Q8K4H1 (AFMID_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable arylformamidase
EC=3.5.1.9

Alternative name(s):
Kynurenine formamidase
Short name=KF

Gene names

Name:

Afmid

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. Ref.1
Catalytic activity	N-formyl-L-kynurenine + H2O = formate + L-kynurenine.
Pathway	Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
Subcellular location	Cytoplasm › cytosol. Nucleus. Note: Predominantly cytosolic. Some fraction is nuclear. Ref.2
Tissue specificity	Highly expressed in liver. Expressed in kidney. Weakly or not expressed in other tissues. Ref.2
Induction	Down-regulated upon IL2-mediated activation. Transcriptional activation correlates with reduced histone acetylation. Ref.2
Post-translational modification	The N-terminus is blocked.
Disruption phenotype	Mice display sclerosis of kidney glomeruli, possibly due to failures in the elimination of toxic metabolites. Ref.5
Miscellaneous	The Afmid gene shares a bidirectional promoter region with Tk1 gene.
Sequence similarities	Belongs to the AFMID family.
Biophysicochemical properties	Kinetic parameters: KM=0.18 mM for N-formyl-L-kynurenine Ref.6 Vmax=42 µmol/min/mg enzyme
Sequence caution	The sequence AAH24452.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tryptophan catabolic process to kynurenine Inferred from direct assay Ref.5. Source: MGI
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arylformamidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8K4H1-1)

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: Q8K4H1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     296-305: IILKTVFQKL → VGLTPTTVFL...ITLAGLGLKI

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 305	305	Probable arylformamidase		PRO_0000248309
Sites
	Active site	162	1	Probable
	Active site	247	1	Probable
	Active site	279	1	Probable
Natural variations
	Alternative sequence	296 – 305	10	IILKTVFQKL → VGLTPTTVFLNGQRGSHAHT WAWPGRQEQRERLAVPRWKS QSRLHRRACGECLLFIIVVA ETMSHCITLAGLGLKI in isoform 2.		VSP_020237
Experimental info
	Mutagenesis	162	1	S → A: Loss of enzyme activity. Ref.6
	Mutagenesis	247	1	D → A: Loss of enzyme activity. Ref.6
	Mutagenesis	279	1	H → A: Loss of enzyme activity. Ref.6
	Sequence conflict	33	1	H → R in AAH43309. Ref.4
	Sequence conflict	33	1	H → R in AAH24452. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 898000A577132A52	FASTA	305	34,229
	10 20 30 40 50 60 MAFPSLSAGQ NPWRNLSSEE LEKQYSPSRW VIHTKPEEVV GNFVQIGSQA TQKARATRRN 70 80 90 100 110 120 QLDVPYGDGE GEKLDIYFPD EDSKAFPLFL FLHGGYWQSG SKDDSAFMVN PLTAQGIVVV 130 140 150 160 170 180 IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY PSNEGIYLCG HSAGAHLAAM VLLARWTKHG 190 200 210 220 230 240 VTPNLQGFLL VSGIYDLEPL IATSQNDPLR MTLEDAQRNS PQRHLDVVPA QPVAPACPVL 250 260 270 280 290 300 VLVGQHDSPE FHRQSKEFYE TLLRVGWKAS FQQLRGVDHF DIIENLTRED DVLTQIILKT VFQKL
	Isoform 2 [UniParc]. Checksum: 0F20521893042E06	FASTA	371	41,574
	10 20 30 40 50 60 MAFPSLSAGQ NPWRNLSSEE LEKQYSPSRW VIHTKPEEVV GNFVQIGSQA TQKARATRRN 70 80 90 100 110 120 QLDVPYGDGE GEKLDIYFPD EDSKAFPLFL FLHGGYWQSG SKDDSAFMVN PLTAQGIVVV 130 140 150 160 170 180 IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY PSNEGIYLCG HSAGAHLAAM VLLARWTKHG 190 200 210 220 230 240 VTPNLQGFLL VSGIYDLEPL IATSQNDPLR MTLEDAQRNS PQRHLDVVPA QPVAPACPVL 250 260 270 280 290 300 VLVGQHDSPE FHRQSKEFYE TLLRVGWKAS FQQLRGVDHF DIIENLTRED DVLTQVGLTP 310 320 330 340 350 360 TTVFLNGQRG SHAHTWAWPG RQEQRERLAV PRWKSQSRLH RRACGECLLF IIVVAETMSH 370 CITLAGLGLK I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Kynurenine formamidase: determination of primary structure and modeling-based prediction of tertiary structure and catalytic triad." Pabarcus M.K., Casida J.E. Biochim. Biophys. Acta 1596:201-211(2002) [PubMed: 12007602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 16-29; 35-53; 150-160 AND 224-242, FUNCTION. Strain: Swiss Webster. Tissue: Liver.
[2]	"Alternate activation of two divergently transcribed mouse genes from a bidirectional promoter is linked to changes in histone modification." Schuettengruber B., Doetzlhofer A., Kroboth K., Wintersberger E., Seiser C. J. Biol. Chem. 278:1784-1793(2003) [PubMed: 12411446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: FVB/N. Tissue: Kidney and Liver.
[5]	"Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype." Dobrovolsky V.N., Bowyer J.F., Pabarcus M.K., Heflich R.H., Williams L.D., Doerge D.R., Arvidsson B., Bergquist J., Casida J.E. Biochim. Biophys. Acta 1724:163-172(2005) [PubMed: 15866519] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[6]	"Cloning, expression, and catalytic triad of recombinant arylformamidase." Pabarcus M.K., Casida J.E. Protein Expr. Purif. 44:39-44(2005) [PubMed: 15935693] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-162; ASP-247 AND HIS-279.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF399717 mRNA. Translation: AAM62284.1. AY099479 mRNA. Translation: AAM44406.1. AL591433 Genomic DNA. Translation: CAM19096.1. BC024452 mRNA. Translation: AAH24452.1. Different initiation. BC043309 mRNA. Translation: AAH43309.1. BC066780 mRNA. Translation: AAH66780.1.
IPI	IPI00281894. IPI00649750.
RefSeq	NP_082103.1. NM_027827.3.
UniGene	Mm.273958.
3D structure databases
ProteinModelPortal	Q8K4H1.
SMR	Q8K4H1. Positions 20-298.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8K4H1.
Protein family/group databases
MEROPS	S09.977.
Proteomic databases
PRIDE	Q8K4H1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000073388; ENSMUSP00000073102; ENSMUSG00000017718.
GeneID	71562.
KEGG	mmu:71562.
NMPDR	fig|10090.3.peg.25709.
UCSC	uc007moa.2. mouse. uc007mob.2. mouse.
Organism-specific databases
CTD	125061.
MGI	MGI:2448704. Afmid.
Phylogenomic databases
eggNOG	roNOG15097.
GeneTree	ENSGT00390000011093.
HOVERGEN	HBG100436.
InParanoid	Q8K4H1.
OMA	RSGIVEH.
OrthoDB	EOG470THR.
PhylomeDB	Q8K4H1.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15003.
BRENDA	3.5.1.9. 3474.
Reactome	REACT_112621. Metabolism.
Gene expression databases
ArrayExpress	Q8K4H1.
Bgee	Q8K4H1.
CleanEx	MM_AFMID.
Genevestigator	Q8K4H1.
GermOnline	ENSMUSG00000017718. Mus musculus.
Family and domain databases
InterPro	IPR013094. AB_hydrolase_3. [Graphical view]
KO	K01432.
Pfam	PF07859. Abhydrolase_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	334001.
SOURCE	Search...

Entry information

Entry name

AFMID_MOUSE

Accession

Primary (citable) accession number: Q8K4H1
Secondary accession number(s): B1AQK9, Q80XP3, Q8R1K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	October 1, 2002
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program