[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). PubMed=7528745 [NCBI, ExPASy, EBI, Israel, Japan] Hall A.V., Antoniou H., Wang Y., Cheung A.H., Arbus A.M., Olson S.L., Lu W.C., Kau C.-L., Marsden P.A.; "Structural organization of the human neuronal nitric oxide synthase gene (NOS1)."; J. Biol. Chem. 269:33082-33090(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). TISSUE=Cerebellum; PubMed=7515942 [NCBI, ExPASy, EBI, Israel, Japan] Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J., Esumi H.; "Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines."; J. Neurochem. 63:140-145(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=Brain; DOI=10.1016/0014-5793(93)81210-Q; PubMed=7678401 [NCBI, ExPASy, EBI, Israel, Japan] Nakane M., Schmidt H.H.H.W., Pollock J.S., Foerstermann U., Murad F.; "Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle."; FEBS Lett. 316:175-180(1993).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Retina; DOI=10.1007/BF02150230; PubMed=8879752 [NCBI, ExPASy, EBI, Israel, Japan] Park C.-S., Gianotti C., Park R., Krishna G.; "Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina."; Cell. Mol. Neurobiol. 16:499-515(1996).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4). TISSUE=Testis; DOI=10.1074/jbc.272.17.11128; PubMed=9111048 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Goligorsky M.S., Lin M., Wilcox J.N., Marsden P.A.; "A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase."; J. Biol. Chem. 272:11392-11401(1997).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-228; ALA-394; ASP-725; ASP-864 AND ARG-1064. Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]	INVOLVEMENT IN IHPS1 SUSCEPTIBILITY. DOI=10.1073/pnas.0305473101; PubMed=14757827 [NCBI, ExPASy, EBI, Israel, Japan] Saur D., Vanderwinden J.-M., Seidler B., Schmid R.M., De Laet M.-H., Allescher H.-D.; "Single-nucleotide promoter polymorphism alters transcription of neuronal nitric oxide synthase exon 1c in infantile hypertrophic pyloric stenosis."; Proc. Natl. Acad. Sci. U.S.A. 101:1662-1667(2004).

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter.
CATALYTIC ACTIVITY: L-arginine + n NADPH + m O₂ = citrulline + nitric oxide + n NADP⁺.
COFACTOR: Heme group.
COFACTOR: Binds 1 FAD.
COFACTOR: Binds 1 FMN.
COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein. Inhibited by NOSIP.
SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Forms a ternary complex with CAPON and RASD1. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location (By similarity). Interacts with HTR4 (By similarity).
SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein. Cell projection, dendritic spine (By similarity). Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines (By similarity).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing. Isoform 3 is produced by different alternative splicing events implicating either the untranslated exons TEX1 (TN-NOS) or TEX1B (TN-NOSB) leading to a N-terminus truncated protein which possesses enzymatic activity comparable to that of isoform 1. The C-terminal truncated isoform 4 is produced by insertion of the TEX2 exon between exons 3 and 4 of isoform 1, leading to a frameshift and a premature stop codon.

Name	1
Synonyms	N-NOS-1
Isoform ID	P29475-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	N-NOS-2
Isoform ID	P29475-2
Features which should be applied to build the isoform sequence: VSP_003574.

Name	3
Synonyms	TN-NOS, TN-NOSB
Isoform ID	P29475-3
Features which should be applied to build the isoform sequence: VSP_003571.

Name	4
Synonyms	TEX2-insertion
Isoform ID	P29475-4
Features which should be applied to build the isoform sequence: VSP_003572, VSP_003573.

TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed: detected in skeletal muscle and brain, also in testis, lung and kidney, and at low levels in heart, adrenal gland and retina. Not detected in the platelets. Isoform 3 is expressed only in testis. Isoform 4 is detected in testis, skeletal muscle, lung, and kidney, at low levels in the brain, but not in the heart and adrenal gland.
DOMAIN: The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles (By similarity).
DISEASE: Genetic variations in NOS1 gene are associated with susceptibility to infantile hypertrophic pyloric stenosis type 1 (IHPS1) [MIM:179010]. IHPS has an incidence of 1-5 per 1'000 live births in whites and a marked preponderance of males to females (4:1). IHPS is the most frequent disorder requiring surgery in the first year of life. The disorder is characterized by hypertrophy and hyperplasia of the circular muscle layer of the pylorus, leading to persistent vomiting 2-12 weeks after birth. Defective pyloric relaxation and increased pyloric smooth muscle mass have been suggested to be responsible for gastric-outlet obstruction.
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.
SIMILARITY: Contains 1 PDZ (DHR) domain.
WEB RESOURCE: Name=Wikipedia; Note=Nitric oxide synthase entry; URL="http://en.wikipedia.org/wiki/Nitric_oxide_synthase";.

