Reviewed, UniProtKB/Swiss-Prot P29476 (NOS1_RAT)

Names and origin

Protein names

Recommended name:
    Nitric oxide synthase, brain
    EC=1.14.13.39
Alternative name(s):
    BNOS
    NOS type I
    Neuronal NOS
      Short name=N-NOS
      Short name=nNOS
    Constitutive NOS
    NC-NOS

Gene names

Name:	Nos1
Synonyms:	Bnos

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.
Catalytic activity	L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.
Cofactor	Heme group By similarity. Binds 1 FAD By similarity. Binds 1 FMN By similarity. Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme By similarity.
Enzyme regulation	Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein By similarity. Inhibited by NOSIP.
Subunit structure	Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON By similarity. 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. Interacts with HTR4 By similarity.
Subcellular location	Cell membrane › sarcolemma; Peripheral membrane protein By similarity. 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 By similarity. In neurons, enriched in dendritic spines.
Tissue specificity	Isoform N-NOS-1 is expressed in brain and colorectum. Found in the Auerbach's plexus of the enteric nervous system. Isoform PNNOS is expressed in the penis, urethra, prostate, and skeletal muscle, and coexists with the cerebellar nnos in the pelvic plexus, bladder and liver, and is detectable in the cerebellum. Ref.3
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.
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD arginine catabolic process Inferred from direct assay. Source: UniProtKB negative regulation of blood pressure Inferred from mutant phenotype. Source: RGD negative regulation of heart contraction Inferred from mutant phenotype. Source: RGD negative regulation of insulin secretion Inferred from mutant phenotype. Source: RGD nitric oxide biosynthetic process Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of vasodilation Inferred from mutant phenotype. Source: RGD regulation of sensory perception of pain Inferred from mutant phenotype. Source: RGD response to estrogen stimulus Inferred from direct assay. Source: RGD response to ethanol Inferred from expression pattern. Source: RGD response to heat Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: UniProtKB response to organic cyclic substance Inferred from expression pattern. Source: RGD response to organic nitrogen Inferred from expression pattern. Source: RGD response to vitamin E Inferred from expression pattern. Source: RGD
Cellular component	azurophil granule Inferred from direct assay. Source: RGD cytosol Inferred from direct assay. Source: RGD dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from direct assay. Source: RGD nuclear membrane Inferred from direct assay. Source: RGD perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB photoreceptor inner segment Inferred from direct assay. Source: UniProtKB sarcolemma Inferred from direct assay. Source: UniProtKB synapse Inferred from direct assay. Source: RGD
Molecular function	FAD binding Inferred from direct assay. Source: UniProtKB FMN binding Inferred from direct assay. Source: UniProtKB NADP or NADPH binding Inferred from direct assay. Source: UniProtKB amino acid binding Inferred by curator. Source: UniProtKB cadmium ion binding Inferred from direct assay. Source: UniProtKB calmodulin binding Inferred from direct assay. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro enzyme binding Inferred from physical interaction. Source: RGD heme binding Inferred from direct assay. Source: UniProtKB nitric-oxide synthase activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlg4	P31016	1	EBI-349460,EBI-375655
Snta1	Q61234	1	EBI-349460,EBI-295952	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform N-NOS-1 (identifier: P29476-1)

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 N-NOS-2 (identifier: P29476-2)

The sequence of this isoform differs from the canonical sequence as follows:
     504-608: Missing.

Isoform PNNOS (identifier: P29476-3)

The sequence of this isoform differs from the canonical sequence as follows:
     839-839: K → KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1429

1429

Nitric oxide synthase, brain

PRO_0000170924

Regions

Domain

17 – 99

83

PDZ

Domain

755 – 935

181

Flavodoxin-like

Domain

990 – 1237

248

FAD-binding FR-type

Nucleotide binding

881 – 912

32

FMN By similarity

Nucleotide binding

1027 – 1038

12

FAD By similarity

Nucleotide binding

1170 – 1180

11

FAD By similarity

Nucleotide binding

1245 – 1263

19

NADP By similarity

Nucleotide binding

1343 – 1358

16

NADP By similarity

Region

1 – 200

200

Interaction with NOSIP

Region

163 – 240

78

PIN (nNOS-inhibiting protein) binding By similarity

Region

725 – 745

21

Calmodulin-binding Potential

Region

750 – 769

20

Tetrahydrobiopterin-binding

Sites

Metal binding

415

1

Iron (heme axial ligand) By similarity

Binding site

588

1

Substrate

Natural variations

Alternative sequence

504 – 608

105

Missing in isoform N-NOS-2.

