Nitric oxide synthase, inducible - Rattus norvegicus (Rat)

Names and origin

Protein names

Recommended name:
    Nitric oxide synthase, inducible
    EC=1.14.13.39
Alternative name(s):
    Inducible NO synthase
      Short name=Inducible NOS
      Short name=iNOS
    NOS type II

Gene names

Name:

Nos2

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

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Protein attributes

Sequence length	1147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body.
Catalytic activity	L-arginine + n NADPH + m O(2) = citrulline + nitric oxide + n NADP(+).
Cofactor	Heme group. Binds 1 FAD. Binds 1 FMN. Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
Enzyme regulation	Not stimulated by calcium/calmodulin. Aspirin inhibits expression and function of this enzyme and effects may be exerted at the level of translational/post-translational modification and directly on the catalytic activity By similarity.
Subunit structure	Homodimer. Binds SLC9A3R1 By similarity.
Tissue specificity	In normal kidney, expressed primarily in the medullary thick ascending limb, with minor amounts in the medullary collecting duct and vasa recta bundle.
Induction	By interferon gamma and lipopolysaccharides (LPS).
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.
Caution	Ref.9 sequence was originally thought to originate from human but appears to be from rat.

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Ontologies

Keywords
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Zinc
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from sequence or structural similarity. Source: UniProtKB nitric oxide biosynthetic process Ref.9 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Ref.9 Traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1147

