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O09046 (OXLA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=LAAO
Short name=LAO
EC=1.4.3.2
Alternative name(s):
Interleukin-4-induced protein 1
Short name=IL4-induced protein 1
Protein Fig-1
Short name=mFIG1
Gene names
Name:Il4i1
Synonyms:Fig1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lysosomal L-amino-acid oxidase with highest specific activity with phenylalanine. May play a role in lysosomal antigen processing and presentation. Ref.6

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD.

Subcellular location

Isoform 1: Lysosome Ref.6.

Isoform 2: Lysosome Ref.6.

Tissue specificity

Isoform 1 primarily found in immune tissues, mostly in B-lymphocytes. Isoform 2 restricted to the testis, predominantly in Sertoli cells at the periphery of the ducts, and the brain, including Purkinje cells, hippocampus and mitral cells in the olfactory bulb. No isoform 2 expression in fetal tissues. Ref.7

Induction

By interleukin-4.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=6.5 mM for phenylalanine (at 37 degrees Celsius)

Vmax=0.0099 nmol/min/mg enzyme toward phenylalanine (at 37 degrees Celsius)

pH dependence:

Optimum pH is 4.0.

Sequence caution

The sequence BAB29253.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityAlternative promoter usage
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processaromatic amino acid family metabolic process

Inferred from direct assay Ref.6. Source: MGI

   Cellular componentlysosome

Inferred from direct assay Ref.6. Source: MGI

   Molecular functionL-amino-acid oxidase activity

Inferred from direct assay Ref.6. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: O09046-1)

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: O09046-2)

Also known as: IL4I1_2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAGLA → MGARRAPQRPPCT
Note: Uses the promoter of the upstream NUP62 gene and shares the first 2 non-coding exons with NUP62.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 630609L-amino-acid oxidase
PRO_0000001711

Regions

Nucleotide binding114 – 1152FAD By similarity
Nucleotide binding488 – 4914FAD By similarity

Sites

Binding site881FAD By similarity
Binding site961FAD By similarity
Binding site1151Substrate By similarity
Binding site2861FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3951Substrate By similarity
Binding site4791FAD By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 198 By similarity

Natural variations

Alternative sequence1 – 55MAGLA → MGARRAPQRPPCT in isoform 2.
VSP_017174

Experimental info

Sequence conflict121A → V in AAO17038. Ref.2
Sequence conflict121A → V in AAO17039. Ref.2
Sequence conflict561S → L in AAO65453. Ref.2
Sequence conflict561S → L in AAS00457. Ref.2
Sequence conflict1841M → V in BAE30174. Ref.3
Sequence conflict1841M → V in BAE31293. Ref.3
Sequence conflict3851R → Q in AAO23118. Ref.2
Sequence conflict3851R → Q in BAE21502. Ref.3
Sequence conflict3851R → Q in BAE29676. Ref.3
Sequence conflict3851R → Q in BAE30047. Ref.3
Sequence conflict3851R → Q in BAE30174. Ref.3
Sequence conflict3851R → Q in BAE31293. Ref.3
Sequence conflict4541Q → R in BAE21502. Ref.3
Sequence conflict5371E → Q in BAE21502. Ref.3
Sequence conflict5511P → L in AAO17038. Ref.2
Sequence conflict5511P → L in AAO17039. Ref.2
Sequence conflict5681A → M in AAO17038. Ref.2
Sequence conflict5681A → M in AAO17039. Ref.2
Sequence conflict598 – 63033PSEHV…VGDHS → LRSMYRCMGKSSLSGMVMGD LAPRKCTEWGTTPNRKEEVS TQLLSQPSSGQTDHLH in BAB29253. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: A674C5D60D89A071

FASTA63070,191
        10         20         30         40         50         60 
MAGLALRLVL AATLLGLAGS LDWKAASSLN PIEKCMEDHD YEQLLKVVTL GLNRTSKPQK 

        70         80         90        100        110        120 
VVVVGAGVAG LVAAKMLSDA GHKVTILEAD NRIGGRIFTF RDEKTGWIGE LGAMRMPSSH 

       130        140        150        160        170        180 
RILHKLCRTL GLNLTQFTQY DENTWTEVHN VKLRNYVVEK MPEKLGYNLN NRERGHSPED 

       190        200        210        220        230        240 
IYQMALNKAF KDLKALGCKK AMNKFNKHTL LEYLLEEGNL SRPAVQLLGD VMSEEGFFYL 

       250        260        270        280        290        300 
SFAEALRAHA CLSDRLRYSR IVGGWDLLPR ALLSSLSGAL LLNAPVVSIT QGRNDVRVHI 

       310        320        330        340        350        360 
ATSLHSEKTL TADVVLLTAS GPALQRITFS PPLTRKRQEA LRALHYVAAS KVFLSFRRPF 

       370        380        390        400        410        420 
WHEEHIEGGH SNTDRPSRLI FYPARGEGSL LLASYTWSDA AAPFAGLSTD QTLRLVLQDV 

       430        440        450        460        470        480 
AALHGPVVFR LWDGRGVVKR WAEDPHSQGG FVVQPPLYGR EAEDYDWSAP FGRIYFAGEH 

       490        500        510        520        530        540 
TALPHGWVET AVKSGLRAAV RINNNYGYGE VDPQMMEHAY AEANYLDQYP EGERPEEQQA 

       550        560        570        580        590        600 
REEVSPDEQE PSHKHLLVET SPEGQQHAFV EAIPELQGHV FVETVPQEKG HAHQNIYPSE 

       610        620        630 
HVQVHGEVIP EWHGHGGSGT PQMHRVGDHS

« Hide

Isoform 2 (IL4I1_2) [UniParc].

