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Q62600

- NOS3_RAT

UniProt

Q62600 - NOS3_RAT

Protein

Nitric oxide synthase, endothelial

Gene

Nos3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.

    Catalytic activityi

    2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

    Cofactori

    Heme group.
    Binds 1 FAD.
    Binds 1 FMN.
    Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

    Enzyme regulationi

    Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi93 – 931ZincBy similarity
    Metal bindingi98 – 981ZincBy similarity
    Metal bindingi183 – 1831Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi648 – 67932FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi792 – 80312FADBy similarityAdd
    BLAST
    Nucleotide bindingi1009 – 102719NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1107 – 112216NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. beta-catenin binding Source: RGD
    3. cadherin binding Source: RGD
    4. calmodulin binding Source: RGD
    5. flavin adenine dinucleotide binding Source: InterPro
    6. FMN binding Source: InterPro
    7. heme binding Source: InterPro
    8. Hsp90 protein binding Source: RGD
    9. iron ion binding Source: InterPro
    10. NADP binding Source: InterPro
    11. NADPH-hemoprotein reductase activity Source: RefGenome
    12. nitric-oxide synthase activity Source: RGD
    13. nitric-oxide synthase binding Source: RGD
    14. protein binding Source: IntAct
    15. scaffold protein binding Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. bone development Source: RGD
    3. cellular response to cAMP Source: RGD
    4. cellular response to growth factor stimulus Source: RGD
    5. cellular response to heat Source: RGD
    6. cellular response to magnesium ion Source: RGD
    7. cellular response to organic cyclic compound Source: RGD
    8. cellular response to transforming growth factor beta stimulus Source: RGD
    9. cellular response to tumor necrosis factor Source: RGD
    10. female pregnancy Source: RGD
    11. negative regulation of blood pressure Source: RefGenome
    12. negative regulation of smooth muscle cell proliferation Source: RGD
    13. nitric oxide biosynthetic process Source: RGD
    14. nitric oxide mediated signal transduction Source: RefGenome
    15. positive regulation of apoptotic process Source: RGD
    16. positive regulation of guanylate cyclase activity Source: RefGenome
    17. positive regulation of vasodilation Source: RefGenome
    18. response to activity Source: RGD
    19. response to amino acid Source: RGD
    20. response to axon injury Source: RGD
    21. response to candesartan Source: RGD
    22. response to corticosterone Source: RGD
    23. response to cytokine Source: RGD
    24. response to drug Source: RGD
    25. response to estradiol Source: RGD
    26. response to ethanol Source: RGD
    27. response to fructose Source: RGD
    28. response to hyperoxia Source: RGD
    29. response to hypoxia Source: RGD
    30. response to ketone Source: RGD
    31. response to lead ion Source: RGD
    32. response to lipopolysaccharide Source: RGD
    33. response to lipoprotein particle Source: RGD
    34. response to mechanical stimulus Source: RGD
    35. response to metal ion Source: RGD
    36. response to organic cyclic compound Source: RGD
    37. response to peptide Source: RGD
    38. response to peptide hormone Source: RGD
    39. response to salt Source: RGD
    40. response to statin Source: RGD
    41. retina development in camera-type eye Source: RGD
    42. signal transduction Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calcium, Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

    Enzyme and pathway databases

    SABIO-RKQ62600.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitric oxide synthase, endothelial (EC:1.14.13.39)
    Alternative name(s):
    Constitutive NOS
    Short name:
    cNOS
    EC-NOS
    Endothelial NOS
    Short name:
    eNOS
    NOS type III
    Short name:
    NOSIII
    Gene namesi
    Name:Nos3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3186. Nos3.

    Subcellular locationi

    Membranecaveola By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus By similarity. Cell membrane By similarity
    Note: Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: RGD
    2. caveola Source: UniProtKB-SubCell
    3. cytoplasm Source: BHF-UCL
    4. cytoskeleton Source: UniProtKB-SubCell
    5. cytosol Source: RGD
    6. Golgi apparatus Source: RGD
    7. membrane raft Source: RGD
    8. mitochondrion Source: RGD
    9. nucleolus Source: RGD
    10. nucleus Source: BHF-UCL
    11. plasma membrane Source: RGD
    12. sarcolemma Source: RGD
    13. vesicle membrane Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 12021201Nitric oxide synthase, endothelialPRO_0000170946Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi15 – 151S-palmitoyl cysteineBy similarity
    Lipidationi26 – 261S-palmitoyl cysteineBy similarity
    Modified residuei140 – 1401PhosphoserineBy similarity
    Modified residuei494 – 4941Phosphothreonine; by AMPK1 Publication
    Modified residuei632 – 6321PhosphoserineBy similarity
    Modified residuei1174 – 11741PhosphothreonineBy similarity
    Modified residuei1176 – 11761Phosphoserine; by AMPK1 Publication