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

U17327; AAA62405.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17326; AAB60654.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17299; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17300; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17301; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17302; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17303; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17304; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17305; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17307; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17308; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17309; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17310; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17311; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17312; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17313; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17314; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17315; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17316; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17317; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17318; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17319; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17320; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17321; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17322; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17323; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17324; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17325; AAB60654.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16408; BAA03895.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L02881; AAA36376.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U31466; AAB49040.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U66362; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AY445095; AAR07069.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

G01946; G01946.

NP_000611.1; -.

3D structure databases

HSSP

P29476; 1QAV. [HSSP ENTRY / PDB]

SMR

P29475; 12-126, 304-723, 968-1402.

ModBase

P29475.

PTM databases

PhosphoSite

P29475; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11229; -.

Polymorphism databases

NIEHS-SNPs

NOS1.

Organism-specific databases

HIX0036725; -.

HGNC:7872; NOS1.

CAB002167; -.

163731; gene. [NCBI / EBI]
179010; phenotype. [NCBI / EBI]

PharmGKB

PA134876543; -.

GeneCards

P29475.

Gene expression databases

ArrayExpress

P29475; -.

CleanEx

HS_NOS1; -.

GermOnline

ENSG00000089250; Homo sapiens.

Ontologies

GO:0042995;	Cellular component: cell projection (inferred from electronic annotation from UniProtKB-KW).
GO:0005856;	Cellular component: cytoskeleton (inferred from sequence or structural similarity from UniProtKB).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0001917;	Cellular component: photoreceptor inner segment (inferred from sequence or structural similarity from UniProtKB).
GO:0042383;	Cellular component: sarcolemma (inferred from direct assay from UniProtKB).
GO:0016529;	Cellular component: sarcoplasmic reticulum (inferred from direct assay from UniProtKB).
GO:0034618;	Molecular function: arginine binding (traceable author statement from UniProtKB).
GO:0046870;	Molecular function: cadmium ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004517;	Molecular function: nitric-oxide synthase activity (inferred from electronic annotation from InterPro).
GO:0034617;	Molecular function: tetrahydrobiopterin binding (non-traceable author statement from UniProtKB).
GO:0006527;	Biological process: arginine catabolic process (inferred by curator from UniProtKB).
GO:0033555;	Biological process: multicellular organismal response to stress (inferred from mutant phenotype from UniProtKB).
GO:0007520;	Biological process: myoblast fusion (traceable author statement from UniProtKB).
GO:0010523;	Biological process: negative regulation of calcium ion transport into cytosol (traceable author statement from UniProtKB).
GO:0042136;	Biological process: neurotransmitter biosynthetic process (traceable author statement from UniProtKB).
GO:0006809;	Biological process: nitric oxide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0045909;	Biological process: positive regulation of vasodilation (inferred from direct assay from UniProtKB).
GO:0055117;	Biological process: regulation of cardiac muscle contraction (traceable author statement from UniProtKB).
GO:0009408;	Biological process: response to heat (inferred from direct assay from UniProtKB).
GO:0001666;	Biological process: response to hypoxia (inferred from expression pattern 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.
IPR001478; PDZ.
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.
PF00595; PDZ; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000333; NOS; 1.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

SMART

SM00228; PDZ; 1.
SMART graphical view of domain structure.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PS50106; PDZ; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000089250; Homo sapiens. [Contig view]

GeneID

4842; -.

KEGG

hsa:4842; -.

Phylogenomic databases

HOGENOM

P29475; -.

HOVERGEN

P29475; -.

Other

DrugBank

DB00155; L-Citrulline.

NextBio

18658; -.

