Q9BV20 (MTNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylthioribose-1-phosphate isomerase
Short name=M1Pi
Short name=MTR-1-P isomerase
EC=5.3.1.23

Alternative name(s):
Mediator of RhoA-dependent invasion
S-methyl-5-thioribose-1-phosphate isomerase
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein

Gene names

Name:	MRI1
Synonyms:	MRDI
ORF Names:	UNQ6390/PRO21135

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. Ref.5
Catalytic activity	S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate. HAMAP-Rule MF_03119
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. HAMAP-Rule MF_03119
Subcellular location	Nucleus. Cytoplasm. Cell projection. Note: Primarily nuclear, but cytoplasmic in cancer cells, with enrichment at leading edge of the plasma membrane in late stage tumor cells. Ref.5
Induction	By RhoA activation in cancer cells (at protein level). Ref.5
Sequence similarities	Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cell projection Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP L-methionine salvage from methylthioadenosine Inferred from Biological aspect of Ancestor. Source: RefGenome polyamine metabolic process Traceable author statement. Source: Reactome
Cellular_component	cell projection Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	S-methyl-5-thioribose-1-phosphate isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-747381,EBI-747381

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BV20-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BV20-2)

The sequence of this isoform differs from the canonical sequence as follows:
     125-200: VICCTEDMLE...LGRLEHAFCT → RETELCEHWEEHTRQRELPLRGPLGGTVL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Methylthioribose-1-phosphate isomerase HAMAP-Rule MF_03119		PRO_0000317325
Sites
	Active site	248	1	Proton donor Ref.5
	Site	168	1	Transition state stabilizer
Natural variations
	Alternative sequence	125 – 200	76	VICCT…HAFCT → RETELCEHWEEHTRQRELPL RGPLGGTVL in isoform 2.		VSP_030935
	Natural variant	235	1	M → V. Corresponds to variant rs35098252 [ dbSNP | Ensembl ].		VAR_059253
	Natural variant	319	1	G → A. Corresponds to variant rs10402855 [ dbSNP | Ensembl ].		VAR_059254
Experimental info
	Mutagenesis	168	1	C → S: Abolishes enzymatic activity. Ref.5
	Mutagenesis	248	1	D → A: Abolishes enzymatic activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A6A1B5EC76632F4F	FASTA	369	39,150
	10 20 30 40 50 60 MTLEAIRYSR GSLQILDQLL LPKQSRYEAV GSVHQAWEAI RAMKVRGAPA IALVGCLSLA 70 80 90 100 110 120 VELQAGAGGP GLAALVAFVR DKLSFLVTAR PTAVNMARAA RDLADVAARE AEREGATEEA 130 140 150 160 170 180 VRERVICCTE DMLEKDLRDN RSIGDLGARH LLERVAPSGG KVTVLTHCNT GALATAGYGT 190 200 210 220 230 240 ALGVIRSLHS LGRLEHAFCT ETRPYNQGAR LTAFELVYEQ IPATLITDSM VAAAMAHRGV 250 260 270 280 290 300 SAVVVGADRV VANGDTANKV GTYQLAIVAK HHGIPFYVAA PSSSCDLRLE TGKEIIIEER 310 320 330 340 350 360 PGQELTDVNG VRIAAPGIGV WNPAFDVTPH DLITGGIITE LGVFAPEELR TALTTTISSR DGTLDGPQM
	Isoform 2 [UniParc]. Checksum: B9C6A0C26615AA76	FASTA	322	34,529
	10 20 30 40 50 60 MTLEAIRYSR GSLQILDQLL LPKQSRYEAV GSVHQAWEAI RAMKVRGAPA IALVGCLSLA 70 80 90 100 110 120 VELQAGAGGP GLAALVAFVR DKLSFLVTAR PTAVNMARAA RDLADVAARE AEREGATEEA 130 140 150 160 170 180 VRERRETELC EHWEEHTRQR ELPLRGPLGG TVLETRPYNQ GARLTAFELV YEQIPATLIT 190 200 210 220 230 240 DSMVAAAMAH RGVSAVVVGA DRVVANGDTA NKVGTYQLAI VAKHHGIPFY VAAPSSSCDL 250 260 270 280 290 300 RLETGKEIII EERPGQELTD VNGVRIAAPG IGVWNPAFDV TPHDLITGGI ITELGVFAPE 310 320 ELRTALTTTI SSRDGTLDGP QM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORM 1). Tissue: Brain.
[5]	"A mediator of Rho-dependent invasion moonlights as a methionine salvage enzyme." Kabuyama Y., Litman E.S., Templeton P.D., Metzner S.I., Witze E.S., Argast G.M., Langer S.J., Polvinen K., Shellman Y., Chan D., Shabb J.B., Fitzpatrick J.E., Resing K.A., Sousa M.C., Ahn N.G. Mol. Cell. Proteomics 8:2308-2320(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ACTIVE SITE, INDUCTION BY RHOA, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-168 AND ASP-248.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY358176 mRNA. Translation: AAQ88543.1. AL834276 mRNA. Translation: CAD38951.1. CH471106 Genomic DNA. Translation: EAW84370.1. CH471106 Genomic DNA. Translation: EAW84371.1. BC001703 mRNA. Translation: AAH01703.1.
IPI	IPI00005948. IPI00184525.
RefSeq	NP_001026897.1. NM_001031727.2. NP_115661.1. NM_032285.2.
UniGene	Hs.439370.
3D structure databases
HSSP	HSSP built from PDB template 1W2W based on UniProtKB Q06489.
ProteinModelPortal	Q9BV20.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1197605.
STRING	9606.ENSP00000040663.
PTM databases
PhosphoSite	Q9BV20.
Polymorphism databases
DMDM	74733279.
Proteomic databases
PaxDb	Q9BV20.
PeptideAtlas	Q9BV20.
PRIDE	Q9BV20.
Protocols and materials databases
DNASU	84245.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000040663; ENSP00000040663; ENSG00000037757. ENST00000319545; ENSP00000314871; ENSG00000037757.
GeneID	84245.
KEGG	hsa:84245.
UCSC	uc002mxe.3. human. uc002mxf.3. human.
Organism-specific databases
CTD	84245.
GeneCards	GC19P013875.
HGNC	HGNC:28469. MRI1.
HPA	CAB045988. HPA042744.
MIM	615105. gene.
neXtProt	NX_Q9BV20.
PharmGKB	PA164723110.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0182.
HOGENOM	HOG000224730.
InParanoid	Q9BV20.
KO	K08963.
OMA	RGVEDGW.
OrthoDB	EOG41C6WN.
PhylomeDB	Q9BV20.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00904; UER00874.
Gene expression databases
Bgee	Q9BV20.
Genevestigator	Q9BV20.
Family and domain databases
HAMAP	MF_01678. Salvage_MtnA.
InterPro	IPR000649. IF-2B-related. IPR005251. IF-2BI_MTNA. IPR011559. Initiation_fac_2B_a/b/d. [Graphical view]
PANTHER	PTHR10233. PTHR10233. 1 hit. PTHR10233:SF6. PTHR10233:SF6. 1 hit.
Pfam	PF01008. IF-2B. 1 hit. [Graphical view]
TIGRFAMs	TIGR00524. eIF-2B_rel. 1 hit. TIGR00512. salvage_mtnA. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	84245.
NextBio	73721.
SOURCE	Search...

Entry information

Entry name

MTNA_HUMAN

Accession

Primary (citable) accession number: Q9BV20
Secondary accession number(s): Q8NDC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.