VSP_003580

Alternative sequence

839

1

K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS.

VSP_003581

Experimental info

Mutagenesis

588

1

Y → F: No decrease in activity. Ref.5

Mutagenesis

588

1

Y → H: 50% decrease of activity. Ref.5

Mutagenesis

588

1

Y → S: 30% decrease of activity. Ref.5

Sequence conflict

269

1

I → V Ref.2

Sequence conflict

269

1

I → V Ref.3

Sequence conflict

953

1

P → A Ref.2

Sequence conflict

953

1

P → A Ref.3

Sequence conflict

1008

1

F → S in AAC52782. Ref.2

Sequence conflict

1311

1

A → V in AAC52782. Ref.2

Secondary structure

1

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1429

Helix Strand Turn

Details...

Beta strand

15 – 21

7

Turn

24 – 26

3

Beta strand

29 – 34

6

Beta strand

36 – 39

4

Beta strand

41 – 46

6

Helix

51 – 55

5

Beta strand

63 – 67

5

Helix

77 – 86

10

Beta strand

89 – 98

10

Beta strand

103 – 111

9

Beta strand

117 – 124

8

Beta strand

301 – 305

5

Turn

306 – 308

3

Beta strand

311 – 314

4

Helix

316 – 319

4

Helix

351 – 368

18

Helix

375 – 391

17

Helix

398 – 410

13

Helix

418 – 423

6

Beta strand

425 – 428

4

Helix

435 – 450

16

Helix

451 – 453

3

Beta strand

458 – 461

4

Beta strand

466 – 470

5

Beta strand

476 – 480

5

Beta strand

484 – 486

3

Beta strand

492 – 494

3

Helix

496 – 498

3

Helix

499 – 508

10

Beta strand

522 – 525

4

Beta strand

532 – 534

3

Helix

538 – 540

3

Beta strand

543 – 545

3

Helix

554 – 557

4

Beta strand

560 – 563

4

Beta strand

571 – 574

4

Beta strand

577 – 580

4

Helix

590 – 594

5

Helix

596 – 599

4

Turn

601 – 604

4

Helix

607 – 612

6

Helix

621 – 623

3

Helix

625 – 643

19

Helix

651 – 669

19

Helix

676 – 679

4

Beta strand

682 – 684

3

Helix

685 – 687

3

Helix

689 – 692

4

Beta strand

701 – 705

5

Helix

710 – 712

3

Beta strand

754 – 760

7

Beta strand

762 – 764

3

Helix

765 – 777

13

Turn

778 – 780

3

Beta strand

781 – 787

7

Turn

788 – 790

3

Helix

796 – 798

3

Beta strand

800 – 806

7

Turn

810 – 812

3

Helix

816 – 818

3

Helix

819 – 828

10

Helix

841 – 844

4

Turn

873 – 876

4

Beta strand

878 – 885

8

Beta strand

889 – 891

3

Helix

894 – 905

12

Beta strand

909 – 912

4

Beta strand

915 – 918

4

Turn

919 – 922

4

Helix

923 – 942

20

Beta strand

946 – 948

3

Beta strand

968 – 973

6

Helix

980 – 988

9

Beta strand

993 – 1002

10

Beta strand

1012 – 1018

7

Helix

1023 – 1025

3

Beta strand

1032 – 1035

4

Helix

1041 – 1048

8

Beta strand

1051 – 1053

3

Beta strand

1061 – 1072

12

Beta strand

1076 – 1081

6

Helix

1090 – 1096

7

Helix

1106 – 1113

8

Helix

1119 – 1128

10

Helix

1133 – 1142

10

Helix

1146 – 1152

7

Helix

1160 – 1166

7

Beta strand

1173 – 1176

4

Turn

1181 – 1183

3

Beta strand

1187 – 1193

7

Beta strand

1196 – 1198

3

Helix

1200 – 1202

3

Beta strand

1206 – 1208

3

Helix

1210 – 1215

6

Beta strand

1223 – 1229

7

Beta strand

1244 – 1247

4

Helix

1250 – 1253

4

Helix

1254 – 1270

17

Beta strand

1277 – 1284

8

Turn

1286 – 1288

3

Helix

1293 – 1301

9

Beta strand

1304 – 1314

11

Helix

1323 – 1330

8

Helix

1332 – 1340

9

Beta strand

1345 – 1350

6

Helix

1352 – 1369

18

Helix

1374 – 1386

13

Beta strand

1390 – 1394

5

Helix

1401 – 1411

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform N-NOS-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 7255C5AE165200F5	FASTA	1,429	160,559
	10 20 30 40 50 60 MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 70 80 90 100 110 120 GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 130 140 150 160 170 180 RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI 190 200 210 220 230 240 DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD 250 260 270 280 290 300 GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF 310 320 330 340 350 360 LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE 370 380 390 400 410 420 FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ 430 440 450 460 470 480 WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI 490 500 510 520 530 540 RYAGYKQPDG STLGDPANVQ FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL 550 560 570 580 590 600 VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 610 620 630 640 650 660 NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK 670 680 690 700 710 720 HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN 730 740 750 760 770 780 GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA 790 800 810 820 830 840 FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS 850 860 870 880 890 900 YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD 910 920 930 940 950 960 TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKPNNSLISN 970 980 990 1000 1010 1020 DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR QNLQSPKFSR STIFVRLHTN 1030 1040 1050 1060 1070 1080 GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK 1090 1100 1110 1120 1130 1140 DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW 1150 1160 1170 1180 1190 1200 GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR 1210 1220 1230 1240 1250 1260 DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW 1270 1280 1290 1300 1310 1320 QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK 1330 1340 1350 1360 1370 1380 KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF 1390 1400 1410 1420 ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDADEVFSS
	Isoform N-NOS-2. Checksum: 2B527386DF5B4160	FASTA	1,324	148,548
	10 20 30 40 50 60 MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 70 80 90 100 110 120 GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 130 140 150 160 170 180 RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI 190 200 210 220 230 240 DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD 250 260 270 280 290 300 GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF 310 320 330 340 350 360 LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE 370 380 390 400 410 420 FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ 430 440 450 460 470 480 WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI 490 500 510 520 530 540 RYAGYKQPDG STLGDPANVQ FTEEVAKKMD LDMRKTSSLW KDQALVEINI AVLYSFQSDK 550 560 570 580 590 600 VTIVDHHSAT ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM LNYRLTPSFE 610 620 630 640 650 660 YQPDPWNTHV WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM GQAMAKRVKA TILYATETGK 670 680 690 700 710 720 SQAYAKTLCE IFKHAFDAKA MSMEEYDIVH LEHEALVLVV TSTFGNGDPP ENGEKFGCAL 730 740 750 760 770 780 MEMRHPNSVQ EERKSYKVRF NSVSSYSDSR KSSGDGPDLR DNFESTGPLA NVRFSVFGLG 790 800 810 820 830 840 SRAYPHFCAF GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG 850 860 870 880 890 900 DDVNIEKPNN SLISNDRSWK RNKFRLTYVA EAPDLTQGLS NVHKKRVSAA RLLSRQNLQS 910 920 930 940 950 960 PKFSRSTIFV RLHTNGNQEL QYQPGDHLGV FPGNHEDLVN ALIERLEDAP PANHVVKVEM 970 980 990 1000 1010 1020 LEERNTALGV ISNWKDESRL PPCTIFQAFK YYLDITTPPT PLQLQQFASL ATNEKEKQRL 1030 1040 1050 1060 1070 1080 LVLSKGLQEY EEWKWGKNPT MVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP 1090 1100 1110 1120 1130 1140 DEVHLTVAIV SYHTRDGEGP VHHGVCSSWL NRIQADDVVP CFVRGAPSFH LPRNPQVPCI 1150 1160 1170 1180 1190 1200 LVGPGTGIAP FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE TLQAKNKGVF 1210 1220 1230 1240 1250 1260 RELYTAYSRE PDRPKKYVQD VLQEQLAESV YRALKEQGGH IYVCGDVTMA ADVLKAIQRI 1270 1280 1290 1300 1310 1320 MTQQGKLSEE DAGVFISRLR DDNRYHEDIF GVTLRTYEVT NRLRSESIAF IEESKKDADE VFSS
	Isoform PNNOS. Checksum: A0522B26817B6705	FASTA	1,463	164,430
	10 20 30 40 50 60 MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 70 80 90 100 110 120 GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 130 140 150 160 170 180 RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI 190 200 210 220 230 240 DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD 250 260 270 280 290 300 GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF 310 320 330 340 350 360 LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE 370 380 390 400 410 420 FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ 430 440 450 460 470 480 WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI 490 500 510 520 530 540 RYAGYKQPDG STLGDPANVQ FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL 550 560 570 580 590 600 VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 610 620 630 640 650 660 NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK 670 680 690 700 710 720 HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN 730 740 750 760 770 780 GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA 790 800 810 820 830 840 FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKY 850 860 870 880 890 900 PEPLRFFPRK GPSLSHVDSE AHSLVAARDS QHRSYKVRFN SVSSYSDSRK SSGDGPDLRD 910 920 930 940 950 960 NFESTGPLAN VRFSVFGLGS RAYPHFCAFG HAVDTLLEEL GGERILKMRE GDELCGQEEA 970 980 990 1000 1010 1020 FRTWAKKVFK AACDVFCVGD DVNIEKPNNS LISNDRSWKR NKFRLTYVAE APDLTQGLSN 1030 1040 1050 1060 1070 1080 VHKKRVSAAR LLSRQNLQSP KFSRSTIFVR LHTNGNQELQ YQPGDHLGVF PGNHEDLVNA 1090 1100 1110 1120 1130 1140 LIERLEDAPP ANHVVKVEML EERNTALGVI SNWKDESRLP PCTIFQAFKY YLDITTPPTP 1150 1160 1170 1180 1190 1200 LQLQQFASLA TNEKEKQRLL VLSKGLQEYE EWKWGKNPTM VEVLEEFPSI QMPATLLLTQ 1210 1220 1230 1240 1250 1260 LSLLQPRYYS ISSSPDMYPD EVHLTVAIVS YHTRDGEGPV HHGVCSSWLN RIQADDVVPC 1270 1280 1290 1300 1310 1320 FVRGAPSFHL PRNPQVPCIL VGPGTGIAPF RSFWQQRQFD IQHKGMNPCP MVLVFGCRQS 1330 1340 1350 1360 1370 1380 KIDHIYREET LQAKNKGVFR ELYTAYSREP DRPKKYVQDV LQEQLAESVY RALKEQGGHI 1390 1400 1410 1420 1430 1440 YVCGDVTMAA DVLKAIQRIM TQQGKLSEED AGVFISRLRD DNRYHEDIFG VTLRTYEVTN 1450 1460 RLRSESIAFI EESKKDADEV FSS

