Neuronal nitric oxide synthase

Mutant mice are viable
Mutant mice are fertile
No apparent histopathological abnormalities in CNS
Decreased infarct volume after middle cerebral artery occlusion
Grossly enlarged stomachs
Hypertrophy of pyloric sphincter and the circular muscle layer

Huang et al, 1993
Huang et al, 1994

METHODOLOGY ( FROM T-BASE)

((nos))

Line Name DNA Construct
1. NOS (-/-) The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....
2. NOS (+/-) The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....
3. eNOS (-/-) The targeting vector contains 5' and 3' flanking regions of homology, and is designed to replace the HindIII to SalI fragment that contains exons e....
4. nNOS (kn) (-/-) The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....
5. nNOS (-/-) & cerebr The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....
6. nNOS (-/-) The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....
7. iNOS A replacement type targeting construct was prepared from 129/Sv genomic DNA. A single targeted clone was identified among 636 screened after two independent electropora....
8. nNOS (aggressive be The mouse neuronal nitric oxide synthase (NOS) gene was cloned from a lambda genomic library using the rat cDNA clone (G00-032-710) as a probe. The targeting vector was....

PROTEIN SEQUENCE ( FROM SWISS-PROT)

SWISS-PROT: P29477

ID   NOS2_MOUSE     STANDARD;      PRT;  1144 AA.
AC   P29477;
DT   01-APR-1993 (REL. 25, CREATED)
DT   01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   NITRIC OXIDE SYNTHASE, INDUCIBLE (EC 1.14.13.39) (NOS, TYPE II)
DE   (MACROPHAGE NOS) (MAC-NOS).
GN   NOS2 OR INOSL.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92229444. [MEDLINE, MEDLARS]
RA   XIE Q.-W., CHO H.J., CALAYCAY J., MUMFORD R.A., SWIDEREK K.M.,
RA   LEE T.D., DING A., TROSO T., NATHAN C.;
RL   SCIENCE 256:225-228(1992).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92357701. [MEDLINE, MEDLARS]
RA   LOWENSTEIN C.J., GLATT C.S., BREDT D.S., SNYDER S.H.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 89:6711-6715(1992).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 92210618. [MEDLINE, MEDLARS]
RA   LYONS C.R., ORLOFF G.J., CUNNINGHAM J.M.;
RL   J. BIOL. CHEM. 267:6370-6374(1992).
CC   -!- FUNCTION: THIS ENZYME PRODUCES NITRIC OXIDE (NO) WHICH IS A
CC       MESSENGER MOLECULE WITH DIVERSE FUNCTIONS THROUGHOUT THE BODY.
CC       IN MACROPHAGES, NO MEDIATES TUMORICIDAL AND BACTERICIDAL ACTIONS.
CC   -!- CATALYTIC ACTIVITY: L-ARGININE + N NADPH + M O(2) = CITRULLINE +
CC       NITRIC OXIDE + N NADP(+).
CC   -!- COFACTOR: THIS FLAVOPROTEIN BINDS ONE MOLE EACH OF FAD AND FMN.
CC   -!- ENZYME REGULATION: NOT STIMULATED BY CALCIUM/CALMODULIN.
CC   -!- TISSUE SPECIFICITY: MACROPHAGES.
CC   -!- INDUCTION: BY TREATMENT WITH ENDOTOXINS OR CYTOKINES.
CC   -!- SIMILARITY: STRONG, TO OTHER NOS ISOZYMES. ALSO TO CYTOCHROME
CC       P-450 REDUCTASE.
DR   EMBL; M87039; G198407; -. [EMBL / GenBank]
DR   EMBL; M92649; -; NOT_ANNOTATED_CDS. [EMBL / GenBank]
DR   EMBL; M84373; G200096; -. [EMBL / GenBank]
DR   PIR; A43271; A43271.
DR   PIR; A42166; A42166.
DR   PRODOM [Domain structure / List of seq. sharing at least 1 domain]
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   OXIDOREDUCTASE; NADP; FAD; FMN.
FT   NP_BIND     617    648       FMN (PYRIMIDINE PART) (BY SIMILARITY).
FT   NP_BIND     761    782       FAD (ADP PART) (BY SIMILARITY).
FT   NP_BIND     897    907       FAD (FLAVIN PART) (BY SIMILARITY).
FT   NP_BIND     972    990       NADP (RIBOSE PART) (BY SIMILARITY).
FT   NP_BIND    1070   1085       NADP (ADP PART) (BY SIMILARITY).
FT   CONFLICT    191    191       A -> V (IN REF. 2).
FT   CONFLICT    844    844       A -> G (IN REF. 2).
SQ   SEQUENCE   1144 AA;  130574 MW;  7DBBCEAB CRC32;
     MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ
     NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT
     RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL
     IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV
     FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP
     LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA
     CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF
     QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS
     PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE
     TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK
     KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE
     DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS
     IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG
     ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL
     ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR
     YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG
     FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ
     EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR
     MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK
     ATRL
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