    Post-translational modificationi

    Phosphorylation by AMPK at Ser-1176 in the presence of Ca2+-calmodulin (CaM) activates activity. In absence of Ca2+-calmodulin, AMPK also phosphorylates Thr-494, resulting in inhibition of activity.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PRIDEiQ62600.

    PTM databases

    PhosphoSiteiQ62600.

    Expressioni

    Tissue specificityi

    Expressed constitutively by vascular endothelium. Detected in alveolar and serosal epithelial cells as well as in endothelial cells in one day old rat. In adult lung, detected in rare endothelial cells.

    Developmental stagei

    Detected at high levels in lung during the late fetal and postnatal period and at lower levels in adult.

    Gene expression databases

    GenevestigatoriQ62600.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NOSIP and NOSTRIN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CALMP621572EBI-7052018,EBI-397403From a different organism.

    Protein-protein interaction databases

    DIPiDIP-41833N.
    IntActiQ62600. 2 interactions.
    MINTiMINT-202608.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62600.
    SMRiQ62600. Positions 66-480, 728-1161.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini519 – 702184Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini755 – 1001247FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 485389Interaction with NOSIPBy similarityAdd
    BLAST
    Regioni489 – 50921Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi31 – 6838Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NOS family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4362.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.
    InParanoidiQ62600.
    KOiK13242.
    PhylomeDBiQ62600.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 2 hits.
    3.90.340.10. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000333. NOS. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q62600-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APVPPSPTRP     50
    APDHSPPLTR PPDGPKFPRV KNWEVGSITY DTLSAQAQQD GPCTPRRCLG 100
    SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ 150
    EVEAEVVATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC 200
    RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRYAGRGDF RIWNSQLVRY 250
    AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE 300
    LFTLPPELVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA 350
    PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE 400
    INVAVLYSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP 450
    ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGTGIT RKKTFKEVAN 500
    AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL 550
    CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP 600
    RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG 650
    LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA 700
    AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPRLT 750
    HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGSQEGL QYQPGDHIGV 800
    CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP 850
    PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE 900
    EWKWFRCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG 950
    EIHLTVAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL 1000
    PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS 1050
    QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH 1100
    RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGSMELDE AGDVIGVLRD 1150
    QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPTQETP 1200
    GS 1202
    Length:1,202
    Mass (Da):133,290
    Last modified:January 23, 2007 - v4
    Checksum:i52E905C3134E244D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2332QR → PS in AAC34677. 1 PublicationCurated
    Sequence conflicti249 – 2491R → S in AAC34677. 1 PublicationCurated
    Sequence conflicti298 – 3047Missing in AAT99567. (PubMed:15808839)Curated
    Sequence conflicti600 – 6001P → L in CAA09493. 1 PublicationCurated
    Sequence conflicti735 – 7351R → G in AAT99567. (PubMed:15808839)Curated
    Sequence conflicti739 – 7391Q → P in AAT99567. (PubMed:15808839)Curated
    Sequence conflicti748 – 7481R → G in BAD15356. (PubMed:15105416)Curated
    Sequence conflicti771 – 7711S → T in AAT99567. (PubMed:15808839)Curated
    Sequence conflicti852 – 8543CTL → GTV in AAA96141. (PubMed:7527874)Curated
    Sequence conflicti966 – 9661G → V in BAD15356. (PubMed:15105416)Curated
    Sequence conflicti997 – 9982SF → FL in AAT99567. (PubMed:15808839)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB176831 mRNA. Translation: BAD15356.1.
    AF085195 mRNA. Translation: AAC34677.1.
    AY695391 mRNA. Translation: AAT99567.1.
    AJ011115 mRNA. Translation: CAA09493.1.
    AJ011116 mRNA. Translation: CAA09494.1.
    U02534 mRNA. Translation: AAA96141.1.
    AF093837 mRNA. Translation: AAC64178.1.
    U18336 mRNA. Translation: AAC52188.1.
    PIRiI51917.
    I56979.
    RefSeqiNP_068610.1. NM_021838.2.
    UniGeneiRn.44265.