References

[1]	"Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase." Bredt D.S., Hwang P.M., Glatt C.L., Lowenstein C., Reed R.R., Snyder S.H. Nature 351:714-718(1991) [PubMed: 1712077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"Cloning of a novel neuronal nitric oxide synthase expressed in penis and lower urinary tract." Magee T., Fuentes A.M., Garban H., Rajavashisth T., Marquez D., Rodriguez J.A., Rajfer J., Gonzalez-Cadavid N.F. Biochem. Biophys. Res. Commun. 226:145-151(1996) [PubMed: 8806605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNNOS). Strain: Fischer 344. Tissue: Penis.
[3]	"Nitric oxide synthase from rat colorectum: purification, peptide sequencing, partial PCR cloning, and immunohistochemistry." Seo H.G., Tatsumi H., Fujii J., Nishikawa A., Suzuki K., Kangawa K., Taniguchi N. J. Biochem. 115:602-607(1994) [PubMed: 7520037] [Abstract] Cited for: PROTEIN SEQUENCE OF 119-129; 132-142; 144-156; 189-200; 264-268; 270-276; 305-310; 360-369; 376-379; 381-385; 387-396; 779-785; 954-963 AND 1131-1139, TISSUE SPECIFICITY. Tissue: Colon.
[4]	"The identification of the pterin-binding domain in the nitric oxide synthase's sequence." Uvarov V.Y., Lyashenko A.A. Biochem. Biophys. Res. Commun. 206:736-741(1995) [PubMed: 7530005] [Abstract] Cited for: IDENTIFICATION OF TETRAHYDROBIOPTERIN-BINDING DOMAIN.
[5]	"Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling substrate specificity and electron transfer." Sato Y., Sagami I., Matsui T., Shimizu T. Biochem. Biophys. Res. Commun. 281:621-626(2001) [PubMed: 11237702] [Abstract] Cited for: MUTAGENESIS OF TYR-588.
[6]	"Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON." Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H. Neuron 28:183-193(2000) [PubMed: 11086993] [Abstract] Cited for: INTERACTION WITH CAPON AND RASD1.
[7]	"Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON." Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H. Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002) [PubMed: 11867766] [Abstract] Cited for: INTERACTION WITH CAPON AND SYN1.
[8]	"NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity." Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T. J. Biol. Chem. 279:29461-29468(2004) [PubMed: 15105416] [Abstract] Cited for: INTERACTION WITH ZDHHC23.
[9]	"Nitric oxide synthase (NOS)-interacting protein interacts with neuronal NOS and regulates its distribution and activity." Dreyer J., Schleicher M., Tappe A., Schilling K., Kuner T., Kusumawidijaja G., Mueller-Esterl W., Oess S., Kuner R. J. Neurosci. 24:10454-10465(2004) [PubMed: 15548660] [Abstract] Cited for: INTERACTION WITH NOSIP, ENZYME REGULATION, SUBCELLULAR LOCATION.
[10]	"Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex." Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A. Science 284:812-815(1999) [PubMed: 10221915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 14-125.
[11]	"Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with nadph-cytochrome p450 oxidoreductase." Zhang J., Martasek P., Paschke R., Shea T., Masters B.S.S., Kim J.-J.P. J. Biol. Chem. 276:37506-37513(2001) [PubMed: 11473123] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 963-1397.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X59949 mRNA. Translation: CAA42574.1.
U67309 mRNA. Translation: AAC52782.1.

