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Q62968

- SCNAA_RAT

UniProt

Q62968 - SCNAA_RAT

Protein

Sodium channel protein type 10 subunit alpha

Gene

Scn10a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. voltage-gated sodium channel activity Source: RGD

    GO - Biological processi

    1. membrane depolarization during action potential Source: RefGenome
    2. neuronal action potential Source: RefGenome
    3. odontogenesis of dentin-containing tooth Source: RGD
    4. sensory perception of pain Source: RGD
    5. sodium ion transmembrane transport Source: GOC
    6. sodium ion transport Source: RGD

    Keywords - Molecular functioni

    Ion channel, Sodium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Sodium

    Protein family/group databases

    TCDBi1.A.1.10.6. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium channel protein type 10 subunit alpha
    Alternative name(s):
    Peripheral nerve sodium channel 3
    Short name:
    PN3
    Sensory neuron sodium channel
    Sodium channel protein type X subunit alpha
    Voltage-gated sodium channel subunit alpha Nav1.8
    Gene namesi
    Name:Scn10a
    Synonyms:Sns
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3629. Scn10a.

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity
    Note: It can be translocated to the extracellular membrane through association with S100A10.1 Publication

    GO - Cellular componenti

    1. clathrin complex Source: RGD
    2. integral component of membrane Source: RGD
    3. plasma membrane Source: RefGenome
    4. voltage-gated sodium channel complex Source: InterPro

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19561956Sodium channel protein type 10 subunit alphaPRO_0000048509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1323 – 13231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1329 – 13291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1337 – 13371N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1452 – 14521Phosphoserine; by PKCBy similarity
    Glycosylationi1687 – 16871N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Ubiquitinated by NEDD4L; which promotes its endocytosis.By similarity
    Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ62968.
    PRIDEiQ62968.

    PTM databases

    PhosphoSiteiQ62968.

    Expressioni

    Tissue specificityi

    Expressed in dorsal root ganglia, trigeminal ganglia, nodose ganglia and sciatic nerve.3 Publications

    Developmental stagei

    Expressed in dorsal root ganglia at 15 dpc onwards.1 Publication

    Inductioni

    Down-regulated after axotomy in dorsal root ganglia.1 Publication

    Gene expression databases

    GenevestigatoriQ62968.

    Interactioni

    Subunit structurei

    The channel consists of an ion conducting pore forming alpha-subunit regulated by one or more associated auxiliary subunits SCN1B, SCN2B and SCN3B; electrophysiological properties may vary depending on the type of the associated beta subunits. Found in a number of complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others. Interacts with NEDD4 and NEDD4L.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dynlt1Q9Z3362EBI-1800320,EBI-920359
    PrxQ634252EBI-1800320,EBI-1800492
    S100a10P059434EBI-1800320,EBI-1800351

    Protein-protein interaction databases

    IntActiQ62968. 23 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62968.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei126 – 14924Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei155 – 17420Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei188 – 20619Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei213 – 23220Helical; Voltage-sensor; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei249 – 27224Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei373 – 39826Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei659 – 68325Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei695 – 71824Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei727 – 74620Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei753 – 77220Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei789 – 80921Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei864 – 88926Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1149 – 117224Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1186 – 121126Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1218 – 123922Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1244 – 126522Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1285 – 131228Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1393 – 141927Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1473 – 149624Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1508 – 153124Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1538 – 156124Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1574 – 159522Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1611 – 163323Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1699 – 172325Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati125 – 399275IAdd
    BLAST
    Repeati658 – 890233IIAdd
    BLAST
    Repeati1148 – 1420273IIIAdd
    BLAST
    Repeati1472 – 1724253IVAdd
    BLAST
    Domaini1852 – 188130IQAdd
    BLAST

    Domaini

    The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position.