1147

Nitric oxide synthase, inducible

PRO_0000170937

Regions

Domain

536 – 674

139

Flavodoxin-like

Domain

727 – 967

241

FAD-binding FR-type

Nucleotide binding

620 – 651

32

FMN By similarity

Nucleotide binding

764 – 775

12

FAD By similarity

Nucleotide binding

900 – 910

11

FAD By similarity

Nucleotide binding

975 – 993

19

NADP By similarity

Nucleotide binding

1073 – 1088

16

NADP By similarity

Region

506 – 526

21

Calmodulin-binding Potential

Sites

Metal binding

107

1

Zinc By similarity

Metal binding

112

1

Zinc By similarity

Metal binding

197

1

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

10

1

R → K in BAA07994. Ref.7

Sequence conflict

72

1

H → Y in BAA03138. Ref.1

Sequence conflict

107

1

C → R in AAC13747. Ref.3

Sequence conflict

128

1

D → V in BAA12035. Ref.8

Sequence conflict

130

1

P → H in AAC13747. Ref.3

Sequence conflict

171

1

E → G in BAA12035. Ref.8

Sequence conflict

195

1

P → S in BAA12035. Ref.8

Sequence conflict

248

1

S → N in AAC83553. Ref.9

Sequence conflict

248

1

S → T Ref.3 Ref.5

Sequence conflict

264

1

Y → I in AAC13747. Ref.3

Sequence conflict

271

1

D → A in AAC83554. Ref.9

Sequence conflict

277

1

D → E in AAC13747. Ref.3

Sequence conflict

348

1

A → P in BAA03138. Ref.1

Sequence conflict

349

1

V → A in CAA54208. Ref.6

Sequence conflict

380

1

F → L in AAC83553 and AAC83554. Ref.2 Ref.7 Ref.8 Ref.9

Sequence conflict

395

1

R → S in BAA02090. Ref.4

Sequence conflict

399

1

E → G in AAC83553. Ref.9

Sequence conflict

412

1

V → A in AAC13747. Ref.3

Sequence conflict

477

1

M → I Ref.13

Sequence conflict

513

1

T → R in AAB18620. Ref.11

Sequence conflict

515

1

L → W in AAB31028. Ref.12

Sequence conflict

545

1

G → R in AAB31028. Ref.12

Sequence conflict

551

1

A → R in AAB18620. Ref.11

Sequence conflict

556

1

A → S in AAB31028. Ref.12

Sequence conflict

559

1

S → T in AAC83553 and AAC83554. Ref.9

Sequence conflict

564

1

T → N in AAB31028. Ref.12

Sequence conflict

570

1

E → D in AAB31028. Ref.12

Sequence conflict

583

1

L → P Ref.5 Ref.10

Sequence conflict

591

1

G → A in AAB31028. Ref.12

Sequence conflict

591

1

G → V Ref.1 Ref.6

Sequence conflict

619

1

A → R in AAA85861. Ref.2

Sequence conflict

640

1

Q → P in AAC83553. Ref.9

Sequence conflict

664

1

D → G in AAB18620. Ref.11

Sequence conflict

679 – 680

2

ET → VP in BAA03138. Ref.1

Sequence conflict

690

1

Q → P in AAB18620. Ref.11

Sequence conflict

711

1

S → N in AAB18620. Ref.11

Sequence conflict

714 – 715

2

SL → TR in AAB18620. Ref.11

Sequence conflict

714

1

S → P in AAC83553 and AAC83554. Ref.2 Ref.7 Ref.8 Ref.9

Sequence conflict

714

1

S → P in AAC16401. Ref.10

Sequence conflict

719

1

K → R in AAB18620. Ref.11

Sequence conflict

721

1

L → P Ref.6

Sequence conflict

722

1

S → R Ref.1 Ref.6 Ref.11

Sequence conflict

724 – 726

3

IHA → FLN Ref.11

Sequence conflict

730

1

F → I in AAB18620. Ref.11

Sequence conflict

731

1

T → A in AAC83553. Ref.9

Sequence conflict

740

1

L → P in CAA54208. Ref.6

Sequence conflict

779

1

A → G in AAC13747. Ref.3

Sequence conflict

834

1

P → S in BAA12035. Ref.8

Sequence conflict

844

1

A → G in BAA03138. Ref.1

Sequence conflict

895

1

S → L in BAA02090. Ref.4

Sequence conflict

911

1

Q → L in AAC13747. Ref.3

Sequence conflict

925

1

V → D in BAA12035. Ref.8

Sequence conflict

937

1

H → N in AAC83554. Ref.9

Sequence conflict

999

1

H → R in AAC83553 and AAC83554. Ref.2 Ref.7 Ref.9

Sequence conflict

1008 – 1009

2

TL → NF in AAC83554. Ref.9

Sequence conflict

1016

1

P → R Ref.5

Sequence conflict

1016

1

P → S Ref.8

Sequence conflict

1017

1

E → R Ref.5 Ref.8

Sequence conflict

1024

1

E → K in AAC83554. Ref.9

Sequence conflict

1076

1

L → I in AAC83553. Ref.9

Sequence conflict

1084

1

M → I in CAA54208. Ref.6

Sequence conflict

1129

1

F → V in AAC83554. Ref.9

Sequence conflict

1133

1

A → V in AAC83553 and AAC83554. Ref.2 Ref.7 Ref.9

Sequence conflict

1138

1

T → A in AAC83553 and AAC83554. Ref.2 Ref.7 Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

Q06518-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 77C77432DD8AB0A9
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FASTA

1,147

130,628

        10         20         30         40         50         60 
MACPWKFLFR VKSYQGDLKE EKDINNNVEK TPGAIPSPTT QDDPKSHKHQ NGFPQFLTGT 

        70         80         90        100        110        120 
AQNVPESLDK LHVTPSTRPQ HVRIKNWGNG EIFHDTLHHK ATSDISCKSK LCMGSIMNSK 

       130        140        150        160        170        180 
SLTRGPRDKP TPVEELLPQA IEFINQYYGS FKEAKIEEHL ARLEAVTKEI ETTGTYQLTL 

       190        200        210        220        230        240 
DELIFATKMA WRNAPRCIGR IQWSNLQVFD ARSCSTASEM FQHICRHILY ATNSGNIRSA 

       250        260        270        280        290        300 
ITVFPQRSDG KHDFRIWNSQ LIRYAGYQMP DGTIRGDPAT LEFTQLCIDL GWKPRYGRFD 

       310        320        330        340        350        360 
VLPLVLQAHG QDPEVFEIPP DLVLEVTMEH PKYEWFQELG LKWYALPAVA NMLLEVGGLE 

       370        380        390        400        410        420 
FPACPFNGWY MGTEIGVRDF CDTQRYNILE EVGRRMGLET HTLASLWKDR AVTEINAAVL 

       430        440        450        460        470        480 
HSFQKQNVTI MDHHTASESF MKHMQNEYRA RGGCPADWIW LVPPVSGSIT PVFHQEMLNY 

       490        500        510        520        530        540 
VLSPFYYYQI EPWKTHIWQD EKLRPRRREI RFTVLVKAVF FASVLMRKVM ASRVRATVLF 

       550        560        570        580        590        600 
ATETGKSEAL ARDLAALFSY AFNTKVVCME QYKANTLEEE QLLLVVTSTF GNGDCPSNGQ 

       610        620        630        640        650        660 
TLKKSLFMMK ELGHTFRYAV FGLGSSMYPQ FCAFAHDIDQ KLSHLGASQL APTGEGDELS 

       670        680        690        700        710        720 
GQEDAFRSWA VQTFRAACET FDVRSKHCIQ IPKRYTSNAT WEPEQYKLTQ SPESLDLNKA 

       730        740        750        760        770        780 
LSSIHAKNVF TMRLKSLQNL QSEKSSRTTL LVQLTFEGSR GPSYLPGEHL GIFPGNQTAL 

       790        800        810        820        830        840 
VQGILERVVD CSSPDQTVCL EVLDESGSYW VKDKRLPPCS LRQALTYFLD ITTPPTQLQL 

       850        860        870        880        890        900 
HKLARFATEE THRQRLEALC QPSEYNDWKF SNNPTFLEVL EEFPSLRVPA AFLLSQLPIL 

       910        920        930        940        950        960 
KPRYYSISSS QDHTPSEVHL TVAVVTYRTR DGQGPLHHGV CSTWINNLKP EDPVPCFVRS 

       970        980        990       1000       1010       1020 
VSGFQLPEDP SQPCILIGPG TGIAPFRSFW QQRLHDSQHR GLKGGRMTLV FGCRHPEEDH 

      1030       1040       1050       1060       1070       1080 
LYQEEMQEMV RKGVLFQVHT GYSRLPGKPK VYVQDILQKE LADEVFSVLH GEQGHLYVCG 

      1090       1100       1110       1120       1130       1140 
DVRMARDVAT TLKKLVAAKL NLSEEQVEDY FFQLKSQKRY HEDIFGAVFS YGAKKGNTLE 


EPKGTRL

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References

[1]	"Cloning of inducible nitric oxide synthase in rat vascular smooth muscle cells." Nunokawa Y., Ishida N., Tanaka S. Biochem. Biophys. Res. Commun. 191:89-94(1993) [PubMed: 7680561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Vascular smooth muscle.
[2]	"Cloning and expression of cytokine-inducible nitric oxide synthase cDNA from rat islets of Langerhans." Karlsen A.E., Andersen H.U., Vissing H., Larsen P.M., Fey S.J., Cuartero B.G., Madsen O.D., Petersen J.S., Mortensen S.B., Mandrup-Poulsen T., Boel E., Nerup J. Diabetes 44:753-758(1995) [

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References