809-2814(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Catalyzes the dehydration of methylthioribulose-1-phosphate
CC (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
CC Functions in the methionine salvage pathway, which plays a key role in
CC cancer, apoptosis, microbial proliferation and inflammation. May
CC inhibit the CASP1-related inflammatory response (pyroptosis), the
CC CASP9-dependent apoptotic pathway and the cytochrome c-dependent and
CC APAF1-mediated cell death. {ECO:0000255|HAMAP-Rule:MF_03116,
CC ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:17086211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03116};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03116};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03116};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 2/6. {ECO:0000255|HAMAP-Rule:MF_03116}.
CC -!- SUBUNIT: Homotetramer. Interacts with APAF1. May interact with CASP1.
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:15262985}.
CC -!- INDUCTION: Up-regulated upon ischemia/hypoxia.
CC {ECO:0000269|PubMed:15262985}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR EMBL; AB028863; BAA78906.1; -; mRNA.
DR EMBL; AK077705; BAC36968.1; -; mRNA.
DR EMBL; AK145450; BAE26445.1; -; mRNA.
DR EMBL; BC028434; AAH28434.1; -; mRNA.
DR CCDS; CCDS16474.1; -.
DR RefSeq; NP_062709.3; NM_019735.4.
DR AlphaFoldDB; Q9WVQ5; -.
DR SMR; Q9WVQ5; -.
DR BioGRID; 207931; 7.
DR STRING; 10090.ENSMUSP00000011055; -.
DR iPTMnet; Q9WVQ5; -.
DR PhosphoSitePlus; Q9WVQ5; -.
DR SwissPalm; Q9WVQ5; -.
DR EPD; Q9WVQ5; -.
DR MaxQB; Q9WVQ5; -.
DR PaxDb; Q9WVQ5; -.
DR PeptideAtlas; Q9WVQ5; -.
DR PRIDE; Q9WVQ5; -.
DR ProteomicsDB; 286083; -.
DR Antibodypedia; 25889; 337 antibodies from 31 providers.
DR Ensembl; ENSMUST00000011055; ENSMUSP00000011055; ENSMUSG00000010911.
DR GeneID; 56369; -.
DR KEGG; mmu:56369; -.
DR UCSC; uc008lin.2; mouse.
DR CTD; 51074; -.
DR MGI; MGI:1926788; Apip.
DR VEuPathDB; HostDB:ENSMUSG00000010911; -.
DR eggNOG; KOG2631; Eukaryota.
DR GeneTree; ENSGT00390000001680; -.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; Q9WVQ5; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 1062330at2759; -.
DR PhylomeDB; Q9WVQ5; -.
DR TreeFam; TF105632; -.
DR Reactome; R-MMU-111458; Formation of apoptosome.
DR Reactome; R-MMU-9627069; Regulation of the apoptosome activity.
DR UniPathway; UPA00904; UER00875.
DR BioGRID-ORCS; 56369; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Apip; mouse.
DR PRO; PR:Q9WVQ5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WVQ5; protein.
DR Bgee; ENSMUSG00000010911; Expressed in heart right ventricle and 235 other tissues.
DR Genevisible; Q9WVQ5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR InterPro; IPR027514; Salvage_MtnB_euk.
DR PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Apoptosis; Cytoplasm; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..241
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000239023"
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT CONFLICT 11
FT /note="C -> S (in Ref. 2; BAC36968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 26949 MW; 4366CF4AD2239DB8 CRC64;
MSGCQAQGDC CSRPCGAQDK EHPRFLIPEL CKQFYHLGWV TGTGGGISLK HGNEIYIAPS
GVQKERIQPE DMFVCDINEQ DISGPPASKK LKKSQCTPLF MNAYTMRGAG AVIHTHSKAA
VMATLLFPGQ EFKITHQEMI KGIRKCTSGG YYRYDDMLVV PIIENTPEEK DLKERMAHAM
NEYPDSCAVL VRRHGVYVWG ETWEKAKTMC ECYDYLFDIA VSMKKMGLDP TQLPVGENGI
V