    Sequence similaritiesi

    Contains 1 IQ domain.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231755.
    HOVERGENiHBG053100.
    InParanoidiQ62968.
    KOiK04842.
    PhylomeDBiQ62968.
    TreeFamiTF323985.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR028809. Na_channel_a10su.
    IPR001696. Na_channel_asu.
    IPR010526. Na_trans_assoc.
    [Graphical view]
    PANTHERiPTHR10037:SF23. PTHR10037:SF23. 1 hit.
    PfamiPF00520. Ion_trans. 4 hits.
    PF06512. Na_trans_assoc. 1 hit.
    [Graphical view]
    PRINTSiPR00170. NACHANNEL.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q62968-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MELPFASVGT TNFRRFTPES LAEIEKQIAA HRAAKKARTK HRGQEDKGEK     50
    PRPQLDLKAC NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKSRT 100
    ISRFSATWAL WLFSPFNLIR RTAIKVSVHS WFSIFITITI LVNCVCMTRT 150
    DLPEKVEYVF TVIYTFEALI KILARGFCLN EFTYLRDPWN WLDFSVITLA 200
    YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVRKLADVT 250
    ILTVFCLSVF ALVGLQLFKG NLKNKCIRNG TDPHKADNLS SEMAEYIFIK 300
    PGTTDPLLCG NGSDAGHCPG GYVCLKTPDN PDFNYTSFDS FAWAFLSLFR 350
    LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE 400
    EQSQATIAEI EAKEKKFQEA LEVLQKEQEV LAALGIDTTS LQSHSGSPLA 450
    SKNANERRPR VKSRVSEGST DDNRSPQSDP YNQRRMSFLG LSSGRRRASH 500
    GSVFHFRAPS QDISFPDGIT DDGVFHGDQE SRRGSILLGR GAGQTGPLPR 550
    SPLPQSPNPG RRHGEEGQLG VPTGELTAGA PEGPALDTTG QKSFLSAGYL 600
    NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISFAQK YLIWECCPKW 650
    RKFKMALFEL VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN 700
    IVFTVFFTME MAFKIIAFDP YYYFQKKWNI FDCVIVTVSL LELSASKKGS 750
    LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG NSVGALGNLT FILAIIVFIF 800
    ALVGKQLLSE DYGCRKDGVS VWNGEKLRWH MCDFFHSFLV VFRILCGEWI 850
    ENMWVCMEVS QKSICLILFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP 900
    EDDGEVNNLQ LALARIQVLG HRASRAIASY ISSHCRFRWP KVETQLGMKP 950
    PLTSSEAKNH IATDAVSAAV GNLTKPALSS PKENHGDFIT DPNVWVSVPI 1000
    AEGESDLDEL EEDMEQASQS SWQEEDPKGQ QEQLPQVQKC ENHQAARSPA 1050
    SMMSSEDLAP YLGESWKRKD SPQVPAEGVD DTSSSEGSTV DCPDPEEILR 1100
    KIPELADDLD EPDDCFTEGC TRRCPCCNVN TSKSPWATGW QVRKTCYRIV 1150
    EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF 1200
    EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL 1250
    RTLRALRPLR ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG 1300
    VNLFAGKFSK CVDTRNNPFS NVNSTMVNNK SECHNQNSTG HFFWVNVKVN 1350
    FDNVAMGYLA LLQVATFKGW MDIMYAAVDS GEINSQPNWE NNLYMYLYFV 1400
    VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ KKYYNAMKKL 1450
    GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMVLICLN MITMMVETDE 1500
    QGEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL 1550
    SIGSLLFSAI LKSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA 1600
    LMMSLPALFN IGLLLFLVMF IYSIFGMASF ANVVDEAGID DMFNFKTFGN 1650
    SMLCLFQITT SAGWDGLLSP ILNTGPPYCD PNLPNSNGSR GNCGSPAVGI 1700
    IFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED DFDMFYETWE 1750
    KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH 1800
    CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRWK 1850
    QEDLSATVIQ KAYRSYMLHR SLTLSNTLHV PRAEEDGVSL PGEGYVTFMA 1900
    NSGLPDKSET ASATSFPPSY DSVTRGLSDR ANINPSSSMQ NEDEVAAKEG 1950
    NSPGPQ 1956
    Length:1,956
    Mass (Da):219,733
    Last modified:November 1, 1996 - v1
    Checksum:i8FC58EDAD263AC67
    GO
    Isoform 2 (identifier: Q62968-2) [UniParc]FASTAAdd to Basket

    Also known as: Nav1.8c

    The sequence of this isoform differs from the canonical sequence as follows:
         1030-1030: Missing.

    Show »
    Length:1,955
    Mass (Da):219,605
    Checksum:i4C6677DF46388F43
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591A → D in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti432 – 4321A → E in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti520 – 5201T → TP in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti587 – 5871D → H in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti757 – 7571F → L in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti938 – 9381R → H in CAA63095. (PubMed:8538791)Curated
    Sequence conflicti1896 – 18961V → I in CAA63095. (PubMed:8538791)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1030 – 10301Missing in isoform 2. 1 PublicationVSP_012258

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92184 mRNA. Translation: CAA63095.1.
    U53833 Genomic DNA. Translation: AAC52619.1.
    AJ623271 mRNA. Translation: CAF25041.1.
    PIRiS68453.
    RefSeqiNP_058943.1. NM_017247.1.
    XP_006244144.1. XM_006244082.1. [Q62968-2]
    UniGeneiRn.10246.