IPI

IPI00204773.
IPI00231079.
IPI00324698.

PIR

S16233.

RefSeq

NP_434686.1.

UniGene

Rn.10573

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B8Q	NMR	-	A	13-133	[»]
1F20	X-ray	1.90	A	963-1397	[»]
1K2R	X-ray	2.15	A/B	299-717	[»]
1K2S	X-ray	2.55	A/B	299-717	[»]
1K2T	X-ray	2.20	A/B	299-717	[»]
1K2U	X-ray	2.20	A/B	299-717	[»]
1LZX	X-ray	2.00	A/B	299-717	[»]
1LZZ	X-ray	2.05	A/B	299-717	[»]
1M00	X-ray	2.05	A/B	299-717	[»]
1MMV	X-ray	2.00	A/B	299-717	[»]
1MMW	X-ray	2.00	A/B	299-717	[»]
1OM4	X-ray	1.75	A/B	297-718	[»]
1OM5	X-ray	2.30	A/B	297-717	[»]
1P6H	X-ray	1.98	A/B	297-717	[»]
1P6I	X-ray	1.90	A/B	297-717	[»]
1P6J	X-ray	2.00	A/B	297-717	[»]
1P6K	X-ray	1.78	A/B	297-717	[»]
1QAU	X-ray	1.25	A	14-125	[»]
1QAV	X-ray	1.90	B	12-126	[»]
1QW6	X-ray	2.10	A	298-716	[»]
1QWC	X-ray	2.30	A	298-716	[»]
1RS6	X-ray	1.95	A/B	297-717	[»]
1RS7	X-ray	1.95	A/B	297-717	[»]
1TLL	X-ray	2.30	A/B	742-1429	[»]
1VAG	X-ray	2.00	A	298-716	[»]
1ZVI	X-ray	2.00	A	298-716	[»]
1ZVL	X-ray	2.50	A/B	298-716	[»]
1ZZQ	X-ray	1.90	A/B	299-718	[»]
1ZZR	X-ray	2.05	A/B	299-718	[»]
1ZZU	X-ray	1.90	A/B	299-718	[»]
2G6H	X-ray	2.00	A/B	299-718	[»]
2G6I	X-ray	1.90	A/B	299-718	[»]
2G6J	X-ray	2.30	A/B	299-718	[»]
2G6K	X-ray	2.00	A/B	299-718	[»]
2G6L	X-ray	2.05	A/B	299-718	[»]
2G6M	X-ray	1.85	A/B	299-718	[»]
2G6N	X-ray	1.90	A/B	299-718	[»]
2HX3	X-ray	2.00	A/B	297-718	[»]
2HX4	X-ray	2.15	A/B	297-718	[»]
3B3M	X-ray	1.95	A/B	297-718	[»]
3B3N	X-ray	1.98	A/B	297-718	[»]
3B3O	X-ray	2.05	A/B	297-718	[»]
3B3P	X-ray	2.45	A/B	297-718	[»]
3DQR	X-ray	2.40	A/B	297-718	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P29476. 4 interactions.

PTM databases

PhosphoSite

P29476.

Proteomic databases

PRIDE

P29476.

Genome annotation databases

Ensembl

ENSRNOG00000001130. Rattus norvegicus. [Contig view]

GeneID

24598.

KEGG

rno:24598.

Organism-specific databases

RGD

3184. Nos1.

Phylogenomic databases

HOVERGEN

P29476.

Enzyme and pathway databases

BRENDA

1.14.13.39. 248.

Family and domain databases

InterPro

IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012144. Nitric-oxide_synthase.
IPR004030. NO_synthase_oxygenase_reg.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR001478. PDZ/DHR/GLGF.
[Graphical view]

Gene3D

G3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]

PIRSF

PIRSF000333. NOS. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

SMART

SM00228. PDZ. 1 hit.
[Graphical view]

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

603800.

Entry information

Entry name

NOS1_RAT

Accession

Primary (citable) accession number: P29476
Secondary accession number(s): P70594

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)