Checksum: D0425122748E7609
Show »

FASTA63871,170

References

« Hide 'large scale' references
[1]"Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA representational difference analysis."
Chu C.C., Paul W.E.
Proc. Natl. Acad. Sci. U.S.A. 94:2507-2512(1997) [PubMed: 9122225] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Strain: BALB/c and CBA/J.
[2]"Interleukin-four induced gene-1 polymorphisms correlate with Sle3 autoimmune susceptibility."
Chu C.C., Kim J.A., Gupta N., Yuen G.J., Thomas R.R., George J., Hsueh K.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Strain: CBA/J, MRL and NZW.
[3]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryonic head, Spleen and Testis.
[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] (ISOFORM 1).
[5]"Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
Chu C.C., Paul W.E.
Mol. Immunol. 35:487-502(1998) [PubMed: 9798653] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-289.
Strain: BALB/c.
Tissue: Spleen.
[6]"IL-4-induced gene-1 is a leukocyte L-amino acid oxidase with an unusual acidic pH preference and lysosomal localization."
Mason J.M., Naidu M.D., Barcia M., Porti D., Chavan S.S., Chu C.C.
J. Immunol. 173:4561-4567(2004) [PubMed: 15383589] [Abstract]
Cited for: CHARACTERIZATION, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION.
[7]"Alternative pre-mRNA processing regulates cell-type specific expression of the IL4l1 and NUP62 genes."
Wiemann S., Kolb-Kokocinski A., Poustka A.
BMC Biol. 3:16-16(2005) [PubMed: 16029492] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U70429 mRNA. Translation: AAB51353.1.
U70430 Genomic RNA. Translation: AAB51354.1.
AF538041 Genomic DNA. Translation: AAM15529.1.
AY442170 Genomic DNA. Translation: AAM15530.2.
AY157537 Genomic DNA. Translation: AAO17038.1.
AY157538 mRNA. Translation: AAO17039.1.
AY161348 Genomic DNA. Translation: AAO23118.1.
AY178834 Genomic DNA. Translation: AAO65453.1.
AY442343 Genomic DNA. Translation: AAS00457.1.
AK014297 mRNA. Translation: BAB29253.1. Different initiation.
AK133082 mRNA. Translation: BAE21502.1.
AK150582 mRNA. Translation: BAE29676.1.
AK151030 mRNA. Translation: BAE30047.1.
AK151171 mRNA. Translation: BAE30174.1.
AK152538 mRNA. Translation: BAE31293.1.
AK172393 mRNA. Translation: BAE42981.1.
BC115960 mRNA. Translation: AAI15961.1.
U89428 Transcribed RNA. Translation: AAC36534.1.
U89429 mRNA. Translation: AAC36535.1.
IPIIPI00113800.
IPI00759856.
RefSeqNP_001164495.1. NM_001171024.1.
NP_034345.2. NM_010215.3.
UniGeneMm.2565.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I8Wmodel-@30-502[»]
ProteinModelPortalO09046.
SMRO09046. Positions 28-505.
ModBaseSearch...

Protein-protein interaction databases

STRINGO09046.

Proteomic databases

PRIDEO09046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033015; ENSMUSP00000033015; ENSMUSG00000074141.
ENSMUST00000107890; ENSMUSP00000103522; ENSMUSG00000074141.
GeneID100328588.
14204.
KEGGmmu:100328588.
mmu:14204.

Organism-specific databases

CTD100328588.
259307.
MGIMGI:109552. Il4i1.

Phylogenomic databases

eggNOGroNOG08409.
GeneTreeENSGT00530000063101.
HOVERGENHBG005729.
OrthoDBEOG43BMP6.

Gene expression databases

ArrayExpressO09046.
BgeeO09046.
CleanExMM_IL4I1.
GenevestigatorO09046.
GermOnlineENSMUSG00000074141. Mus musculus.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
KOK03334.
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

NextBio285446.
SOURCESearch...

Entry information

Entry nameOXLA_MOUSE
AccessionPrimary (citable) accession number: O09046
Secondary accession number(s): Q1LZI6 expand/collapse secondary AC list , Q3T9N9, Q3U7S6, Q3V0K2, Q6Y632, Q6YBV6, Q6YDI8, Q8R2G8, Q9CXK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: November 16, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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