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Protein

Methylthioribulose-1-phosphate dehydratase

Gene

Apip

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death.UniRule annotation2 Publications

Catalytic activityi

S-methyl-5-thio-D-ribulose 1-phosphate = 5-(methylthio)-2,3-dioxopentyl phosphate + H2O.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 2 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (Mri1)
  2. Methylthioribulose-1-phosphate dehydratase (Apip)
  3. Enolase-phosphatase E1 (Enoph1)
  4. Enolase-phosphatase E1 (Enoph1)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141ZincUniRule annotation
Metal bindingi116 – 1161ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB
  • L-methionine biosynthetic process from S-adenosylmethionine Source: UniProtKB-HAMAP
  • negative regulation of apoptotic process Source: UniProtKB
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Apoptosis, Methionine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00904; UER00875.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribulose-1-phosphate dehydrataseUniRule annotation (EC:4.2.1.109UniRule annotation)
Short name:
MTRu-1-P dehydrataseUniRule annotation
Alternative name(s):
APAF1-interacting proteinUniRule annotation
Monocyte/macrophage protein 19
Gene namesi
Name:Apip
Synonyms:Mmrp19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1926788. Apip.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Methylthioribulose-1-phosphate dehydratasePRO_0000239023Add
BLAST

Proteomic databases

EPDiQ9WVQ5.
MaxQBiQ9WVQ5.
PaxDbiQ9WVQ5.
PRIDEiQ9WVQ5.

PTM databases

iPTMnetiQ9WVQ5.
PhosphoSiteiQ9WVQ5.
SwissPalmiQ9WVQ5.

Expressioni

Tissue specificityi

Expressed in skeletal muscle (at protein level).1 Publication

Inductioni

Up-regulated upon ischemia/hypoxia.1 Publication

Gene expression databases

BgeeiQ9WVQ5.
CleanExiMM_APIP.
GenevisibleiQ9WVQ5. MM.

Interactioni

Subunit structurei

Interacts with APAF1. May interact with CASP1.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9WVQ5. 1 interaction.
MINTiMINT-4111745.
STRINGi10090.ENSMUSP00000011055.

Structurei

3D structure databases

ProteinModelPortaliQ9WVQ5.
SMRiQ9WVQ5. Positions 19-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldolase class II family. MtnB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2631. Eukaryota.
COG0235. LUCA.
GeneTreeiENSGT00390000001680.
HOGENOMiHOG000192424.
HOVERGENiHBG080536.
InParanoidiQ9WVQ5.
KOiK08964.
OMAiQCTPLFL.
OrthoDBiEOG74TX0H.
PhylomeDBiQ9WVQ5.
TreeFamiTF105632.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_03116. Salvage_MtnB_euk.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
IPR027514. Salvage_MtnB_euk.
[Graphical view]
PANTHERiPTHR10640. PTHR10640. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR03328. salvage_mtnB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WVQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGCQAQGDC CSRPCGAQDK EHPRFLIPEL CKQFYHLGWV TGTGGGISLK
60 70 80 90 100
HGNEIYIAPS GVQKERIQPE DMFVCDINEQ DISGPPASKK LKKSQCTPLF
110 120 130 140 150
MNAYTMRGAG AVIHTHSKAA VMATLLFPGQ EFKITHQEMI KGIRKCTSGG
160 170 180 190 200
YYRYDDMLVV PIIENTPEEK DLKERMAHAM NEYPDSCAVL VRRHGVYVWG
210 220 230 240
ETWEKAKTMC ECYDYLFDIA VSMKKMGLDP TQLPVGENGI V
Length:241
Mass (Da):26,949
Last modified:November 1, 1999 - v1
Checksum:i4366CF4AD2239DB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111C → S in BAC36968 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028863 mRNA. Translation: BAA78906.1.
AK077705 mRNA. Translation: BAC36968.1.
AK145450 mRNA. Translation: BAE26445.1.
BC028434 mRNA. Translation: AAH28434.1.
CCDSiCCDS16474.1.
RefSeqiNP_062709.3. NM_019735.4.
UniGeneiMm.24772.

Genome annotation databases

EnsembliENSMUST00000011055; ENSMUSP00000011055; ENSMUSG00000010911.
GeneIDi56369.
KEGGimmu:56369.
UCSCiuc008lin.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028863 mRNA. Translation: BAA78906.1.
AK077705 mRNA. Translation: BAC36968.1.
AK145450 mRNA. Translation: BAE26445.1.
BC028434 mRNA. Translation: AAH28434.1.
CCDSiCCDS16474.1.
RefSeqiNP_062709.3. NM_019735.4.
UniGeneiMm.24772.

3D structure databases

ProteinModelPortaliQ9WVQ5.
SMRiQ9WVQ5. Positions 19-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVQ5. 1 interaction.
MINTiMINT-4111745.
STRINGi10090.ENSMUSP00000011055.

PTM databases

iPTMnetiQ9WVQ5.
PhosphoSiteiQ9WVQ5.
SwissPalmiQ9WVQ5.

Proteomic databases

EPDiQ9WVQ5.
MaxQBiQ9WVQ5.
PaxDbiQ9WVQ5.
PRIDEiQ9WVQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000011055; ENSMUSP00000011055; ENSMUSG00000010911.
GeneIDi56369.
KEGGimmu:56369.
UCSCiuc008lin.2. mouse.

Organism-specific databases

CTDi51074.
MGIiMGI:1926788. Apip.

Phylogenomic databases

eggNOGiKOG2631. Eukaryota.
COG0235. LUCA.
GeneTreeiENSGT00390000001680.
HOGENOMiHOG000192424.
HOVERGENiHBG080536.
InParanoidiQ9WVQ5.
KOiK08964.
OMAiQCTPLFL.
OrthoDBiEOG74TX0H.
PhylomeDBiQ9WVQ5.
TreeFamiTF105632.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00875.

Miscellaneous databases

ChiTaRSiApip. mouse.
PROiQ9WVQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVQ5.
CleanExiMM_APIP.
GenevisibleiQ9WVQ5. MM.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_03116. Salvage_MtnB_euk.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
IPR027514. Salvage_MtnB_euk.
[Graphical view]
PANTHERiPTHR10640. PTHR10640. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR03328. salvage_mtnB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cDNA sequence from murine monocyte-macrophage."
    Sha S., Aoki Y., Nishi Y.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage and Monocyte.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein."
    Cho D.-H., Hong Y.-M., Lee H.-J., Woo H.-N., Pyo J.-O., Mak T.W., Jung Y.-K.
    J. Biol. Chem. 279:39942-39950(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  5. "Suppression of hypoxic cell death by APIP-induced sustained activation of AKT and ERK1/2."
    Cho D.-H., Lee H.-J., Kim H.-J., Hong S.-H., Pyo J.-O., Cho C., Jung Y.-K.
    Oncogene 26:2809-2814(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMTNB_MOUSE
AccessioniPrimary (citable) accession number: Q9WVQ5
Secondary accession number(s): Q8BP46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.