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Protein

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein

Gene

Nos1ap

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4.1 Publication

GO - Molecular functioni

  • nitric-oxide synthase binding Source: UniProtKB
  • PDZ domain binding Source: RGD
  • protease binding Source: RGD

GO - Biological processi

  • negative regulation of neuron death Source: RGD
  • neuron projection regeneration Source: RGD
  • neurotransmitter secretion Source: UniProtKB
  • positive regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  • regulation of apoptotic process Source: DFLAT
  • regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: BHF-UCL
  • regulation of cardiac muscle cell action potential Source: BHF-UCL
  • regulation of high voltage-gated calcium channel activity Source: BHF-UCL
  • regulation of nitric oxide biosynthetic process Source: DFLAT
  • regulation of nitric-oxide synthase activity Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
Alternative name(s):
C-terminal PDZ ligand of neuronal nitric oxide synthase protein
Nitric oxide synthase 1 adaptor protein
Gene namesi
Name:Nos1ap
Synonyms:Capon
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620106. Nos1ap.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • presynapse Source: GOC
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi501I → S or A: Does not affect interaction with NOS1. 1 Publication1
Mutagenesisi502A → D: Abolishes interaction with NOS1. 1 Publication1
Mutagenesisi503V → A: Abolishes interaction with NOS1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000893181 – 503Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase proteinAdd BLAST503

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei183PhosphoserineBy similarity1
Modified residuei187PhosphoserineBy similarity1
Modified residuei190PhosphoserineBy similarity1
Modified residuei262PhosphoserineBy similarity1
Modified residuei368PhosphoserineCombined sources1
Modified residuei371PhosphoserineCombined sources1
Modified residuei398PhosphoserineBy similarity1
Modified residuei414PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO54960.
PeptideAtlasiO54960.
PRIDEiO54960.

PTM databases

iPTMnetiO54960.

Expressioni

Tissue specificityi

Brain-specific. Highly expressed in accessory olfactory bulb, caudate-putamen, cerebellum, cerebral cortex, dentate gyrus of the hyppocampus, islands of Calleja, olfactory bulb and supraoptic nucleus.1 Publication

Interactioni

Subunit structurei

Interacts with the PDZ domain of NOS1 or the second PDZ domain of DLG4 through its C-terminus. Interacts with RASD1 and SYN1, SYN2 and SYN3 via its PID domain. Forms a ternary complex with NOS1 and RASD1. Forms a ternary complex with NOS1 and SYN1.4 Publications

GO - Molecular functioni

  • nitric-oxide synthase binding Source: UniProtKB
  • PDZ domain binding Source: RGD
  • protease binding Source: RGD

Protein-protein interaction databases

IntActiO54960. 2 interactors.
MINTiMINT-150976.
STRINGi10116.ENSRNOP00000038197.

Structurei

3D structure databases

ProteinModelPortaliO54960.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 191PIDPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni491 – 503Interaction with NOS1Add BLAST13

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili319 – 360Sequence analysisAdd BLAST42

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi501 – 503PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi298 – 305Poly-Gln8

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4458. Eukaryota.
KOG4815. Eukaryota.
ENOG410ZTVD. LUCA.
HOGENOMiHOG000111298.
HOVERGENiHBG050788.
InParanoidiO54960.
KOiK16513.
PhylomeDBiO54960.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI SFEAKYVGSL DVPRPNSRVE
60 70 80 90 100
IVAAMRRIRY EFKAKNIKKK KVSIMVSVDG VKVILKKKKK KKEWTWDESK
110 120 130 140 150
MLVMQDPIYR IFYVSHDSQD LKIFSYIARD GASNIFRCNV FKSKKKSQAM
160 170 180 190 200
RIVRTVGQAF EVCHKLSLQH TQQNADGQED GESERNSDGS GDPGRQLTGA
210 220 230 240 250
ERVSTATAEE TDIDAVEVPL PGNDILEFSR GVTDLDAIGK DGGSHIDTTV
260 270 280 290 300
SPHPQEPMLA ASPRMLLPSS SSSKPPGLGT GTPLSTHHQM QLLQQLLQQQ
310 320 330 340 350
QQQTQVAVAQ VHLLKDQLAA EAAARLEAQA RVHQLLLQNK DMLQHISLLV
360 370 380 390 400
KQVQELELKL SGQSTMGSQD SLLEITFRSG ALPVLCESTT PKPEDLHSPL
410 420 430 440 450
LGAGLADFAH PVGSPLGRRD CLVKLECFRF LPAEDNQPMA QGEPLLGGLE
460 470 480 490 500
LIKFRESGIA SEYESNTDES EERDSWSQEE LPRLLNVLQR QELGDSLDDE

IAV
Length:503
Mass (Da):55,864
Last modified:June 1, 1998 - v1
Checksum:i801775EB2BF49EFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037071 mRNA. Translation: AAC40065.1.
RefSeqiNP_620277.1. NM_138922.1.
UniGeneiRn.9903.

Genome annotation databases

GeneIDi192363.
KEGGirno:192363.
UCSCiRGD:620106. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037071 mRNA. Translation: AAC40065.1.
RefSeqiNP_620277.1. NM_138922.1.
UniGeneiRn.9903.

3D structure databases

ProteinModelPortaliO54960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54960. 2 interactors.
MINTiMINT-150976.
STRINGi10116.ENSRNOP00000038197.

PTM databases

iPTMnetiO54960.

Proteomic databases

PaxDbiO54960.
PeptideAtlasiO54960.
PRIDEiO54960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi192363.
KEGGirno:192363.
UCSCiRGD:620106. rat.

Organism-specific databases

CTDi9722.
RGDi620106. Nos1ap.

Phylogenomic databases

eggNOGiKOG4458. Eukaryota.
KOG4815. Eukaryota.
ENOG410ZTVD. LUCA.
HOGENOMiHOG000111298.
HOVERGENiHBG050788.
InParanoidiO54960.
KOiK16513.
PhylomeDBiO54960.

Miscellaneous databases

PROiO54960.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAPON_RAT
AccessioniPrimary (citable) accession number: O54960
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.