    Genome annotation databases

    GeneIDi24600.
    KEGGirno:24600.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB176831 mRNA. Translation: BAD15356.1 .
    AF085195 mRNA. Translation: AAC34677.1 .
    AY695391 mRNA. Translation: AAT99567.1 .
    AJ011115 mRNA. Translation: CAA09493.1 .
    AJ011116 mRNA. Translation: CAA09494.1 .
    U02534 mRNA. Translation: AAA96141.1 .
    AF093837 mRNA. Translation: AAC64178.1 .
    U18336 mRNA. Translation: AAC52188.1 .
    PIRi I51917.
    I56979.
    RefSeqi NP_068610.1. NM_021838.2.
    UniGenei Rn.44265.

    3D structure databases

    ProteinModelPortali Q62600.
    SMRi Q62600. Positions 66-480, 728-1161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-41833N.
    IntActi Q62600. 2 interactions.
    MINTi MINT-202608.

    Chemistry

    BindingDBi Q62600.
    ChEMBLi CHEMBL1075230.

    PTM databases

    PhosphoSitei Q62600.

    Proteomic databases

    PRIDEi Q62600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24600.
    KEGGi rno:24600.

    Organism-specific databases

    CTDi 4846.
    RGDi 3186. Nos3.

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    InParanoidi Q62600.
    KOi K13242.
    PhylomeDBi Q62600.

    Enzyme and pathway databases

    SABIO-RK Q62600.

    Miscellaneous databases

    NextBioi 603808.

    Gene expression databases

    Genevestigatori Q62600.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 2 hits.
    3.90.340.10. 1 hit.
    InterProi IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity."
      Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.
      J. Biol. Chem. 279:29461-29468(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Downregulation of endothelial nitric oxide synthase (NOS III) in rat aorta following in-vivo hypoxia."
      Toporsian M., Govindaraju K., Nagi M., Eidelman D., Thibault G., Ward M.E.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-288.
      Strain: Sprague-Dawley.
    3. "Increased resistance to myocardial ischemia in the Brown Norway vs. Dahl S rat: role of nitric oxide synthase and Hsp90."
      Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr., Zhang C., Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E.
      J. Mol. Cell. Cardiol. 38:625-635(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-1202.
      Strain: SS/JrHsdMcwi.
      Tissue: Heart.
    4. "Cloning and expression of the rat endothelial nitric oxide synthase."
      Seidel B., Jiang L., Wolf G.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 473-672 AND 951-1192.
      Tissue: Brain.
    5. "Differential expression and induction of mRNAs encoding two inducible nitric oxide synthases in rat kidney."
      Mohaupt M.G., Elzie J.L., Ahn K.Y., Clapp W.L., Wilcox C.S., Kone B.C.
      Kidney Int. 46:653-665(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 633-862.
      Strain: Sprague-Dawley.
    6. "Endothelin-1, endothelin receptors and ecNOS mRNA expression in vital organs during traumatic shock in rats."
      Minchenko A.G., Armstead V.E., Opentanova I.L., Lefer A.M.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1015-1132.
      Strain: Sprague-Dawley.
      Tissue: Lung.
    7. "Constitutive endothelial nitric oxide synthase gene expression is regulated during lung development."
      Kawai N., Bloch D.B., Filippov G., Rabkina D., Suen H.C., Losty P.D., Janssens S.P., Zapol W.M., de la Monte S., Bloch K.D.
      Am. J. Physiol. 268:L589-L595(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1018-1080.
      Strain: Sprague-Dawley.
      Tissue: Lung.
    8. Cited for: PHOSPHORYLATION AT THR-494 AND SER-1176.

    Entry informationi

    Entry nameiNOS3_RAT
    AccessioniPrimary (citable) accession number: Q62600
    Secondary accession number(s): O88672
    , O89041, Q62734, Q68GV6, Q75NE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 of the entry and version 4 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

    External Data

    Dasty 3