ID   NOS3_PIG       STANDARD;      PRT;  1204 AA.
AC   Q28969;
DT   30-MAY-2000 (Rel. 39, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   NITRIC-OXIDE SYNTHASE, ENDOTHELIAL (EC 1.14.13.39) (EC-NOS) (NOS, TYPE
DE   III) (NOSIII) (ENDOTHELIAL NOS) (ENOS) (CONSTITUTIVE NOS) (CNOS).
GN   NOS3 OR NOS.
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   SEQUENCE FROM N.A., AND CHARACTERIZATION.
RC   TISSUE=PULMONARY ARTERY;
RX   MEDLINE=97293429; PubMed=9149402;
RA   Zhang J., Patel J.M., Block E.R.;
RT   "Molecular cloning, characterization and expression of a nitric oxide
RT   synthase from porcine pulmonary artery endothelial cells.";
RL   Comp. Biochem. Physiol. 116B:485-491(1997).
RN   [2]
RP   SEQUENCE OF 1031-1205 FROM N.A.
RA   Patel J.M., Block E.R.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PRODUCES NITRIC OXIDE (NO) WHICH IS IMPLICATED IN
CC       VASCULAR SMOOTH MUSCLE RELAXATION THROUGH A CGMP-MEDIATED SIGNAL
CC       TRANSDUCTION PATHWAY. NO MEDIATES VASCULAR ENDOTHELIAL GROWTH
CC       FACTOR (VEGF)-INDUCED ANGIOGENESIS IN CORONARY VESSELS AND
CC       PROMOTES BLOOD CLOTTING THROUGH THE ACTIVATION OF PLATELETS (BY
CC       SIMILARITY).
CC   -!- CATALYTIC ACTIVITY: L-ARGININE + N NADPH + M O(2) = CITRULLINE +
CC       NITRIC OXIDE + N NADP(+).
CC   -!- COFACTOR: HEME. BINDS ONE MOLE EACH OF FAD AND FMN. ALSO REQUIRES
CC       TETRAHYDROBIOPTERIN (BH4) WHICH MAY STABILIZE THE DIMERIC FORM OF
CC       THE ENZYME (BY SIMILARITY).
CC   -!- ENZYME REGULATION: STIMULATED BY CALCIUM/CALMODULIN (BY
CC       SIMILARITY).
CC   -!- SUBUNIT: HOMODIMER (BY SIMILARITY).
CC   -!- INDUCTION: REPRESSED BY PROINFLAMMATORY CYTOKINES.
CC   -!- SIMILARITY: BELONGS TO THE NOS FAMILY.
CC   --------------------------------------------------------------------------
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DR   EMBL; U59924; AAB39539.1; -.
DR   EMBL; U33832; AAA84933.1; -.
DR   HSSP; P29477; 2NOS.
DR   INTERPRO; IPR001094; -.
DR   INTERPRO; IPR001433; -.
DR   INTERPRO; IPR001709; -.
DR   INTERPRO; IPR003097; -.
DR   PFAM; PF00667; FAD_binding; 1.
DR   PFAM; PF00175; oxidored_fad; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
KW   Oxidoreductase; NADP; FAD; FMN; Calmodulin-binding; Myristate;
KW   Lipoprotein; Palmitate; Calcium-binding; Heme; Zinc; Metal-binding;
KW   Multigene family.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   BINDING     185    185       HEME (BY SIMILARITY).
FT   DOMAIN      491    511       CALMODULIN-BINDING (POTENTIAL).
FT   NP_BIND     650    681       FMN (PYRIMIDINE PART) (BY SIMILARITY).
FT   NP_BIND     794    805       FAD (ADP PART) (BY SIMILARITY).
FT   NP_BIND     936    946       FAD (FLAVIN PART) (BY SIMILARITY).
FT   NP_BIND    1011   1029       NADP (RIBOSE PART) (BY SIMILARITY).
FT   NP_BIND    1109   1124       NADP (ADP PART) (BY SIMILARITY).
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID        14     14       PALMITATE (BY SIMILARITY).
FT   LIPID        25     25       PALMITATE (BY SIMILARITY).
FT   METAL        95     95       ZINC (BY SIMILARITY).
FT   METAL       100    100       ZINC (BY SIMILARITY).
SQ   SEQUENCE   1204 AA;  133274 MW;  48676BA95D814CFE CRC64;
     GNLKSVGQEP GPPCGLGLGL GLGLCGKQGP ATPAPEPSRA PAPATPHAPE HSPAPNSPTL
     TRPPEGPKFP RVKNWEVGSI TYDTLCAQSQ QDGPCTPRRC LGSLVLPRKL QSRPSPGPPP
     AEQLLSQARD FINQYYSSIK RSGSQAHEER LQEVEAEVAT TGTYHLGESE LVFGAKQAWR
     NAPRCVGRIQ WGKLQVFDAR DCSSAQEMFT YICNHIKYAT NRGNLRSAIT VFPQRTPGRG
     DFRIWNSQLV RYAGYRQQDG SVRGDPANVE ITELCIQHGW TPGNGRFDVL PLLLQAPDEP
     PELFALPPEL VLEVPLEHPT LEWFAALGLR WYALPAVSNM LLEIGGLEFP AAPFSGWYMS
     TEIGTRNLCD PHRYNILEDV AVCMDLDTRT TSSLWKDKAA VEINLAVLHS YQLAKVTIVD
     HHAATASFMK HLENEQKARG GCPADWAWIV PPISGSLTPV FHQEMVNYVL SPAFRYQPDP
     WKGSAAKGTG IARKKTFKEV ANAVKISASL MATVMPKRVK ASILYASETV RAQSYAQQLG
     RLFRKAFDPR VLCMDEYDVV SLEHETLVLV VTSTFGNGDP PENGESFAAA LMEMSGPYNG
     SPRPEQHRSY KIRFNSVSCS DPLVSSWRRK RKESSNTDSA GALGTLRFCV FGLGSRAYPH
     FCAFARAVDT RLEELGGERL LQLGQGDELC GQEEAFRGWA QAAFQASCET FCVGEDAKAA
     ARDIFSPKRS WKRQRYRLSA QVEGLQLLPG LVHVHRRKMF QATVLSVENL QSSKSTRATI
     LVRLDTEGQE GLQYQPGDHI GICPPNRTGL VEALLSRVED PTPPTESVGV EQLEKGSPGG
     PPPSWVRDPR LPPYTLRQAL TFFLDITSPP SPRLLRVLST LAEEPSEQQE LETLSQDPRR
     YEEWKWFRCP TLLEVLEQFP SVALPTPLLL TQLALLQPRY YSVSSAPSTY PGEIHPTVAV
     LAYRTQDGLG PLHYGVCSTW LGQLKPGDPV PCFIRAAPSF RLPPDPSLPC ILVGPGTGIA
     PFRGFWQERL HDIESKGLQP APMTLVFGCR CSQLDHLYRD EVQDAQQRGV FGRVLTAFSR
     EPDSPKTYVQ DILRTELAAE VHRVLCLERG HMFVCGDVTM ATSVLQTVQR ILATEGNMEL
     DEAGDVIGVL RDQQRYHEDI FGLTLRTQEV TSRIRTQSFS LQERHLRGAV PWTFDPPGPD
     TPGP
//