SOURCE

NOS1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Calmodulin-binding; Cell membrane; Cell projection; FAD; FMN; Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1434`	`1434`	`Nitric oxide synthase, brain.`	`PRO_0000170921`
`DOMAIN`	`17 99`	`83`	`PDZ.`
`DOMAIN`	`760 940`	`181`	`Flavodoxin-like.`
`DOMAIN`	`995 1242`	`248`	`FAD-binding FR-type.`
`NP_BIND`	`886 917`	`32`	`FMN (By similarity).`
`NP_BIND`	`1032 1043`	`12`	`FAD (By similarity).`
`NP_BIND`	`1175 1185`	`11`	`FAD (By similarity).`
`NP_BIND`	`1250 1268`	`19`	`NADP (By similarity).`
`NP_BIND`	`1348 1363`	`16`	`NADP (By similarity).`
`REGION`	`1 205`	`205`	`Interaction with NOSIP (By similarity).`
`REGION`	`163 245`	`83`	`PIN (nNOS-inhibiting protein) binding.`
`REGION`	`730 750`	`21`	`Calmodulin-binding (Potential).`
`REGION`	`755 774`	`20`	`Tetrahydrobiopterin-binding (By similarity).`
`METAL`	`420 420`		`Iron (heme axial ligand) (By similarity).`
`VAR_SEQ`	`1 336`		`Missing (in isoform 3).`	`VSP_003571`
`VAR_SEQ`	`285 407`		`PPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLK` `STLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAK` `EFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLK` `DTELI -> MRKLRITEGFGVQRGSHNHPPPQENSPPQRMAAPPSVHAS` `SRSRTGRLRWFSLTPSTLRAHWKRDALSTSAWAPSCILLS` `MQGGLKTSAQKDSSSLSPKSLLINTIHQLKDLAPKPTW` `KGWKR (in isoform 4).`	`VSP_003572`
`VAR_SEQ`	`408 1434`		`Missing (in isoform 4).`	`VSP_003573`
`VAR_SEQ`	`509 613`		`Missing (in isoform 2).`	`VSP_003574`
`VARIANT`	`228 228`	`1`	`P -> S (in dbSNP:rs9658279 [NCBI]).`	`VAR_018948`
`VARIANT`	`394 394`	`1`	`D -> A (in dbSNP:rs9658356 [NCBI]).`	`VAR_018949 [3D]`
`VARIANT`	`725 725`	`1`	`N -> D (in dbSNP:rs9658403 [NCBI]).`	`VAR_018950`
`VARIANT`	`864 864`	`1`	`G -> D (in dbSNP:rs9658445 [NCBI]).`	`VAR_018951`
`VARIANT`	`1064 1064`	`1`	`Q -> R (in dbSNP:rs9658482 [NCBI]).`	`VAR_018952`
`CONFLICT`	`131 131`		`K -> E (in Ref. 4; AAB49040).`
`CONFLICT`	`178 184`		`LAPRPPG -> WPQAPR (in Ref. 3 and 4).`
`CONFLICT`	`492 493`		`QP -> HR (in Ref. 3; AAA36376).`
`CONFLICT`	`549 549`		`V -> L (in Ref. 3; AAA36376).`
`CONFLICT`	`563 563`		`G -> A (in Ref. 3; AAA36376).`
`CONFLICT`	`1407 1407`		`Y -> I (in Ref. 3; AAA36376).`

Sequence information

Length: 1434 AA [This is the length of the unprocessed precursor]

Molecular weight: 160970 Da [This is the MW of the unprocessed precursor]

CRC64: 99235793B953BF37 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 

        70         80         90        100        110        120 
GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 

       130        140        150        160        170        180 
RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD GASGPGNGPQ HAYDDGQEAG SLPHANGLAP 

       190        200        210        220        230        240 
RPPGQDPAKK ATRVSLQGRG ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV 

       250        260        270        280        290        300 
DRDLDGKSHK PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS 

       310        320        330        340        350        360 
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP EDVRTKGQLF 

       370        380        390        400        410        420 
PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ LKDTELIYGA KHAWRNASRC 

       430        440        450        460        470        480 
VGRIQWSKLQ VFDARDCTTA HGMFNYICNH VKYATNKGNL RSAITIFPQR TDGKHDFRVW 

       490        500        510        520        530        540 
NSQLIRYAGY KQPDGSTLGD PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ 

       550        560        570        580        590        600 
IPPELVLEVP IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV 

       610        620        630        640        650        660 
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK VTIVDHHSAT 

       670        680        690        700        710        720 
ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM LNYRLTPSFE YQPDPWNTHV 

       730        740        750        760        770        780 
WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM GQAMAKRVKA TILYATETGK SQAYAKTLCE 

       790        800        810        820        830        840 
IFKHAFDAKV MSMEEYDIVH LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ 

       850        860        870        880        890        900 
EERKSYKVRF NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF 

       910        920        930        940        950        960 
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG DDVNIEKANN 

       970        980        990       1000       1010       1020 
SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA RLLSRQNLQS PKSSRSTIFV 

      1030       1040       1050       1060       1070       1080 
RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN ALIERLEDAP PVNQMVKVEL LEERNTALGV 

      1090       1100       1110       1120       1130       1140 
ISNWTDELRL PPCTIFQAFK YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY 

      1150       1160       1170       1180       1190       1200 
EEWKWGKNPT IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV 

      1210       1220       1230       1240       1250       1260 
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI LVGPGTGIAP 

      1270       1280       1290       1300       1310       1320 
FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE TLQAKNKGVF RELYTAYSRE 

      1330       1340       1350       1360       1370       1380 
PDKPKKYVQD ILQEQLAESV YRALKEQGGH IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE 

      1390       1400       1410       1420       1430 
DAGVFISRMR DDNRYHEDIF GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS

P29475 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools