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UniProtKB/Swiss-Prot entry P29477


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NOS2_MOUSE
Primary accession number P29477
Secondary accession numbers O70515 O70516 Q5SXT3 Q6P6A0 Q8R410
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 102)
Name and origin of the protein
Protein name Nitric oxide synthase, inducible
Synonyms EC 1.14.13.39
Inducible NO synthase
Inducible NOS
iNOS
NOS type II
Macrophage NOS
MAC-NOS
Gene name
Name: Nos2
Synonyms: Inosl
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1373522 [NCBI, ExPASy, EBI, Israel, Japan]
Xie Q.-W., Cho H.J., Calaycay J., Mumford R.A., Swiderek K.M., Lee T.D., Ding A., Troso T., Nathan C.;
"Cloning and characterization of inducible nitric oxide synthase from mouse macrophages.";
Science 256:225-228(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1379716 [NCBI, ExPASy, EBI, Israel, Japan]
Lowenstein C.J., Glatt C.S., Bredt D.S., Snyder S.H.;
"Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 89:6711-6715(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1372907 [NCBI, ExPASy, EBI, Israel, Japan]
Lyons C.R., Orloff G.J., Cunningham J.M.;
"Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line.";
J. Biol. Chem. 267:6370-6374(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7503239 [NCBI, ExPASy, EBI, Israel, Japan]
Kone B.C., Schwoebel J., Turner P., Mohaupt M.G., Cangro C.B.;
"Role of NF-kappa B in the regulation of inducible nitric oxide synthase in an MTAL cell line.";
Am. J. Physiol. 269:F718-F729(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-211; LEU-967 AND PHE-968.
STRAIN=B10.S/J, BALB/cByJ, DBA/2J, NOD/LtJ, and SJL/J;
TISSUE=Spleen;
PubMed=10438970 [NCBI, ExPASy, EBI, Israel, Japan]
Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., Blankenhorn E.P.;
"Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for eae7, a locus controlling susceptibility to monophasic remitting/nonrelapsing experimental allergic encephalomyelitis.";
J. Immunol. 163:2262-2266(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CD-1;
Coge F., Levacher B., Rique H., Leopold O., Boutin J.A., Galizzi J.-P.;
"Genomic structure of the murine inducible nitric oxide synthase (i-NOS) gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR;
Hagiwara K., Endo Y., Xin H., Takahashi M., Huqun X., Nukiwa T.;
"Mouse inducible nitric oxide synthase mRNA.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
EFFECT OF ASPIRIN.
TISSUE=Macrophage;
PubMed=7544010 [NCBI, ExPASy, EBI, Israel, Japan]
Amin A.R., Vyas P., Attur M., Leszczynska-Piziak J., Patel I.R., Weissmann G., Abramson S.B.;
"The mode of action of aspirin-like drugs: effect on inducible nitric oxide synthase.";
Proc. Natl. Acad. Sci. U.S.A. 92:7926-7930(1995).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 116-496.
DOI=10.1126/science.278.5337.425; PubMed=9334294 [NCBI, ExPASy, EBI, Israel, Japan]
Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D., Stuehr D.J., Tainer J.A.;
"The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.";
Science 278:425-431(1997).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 77-496.
DOI=10.1126/science.279.5359.2121; PubMed=9516116 [NCBI, ExPASy, EBI, Israel, Japan]
Crane B.R., Arvai A.S., Ghosh D.K., Wu C., Getzoff E.D., Stuehr D.J., Tainer J.A.;
"Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.";
Science 279:2121-2126(1998).
[13]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
DOI=10.1093/emboj/18.22.6260; PubMed=10562538 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh D.K., Crane B.R., Ghosh S., Wolan D., Gachhui R., Crooks C., Presta A., Tainer J.A., Getzoff E.D., Stuehr D.J.;
"Inducible nitric oxide synthase: role of the N-terminal beta-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction.";
EMBO J. 18:6260-6270(1999).
[14]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-499.
DOI=10.1093/emboj/18.22.6271; PubMed=10562539 [NCBI, ExPASy, EBI, Israel, Japan]
Crane B.R., Rosenfeld R.J., Arvai A.S., Ghosh D.K., Ghosh S., Tainer J.A., Stuehr D.J., Getzoff E.D.;
"N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization.";
EMBO J. 18:6271-6281(1999).
[15]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
DOI=10.1021/bi992409a; PubMed=10769116 [NCBI, ExPASy, EBI, Israel, Japan]
Crane B.R., Arvai A.S., Ghosh S., Getzoff E.D., Stuehr D.J., Tainer J.A.;
"Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins.";
Biochemistry 39:4608-4621(2000).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF TRP-457 MUTANTS.
DOI=10.1021/bi011183k; PubMed=11669619 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A., Getzoff E.D.;
"Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457.";
Biochemistry 40:12826-12832(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
DOI=10.1021/bi026313j; PubMed=12437348 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenfeld R.J., Garcin E.D., Panda K., Andersson G., Aberg A., Wallace A.V., Morris G.M., Olson A.J., Stuehr D.J., Tainer J.A., Getzoff E.D.;
"Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency.";
Biochemistry 41:13915-13925(2002).
[18]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-495.
DOI=10.1016/S0003-9861(02)00555-6; PubMed=12464241 [NCBI, ExPASy, EBI, Israel, Japan]
Fedorov R., Ghosh D.K., Schlichting I.;
"Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes.";
Arch. Biochem. Biophys. 409:25-31(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M87039; AAA39315.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M92649; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
M84373; AAA39834.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43428; AAC52356.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065919; AAC17914.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065920; AAC17915.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065921; AAC17916.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065922; AAC17917.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065923; AAC17918.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF427516; AAL24076.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY090567; AAM11887.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592185; CAI25275.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062378; AAH62378.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43271; A43271.
RefSeq NP_035057.1; -.
UniGene Mm.2893
3D structure databases
PDB
1DD7; X-ray; 2.25 A; A=114-498.[ExPASy / RCSB / EBI]
1DF1; X-ray; 2.35 A; A/B=77-499.[ExPASy / RCSB / EBI]
1DWV; X-ray; 2.35 A; A/B=77-496.[ExPASy / RCSB / EBI]
1DWW; X-ray; 2.35 A; A/B=77-496.[ExPASy / RCSB / EBI]
1DWX; X-ray; 2.60 A; A/B=77-496.[ExPASy / RCSB / EBI]
1JWJ; X-ray; 2.60 A; A/B=66-498.[ExPASy / RCSB / EBI]
1JWK; X-ray; 2.30 A; A/B=66-498.[ExPASy / RCSB / EBI]
1M8D; X-ray; 2.35 A; A/B=65-498.[ExPASy / RCSB / EBI]
1M8E; X-ray; 2.90 A; A/B=65-498.[ExPASy / RCSB / EBI]
1M8H; X-ray; 2.85 A; A/B=65-498.[ExPASy / RCSB / EBI]
1M8I; X-ray; 2.70 A; A/B=65-498.[ExPASy / RCSB / EBI]
1M9T; X-ray; 2.40 A; A/B=65-498.[ExPASy / RCSB / EBI]
1N2N; X-ray; 2.40 A; A/B=77-495.[ExPASy / RCSB / EBI]
1NOC; X-ray; 2.60 A; A=115-498.[ExPASy / RCSB / EBI]
1NOD; X-ray; 2.60 A; A/B=77-499.[ExPASy / RCSB / EBI]
1NOS; X-ray; 2.10 A; A=115-498.[ExPASy / RCSB / EBI]
1QOM; X-ray; 2.70 A; A/B=65-498.[ExPASy / RCSB / EBI]
1QW4; X-ray; 2.40 A; A/B=77-495.[ExPASy / RCSB / EBI]
1QW5; X-ray; 2.70 A; A/B=77-495.[ExPASy / RCSB / EBI]
1R35; X-ray; 2.30 A; A/B=66-498.[ExPASy / RCSB / EBI]
1VAF; X-ray; 2.90 A; A/B=77-495.[ExPASy / RCSB / EBI]
2BHJ; X-ray; 3.20 A; A=77-498.[ExPASy / RCSB / EBI]
2NOD; X-ray; 2.60 A; A/B=77-499.[ExPASy / RCSB / EBI]
2NOS; X-ray; 2.30 A; A=115-498.[ExPASy / RCSB / EBI]
2ORO; X-ray; 2.00 A; A=114-498.[ExPASy / RCSB / EBI]
2ORP; X-ray; 1.97 A; A=114-498.[ExPASy / RCSB / EBI]
2ORQ; X-ray; 2.10 A; A=114-498.[ExPASy / RCSB / EBI]
2ORR; X-ray; 2.00 A; A=114-498.[ExPASy / RCSB / EBI]
2ORS; X-ray; 2.00 A; A=114-498.[ExPASy / RCSB / EBI]
2ORT; X-ray; 1.87 A; A=114-498.[ExPASy / RCSB / EBI]
3NOD; X-ray; 2.70 A; A/B=77-499.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DD7; -.
1DF1; -.
1DWV; -.
1DWW; -.
1DWX; -.
1JWJ; -.
1JWK; -.
1M8D; -.
1M8E; -.
1M8H; -.
1M8I; -.
1M9T; -.
1N2N; -.
1NOC; -.
1NOD; -.
1NOS; -.
1QOM; -.
1QW4; -.
1QW5; -.
1R35; -.
1VAF; -.
2BHJ; -.
2NOD; -.
2NOS; -.
2ORO; -.
2ORP; -.
2ORQ; -.
2ORR; -.
2ORS; -.
2ORT; -.
3NOD; -.
ModBase P29477.
Protein-protein interaction databases
IntAct P29477; -.
PTM databases
PhosphoSite P29477; -.
Organism-specific databases
MGI MGI:97361; Nos2.
Gene expression databases
ArrayExpress P29477; -.
CleanEx MM_NOS2; -.
GermOnline ENSMUSG00000020826; Mus musculus.
Ontologies
GO
GO:0030863; Cellular component: cortical cytoskeleton (inferred from direct assay from MGI).
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from MGI).
GO:0034618; Molecular function: arginine binding (inferred from direct assay from UniProtKB).
GO:0005516; Molecular function: calmodulin binding (traceable author statement from UniProtKB).
GO:0050660; Molecular function: FAD binding (inferred from direct assay from UniProtKB).
GO:0010181; Molecular function: FMN binding (inferred from direct assay from UniProtKB).
GO:0020037; Molecular function: heme binding (inferred from direct assay from UniProtKB).
GO:0004517; Molecular function: nitric-oxide synthase activity (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from MGI).
GO:0034617; Molecular function: tetrahydrobiopterin binding (inferred from direct assay from UniProtKB).
GO:0006527; Biological process: arginine catabolic process (inferred from direct assay from UniProtKB).
GO:0042742; Biological process: defense response to bacterium (inferred from sequence or structural similarity from UniProtKB).
GO:0006954; Biological process: inflammatory response (traceable author statement from UniProtKB).
GO:0006809; Biological process: nitric oxide biosynthetic process (inferred from direct assay from MGI).
GO:0001666; Biological process: response to hypoxia (inferred from direct assay from MGI).
GO:0006801; Biological process: superoxide metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000333; NOS; 1.
PRINTS PR00369; FLAVODOXIN.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29477.
Genome annotation databases
Ensembl ENSMUSG00000020826; Mus musculus. [Contig view]
GeneID 18126; -.
KEGG mmu:18126; -.
Phylogenomic databases
HOGENOM P29477; -.
HOVERGEN P29477; -.
Other
LinkHub P29477; -.
SOURCE Nos2; Mus musculus.
ProtoNet P29477.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calmodulin-binding; FAD; FMN; Heme; Iron; Metal-binding; NADP; Oxidoreductase; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1144  1144     Nitric oxide synthase, inducible. PRO_0000170934
DOMAIN   533    671  139     Flavodoxin-like. 
DOMAIN   724    964  241     FAD-binding FR-type. 
NP_BIND   617    648  32     FMN (By similarity). 
NP_BIND   761    772  12     FAD (By similarity). 
NP_BIND   897    907  11     FAD (By similarity). 
NP_BIND   972    990  19     NADP (By similarity). 
NP_BIND   1070   1085  16     NADP (By similarity). 
REGION   503    523  21     Calmodulin-binding (Potential). 
METAL   104    104        Zinc. 
METAL   109    109        Zinc. 
METAL   194    194        Iron (heme axial ligand). 
VARIANT   211    211  1     C -> R (in strain: NOD/LtJ). 
VARIANT   967    967  1     P -> L (in strain: SJL/J). 
VARIANT   968    968  1     S -> F (in strain: BALB/CBYJ). 
CONFLICT   19     19        K -> T (in Ref. 4; AAC52356). 
CONFLICT   72     72        T -> TP (in Ref. 7 and 9). 
CONFLICT   191    191        A -> V (in Ref. 2; M92649). 
CONFLICT   245    245        S -> T (in Ref. 7 and 9). 
CONFLICT   844    844        A -> G (in Ref. 2; M92649). 
CONFLICT   1075   1075        I -> V (in Ref. 9; AAH62378). 
STRAND   79     83  5      
TURN   84     86  3      
STRAND   89     92  4      
HELIX   94     97  4      
HELIX   130    146  17      
HELIX   153    170  18      
HELIX   177    189  13      
HELIX   195    199  5      
STRAND   204    207  4      
HELIX   214    229  16      
HELIX   230    232  3      
STRAND   237    240  4      
STRAND   245    249  5      
STRAND   255    259  5      
HELIX   275    277  3      
HELIX   278    287  10      
STRAND   301    304  4      
STRAND   311    313  3      
HELIX   317    319  3      
STRAND   322    324  3      
STRAND   339    342  4      
STRAND   350    353  4      
STRAND   356    359  4      
HELIX   414    422  9      
HELIX   430    442  13      
STRAND   480    485  6      
HELIX   489    491  3      
Sequence information
Length: 1144 AA [This is the length of the unprocessed precursor] Molecular weight: 130575 Da [This is the MW of the unprocessed precursor] CRC64: 0735BE676113457F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ 

        70         80         90        100        110        120 
NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT 

       130        140        150        160        170        180 
RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL 

       190        200        210        220        230        240 
IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV 

       250        260        270        280        290        300 
FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP 

       310        320        330        340        350        360 
LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA 

       370        380        390        400        410        420 
CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF 

       430        440        450        460        470        480 
QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS 

       490        500        510        520        530        540 
PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE 

       550        560        570        580        590        600 
TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK 

       610        620        630        640        650        660 
KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE 

       670        680        690        700        710        720 
DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS 

       730        740        750        760        770        780 
IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG 

       790        800        810        820        830        840 
ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL 

       850        860        870        880        890        900 
ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR 

       910        920        930        940        950        960 
YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG 

       970        980        990       1000       1010       1020 
FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ 

      1030       1040       1050       1060       1070       1080 
EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR 

      1090       1100       1110       1120       1130       1140 
MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK 


ATRL 

P29477 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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