    Genome annotation databases

    GeneIDi29571.
    KEGGirno:29571.
    UCSCiRGD:3629. rat. [Q62968-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92184 mRNA. Translation: CAA63095.1 .
    U53833 Genomic DNA. Translation: AAC52619.1 .
    AJ623271 mRNA. Translation: CAF25041.1 .
    PIRi S68453.
    RefSeqi NP_058943.1. NM_017247.1.
    XP_006244144.1. XM_006244082.1. [Q62968-2 ]
    UniGenei Rn.10246.

    3D structure databases

    ProteinModelPortali Q62968.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q62968. 23 interactions.

    Chemistry

    BindingDBi Q62968.
    ChEMBLi CHEMBL4017.
    GuidetoPHARMACOLOGYi 585.

    Protein family/group databases

    TCDBi 1.A.1.10.6. the voltage-gated ion channel (vic) superfamily.

    PTM databases

    PhosphoSitei Q62968.

    Proteomic databases

    PaxDbi Q62968.
    PRIDEi Q62968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29571.
    KEGGi rno:29571.
    UCSCi RGD:3629. rat. [Q62968-1 ]

    Organism-specific databases

    CTDi 6336.
    RGDi 3629. Scn10a.

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231755.
    HOVERGENi HBG053100.
    InParanoidi Q62968.
    KOi K04842.
    PhylomeDBi Q62968.
    TreeFami TF323985.

    Miscellaneous databases

    NextBioi 609654.
    PROi Q62968.

    Gene expression databases

    Genevestigatori Q62968.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR028809. Na_channel_a10su.
    IPR001696. Na_channel_asu.
    IPR010526. Na_trans_assoc.
    [Graphical view ]
    PANTHERi PTHR10037:SF23. PTHR10037:SF23. 1 hit.
    Pfami PF00520. Ion_trans. 4 hits.
    PF06512. Na_trans_assoc. 1 hit.
    [Graphical view ]
    PRINTSi PR00170. NACHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "A tetrodotoxin-resistant voltage-gated sodium channel expressed by sensory neurons."
      Akopian A.N., Sivilotti L., Wood J.N.
      Nature 379:257-262(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
      Tissue: Spinal ganglion.
    2. "Structure and function of a novel voltage-gated, tetrodotoxin-resistant sodium channel specific to sensory neurons."
      Sangameswaran L., Delgado S.G., Fish L.M., Koch B.D., Jakeman L.B., Stewart G.R., Sze P., Hunter J.C., Eglen R.M., Herman R.C.
      J. Biol. Chem. 271:5953-5956(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
      Strain: Sprague-Dawley.
      Tissue: Spinal ganglion.
    3. "Role of auxiliary beta1-, beta2-, and beta3-subunits and their interaction with Na(v)1.8 voltage-gated sodium channel."
      Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.
      Biochem. Biophys. Res. Commun. 319:531-540(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), INTERACTION WITH SCN1B; SCN2B AND SCN3B.
      Strain: Sprague-Dawley.
      Tissue: Spinal ganglion.
    4. "Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced by a conserved mechanism in mouse and rat."
      Kerr N.C.H., Holmes F.E., Wynick D.
      J. Biol. Chem. 279:24826-24833(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 963-1097 (ISOFORMS 1 AND 2).
      Strain: Wistar.
      Tissue: Spinal ganglion and Trigeminal ganglion.
    5. "Unilateral nerve injury down-regulates mRNA for Na+ channel SCN10A bilaterally in rat dorsal root ganglia."
      Oaklander A.L., Belzberg A.J.
      Brain Res. Mol. Brain Res. 52:162-165(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Developmental expression of the TTX-resistant voltage-gated sodium channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons."
      Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.
      J. Neurosci. 21:6077-6085(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Annexin II light chain regulates sensory neuron-specific sodium channel expression."
      Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V., Wood J.N.
      Nature 417:653-656(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH S100A10.
    8. "Sensory neuron proteins interact with the intracellular domains of sodium channel NaV1.8."
      Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.
      Brain Res. Mol. Brain Res. 110:298-304(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FSTL1; PRX; DYNLT1 AND PDZD2, IDENTIFICATION IN COMPLEXES WITH PRX; DYNLT1 AND PDZD2.
    9. "Redistribution of Na(V)1.8 in uninjured axons enables neuropathic pain."
      Gold M.S., Weinreich D., Kim C.-S., Wang R., Treanor J., Porreca F., Lai J.
      J. Neurosci. 23:158-166(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PAIN.

    Entry informationi

    Entry nameiSCNAA_RAT
    AccessioniPrimary (citable) accession number: Q62968
    Secondary accession number(s): Q63554, Q6EWG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 112 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

    External Data

    Dasty 3