Descriptions

Nitric oxide synthase produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. The primary sequences of the three mammalian nitric oxide synthase (NOS) isoforms differ by the insertion of a 52-55-amino acid loop into the reductase domains of the endothelial (eNOS) and neuronal (nNOS), but not inducible (iNOS). The loop mediates the autoinhibition in eNOS and nNOS. Deletion of the autoinhibitory loop in bovine eNOS increases its catalytic acitivity.

Autoinhibitory domains (AIDs)

Target domain

357-718 (NO synthase domain); 996-1364 (FAD/NAD-binding domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O19132

Entry ID Method Resolution Chain Position Source
AF-O19132-F1 Predicted AlphaFoldDB

No variants for O19132

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O19132

No associated diseases with O19132

2 regional properties for O19132

Type Name Position InterPro Accession
domain Kinesin motor domain 6 - 335 IPR001752
conserved_site Kinesin motor domain, conserved site 226 - 237 IPR019821

Functions

Description
EC Number 1.14.13.39 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Cell membrane, sarcolemma ; Peripheral membrane protein
  • Cell projection, dendritic spine
  • 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 (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
dendritic spine A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
sarcolemma The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.

7 GO annotations of molecular function

Name Definition
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
nitric-oxide synthase activity Catalysis of the reaction: L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.

1 GO annotations of biological process

Name Definition
nitric oxide biosynthetic process The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
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