O19132 (NOS1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nitric oxide synthase, brain
EC=1.14.13.39

Alternative name(s):
Constitutive NOS
NC-NOS
NOS type I
Neuronal NOS
Short name=N-NOS
Short name=nNOS
Peptidyl-cysteine S-nitrosylase NOS1
bNOS

Gene names

Name:

NOS1

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	1435 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR By similarity.
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. Inhibited by NOSIP By similarity.
Subunit structure	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. Interacts with VAC14 By similarity. Interacts with SLC6A4 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. In neurons, enriched in dendritic spines By similarity.
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. Mediates interaction with VAC14 By similarity.
Post-translational modification	Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro) 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
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1435	1435	Nitric oxide synthase, brain		PRO_0000170923
Regions
	Domain	17 – 99	83	PDZ
	Domain	761 – 941	181	Flavodoxin-like
	Domain	996 – 1243	248	FAD-binding FR-type
	Nucleotide binding	887 – 918	32	FMN By similarity
	Nucleotide binding	1033 – 1044	12	FAD By similarity
	Nucleotide binding	1176 – 1186	11	FAD By similarity
	Nucleotide binding	1251 – 1269	19	NADP By similarity
	Nucleotide binding	1349 – 1364	16	NADP By similarity
	Region	1 – 206	206	Interaction with NOSIP By similarity
	Region	164 – 246	83	PIN (nNOS-inhibiting protein) binding By similarity
	Region	731 – 751	21	Calmodulin-binding Potential
	Region	756 – 775	20	Tetrahydrobiopterin-binding By similarity
Sites
	Metal binding	421	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O19132 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 3ED87ECDD83A7A5A	FASTA	1,435	160,865
	10 20 30 40 50 60 MEEHVFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 70 80 90 100 110 120 GDIILAVNGR PLVDLSYDSA LEVLRGVASE THVVLILRGP EGFTTNLETT FTGDGTPKTI 130 140 150 160 170 180 RVTQPLGAPT KAVDLSHQPP SAGKEQPRPV DGAAGPGSWP QPTQGHGQEA GSPSRANGLA 190 200 210 220 230 240 PRTSSQDPAK KSGWAGLQGS GDKNELLKEI EPVLTLLAGG SKAVDGGGPA KAETRDTGVQ 250 260 270 280 290 300 VDRDFDAKSH KPLPLGVEND RVFSDLWGKG SAPVVLNNPY SEKEQPPASG KQSPTKNGSP 310 320 330 340 350 360 SKCPRFLKVK NWETDVVLTD TLHLKSTLET GCTEHICMGS IMFPSQHTRR PEDIRTKEQL 370 380 390 400 410 420 FPLAKEFIDQ YYSSIKRFGS KAHMERLEEV NKEIESTSTY QLKDTELIYG AKHAWRNASR 430 440 450 460 470 480 CVGRIQWSKL QVFDARDCTT AHGMFNYICN HIKYATNKGN LRSAITIFPQ RTDGKHDFRV 490 500 510 520 530 540 WNSQLIRYAG YKQPDGSTLG DPANVQFTEI CIQQGWKPPR SRFDVLPLLL QANGNDPELF 550 560 570 580 590 600 QIPPELVLEV PIRHPKFEWF KDLGLKWYGL PAVSNMLLEI GGLEFSACPF SGWYMGTEIG 610 620 630 640 650 660 VRDYCDNSRY NILEEVAKKM NLDMRKTSSL WKDQALVEIN IAVLYSFQSD KVTIVDHHSA 670 680 690 700 710 720 TESFIKHMEN EYRCRGGCPA DWVWIVPPMS GSITPVFHQE MLNYRLTPCF EYQPDPWNTH 730 740 750 760 770 780 VWKGTNGTPT KRRAIGFKKL AEAVKFSAKL MGQAMAKRVK ATILYATETG KSQAYAKTLC 790 800 810 820 830 840 EIFKHAFDAK VMSMEEYDIV HLEHETLVLV VTSTFGNGDP PENGEKFRCA LMEMRHPNSL 850 860 870 880 890 900 QEERKSYKVR FNSVSSYSDS RKSSGDGPDV RDHFESAGPL ANVRFSVFGL GSRAYPHFCA 910 920 930 940 950 960 FGHAVDTLLE ELGGERILKM REGDELCGQE EAFRTWAKKV FKAACDVFCV GDDVNIEKAN 970 980 990 1000 1010 1020 NSLISNDRSW KRNKFRLTYV AEAPGLTQGL SSVHKKRVSA ARLLSRQNLQ SPKSSRSTIF 1030 1040 1050 1060 1070 1080 VRLHTNGSQE LQYQPGDHLG VFPGNHEDLV NALIERLEDA PPANQMVKVE LLEERNTALG 1090 1100 1110 1120 1130 1140 VISNWKDEPR LPPCTVFQAF KYYLDITTPP TPLQLQQFAS LASNEKEKQR LLVLSKGLQE 1150 1160 1170 1180 1190 1200 YEEWKWGKNP TIVEVLEEFP SIQMPATLLL TQLSLLQPRY YSISSSPDMY PDEVHLTVAI 1210 1220 1230 1240 1250 1260 VSYHTRDGEG PIHHGVCSSW LNRIPADEVV PCFVRGAPSF RLPRNPQVPC ILVGPGTAFA 1270 1280 1290 1300 1310 1320 PFRSFWQQRQ FDIQHKGMSP CPMVLVFGCR QSKIDHIYRE EALQAKNKGV FRELYTAYSR 1330 1340 1350 1360 1370 1380 EPDKPKKYVQ DILQEQLAEQ VYRALKEQGG HIYVCGDVTM AADVLKAVQR IMAQQGKLSA 1390 1400 1410 1420 1430 EDAGVFISRL RDDNRYHEDI FGVTLRTYEV TNRLRSESIA FIEESKKDTD EVFSS

References

[1]	"Molecular cloning of a cDNA encoding a constitutive nitric oxide synthase from rabbit brain." Jeong Y., Yim J. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U91584 mRNA. Translation: AAB68663.1.
RefSeq	NP_001075854.1. NM_001082385.1.
UniGene	Ocu.2169.
3D structure databases
ProteinModelPortal	O19132.
SMR	O19132. Positions 7-133, 304-722, 756-1419.
ModBase	Search...
Protein-protein interaction databases
STRING	O19132.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009243.
Organism-specific databases
CTD	4842.
Phylogenomic databases
eggNOG	maNOG15221.
HOVERGEN	HBG000159.
Family and domain databases
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR012144. Nitric-oxide_synthase. IPR004030. NO_synthase_oxygenase_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR001478. PDZ/DHR/GLGF. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:1.20.990.10. NADPH_Cyt_P450_Rdtase_dom3. 1 hit. G3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.
PANTHER	PTHR19384:SF5. PTHR19384:SF5. 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]
SUPFAM	SSF56512. NO_synthase_oxygenase_reg. 1 hit. SSF50156. PDZ. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOS1_RABIT

Accession

Primary (citable) accession number: O19132

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program