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P0DMA5

- SCNAA_ONYTO

UniProt

P0DMA5 - SCNAA_ONYTO

Protein

Sodium channel protein type 10 subunit alpha

Gene

Scn10a

Organism
Onychomys torridus (Southern grasshopper mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 8 (01 Oct 2014)
      Sequence version 1 (22 Jan 2014)
      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.1 Publication

    GO - Molecular functioni

    1. voltage-gated sodium channel activity Source: InterPro

    GO - Biological processi

    1. sensory perception of pain Source: InterPro

    Keywords - Molecular functioni

    Ion channel, Sodium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Sodium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium channel protein type 10 subunit alpha
    Gene namesi
    Name:Scn10a
    Synonyms:Sns
    OrganismiOnychomys torridus (Southern grasshopper mouse)
    Taxonomic identifieri38674 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeNeotominaeOnychomys

    Subcellular locationi

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

    GO - Cellular componenti

    1. voltage-gated sodium channel complex Source: InterPro

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi746 – 7472IA → TS: No effect on inhibition by the venom of Centruroides sculpturatus.
    Mutagenesisi859 – 8591Q → E: Complete loss of inhibition by the venom of Centruroides sculpturatus; when associated with Q-862. 1 Publication
    Mutagenesisi862 – 8621E → Q: Almost complete loss of inhibition by the venom of Centruroides sculpturatus. Complete loss of inhibition by the venom of Centruroides sculpturatus; when associated with E-859. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19591959Sodium channel protein type 10 subunit alphaPRO_0000424959Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1453 – 14531Phosphoserine; by PKCBy similarity

    Post-translational modificationi

    Ubiquitinated by NEDD4L; which promotes its endocytosis.Curated
    Phosphorylation at Ser-1453 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

    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 By similarity.By similarity

    Structurei

    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
    Transmembranei660 – 68425Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei696 – 71924Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei728 – 74720Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei754 – 77320Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei790 – 81021Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei865 – 89026Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1150 – 117324Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1187 – 121226Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1219 – 124022Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1245 – 126622Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1286 – 131328Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1394 – 142027Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1474 – 149724Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1509 – 153224Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1539 – 156224Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1575 – 159622Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1612 – 163423Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1700 – 172425Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati125 – 399275IAdd
    BLAST
    Repeati659 – 891233IIAdd
    BLAST
    Repeati1149 – 1421273IIIAdd
    BLAST
    Repeati1473 – 1725253IVAdd
    BLAST
    Domaini1853 – 188230IQAdd
    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

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR000048. IQ_motif_EF-hand-BS.
    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.
    SMARTiSM00015. IQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0DMA5-1 [UniParc]FASTAAdd to Basket

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    MEFPIGSVGT TNFRRFTPES LAEIEKQIAA HGAAKKARAK HGERKGQDEK     50
    PRPQLDLKAC NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKGRT 100
    ISRFSATWAL WLFSPFNLIR RTAIKVSVHA WFSIFITITI LFNCVCMTQN 150
    DLPEKIEYAF TVIYTFEALI KILARGFCLN EFTYLRDPWN WLDFSVITLA 200
    YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVRKLADVT 250
    ILTVFCLSVF ALVGLQLFKG NLKNKCIKRS TDPHNAYNFS SQMADNFYIK 300
    NGTTEPLLCG NGSDAGHCPS GYICLKTSDN PDFNYTSFDS FAWAFLSLFR 350
    LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE 400
    EQNQATIAEI EAKEKKFQEA LEVLQKEQEV LAALGIDTTS LHSHNGSPLA 450
    PKNANERKHR IKSRVSEGST DDNRSPQSDP YNQRRMSFLG LSSGRRRASH 500
    SSVFHFRAPS QDVSFPDGIT DDGVFHGDHE SHRSSLLLAR GAGQAGPLPR 550
    SPLASSPNPG PGHREEGQLT APTGELTTGA PEDLALEAAG QKKNFLSAEY 600
    LNEPFRAQRA MSVVSIMTSV IEELEESKLR CPPCLINLAQ KYLIWECCPK 650
    WMKFKMVLFE LVTDPFAELT ITLCIVVNTI FMAMEHYPMT DAFDAMLQAG 700
    NIVFTVFFTM EMAFKIIAFD PYYYFQKKWN VFDCVIVTVS LLELSIAKKG 750
    SLSVLRTFRL LRVFKLAKSW PTLNTLIKII GNSVGALGNL TFILAIIVFI 800
    FALVGKQLLG EDYGCRKDGT ALWNEGQLRW HMCDFFHSFL VIFRILCGEW 850
    IENMWVCMQV SEKSICLILF LTVMVLGNLV VLNLFIALLL NSFSADNLTA 900
    PEDDGEVNNL QVALARTQAF GQRASQAISS YFSSHCRLRW PKVGSQLGVK 950
    PSLTSSKAEH HITADAVNTA VGTSAKPALS GPKEDPRDFI TDANVWVSVP 1000
    IAEGESDLDE LEEDIEQNSQ SSWREESPKG QQDQLWQIQR CEDHQVPNSP 1050
    GSGMSSEDLA SYLGERWKSE ATPQVPAEGV DDTSSSEGST VDCPDPEEIL 1100
    KKIPELADDL EEPDDCFTEG CTRHCPCCKV STSKFPWTTG WQVRKTCYRI 1150
    VEHSWFESFI IFMILLSSGA LAFEDNYLEQ KPRVKSMLEY TDRVFTFIFV 1200
    FEMLLKWVAY GFKKYFTNAW CWLDFLIVNI SLTSLIAKIL DYSDVASLKA 1250
    LRTLRALRPL RALSRFEGMR VVVDALVGAI PSIMNVLLVC LIFWLIFSIM 1300
    GVNLFAGKFS RCIDTSNNPF SVVNSTIVNN KSECRNQNHT GHFFWVNVKV 1350
    NFDNVAMGYL ALLQVATFKG WMDIMYAAVD SREINSQPQW EDNLYMYLYF 1400
    VVFIIFGGFF TLNLFVGVII DNFNQQKKKL GGQDIFMTEE QKKYYNAMKK 1450
    LGSKKPQKPI PRPLNKYQGF VFDIVTRQAF DIIIMVLICL NMITMMVETD 1500
    GQSEEKTKIL GRINQFFVAV FTGECVMKMF ALRQYYFTNG WNVFDFIVVI 1550
    LSIGSLVFSA ILKSLESYFS PTLFRVIRLA RIGRILRLIR AAKGIRTLLF 1600
    ALMMSLPALF NIGLLLFLVM FIYSIFGMAS FANVVEEAGI DDMFNFQTFG 1650
    NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLSNNNTS KGNCGSPTVG 1700
    IVFFTTYIII SFLIVVNMYI AVILENFNVA TEESTEPLSE DDFDMFYETW 1750
    EKFDPEATQF IAFSALSDFA DTLSGPLRIP KPNQNILIQM DLPLVPGDKI 1800
    HCLDILFAFT KNVLGESGEL DSLKTNMEEK FMATNLSKAS YEPIATTLRW 1850
    KQEDISATVI QKAYRSYVLQ RSLTLSNPLR VPRAEDDDAP LPGEGYVTFM 1900
    ANDSGRLPDK SETTSATSFP PSYDSVTRGL SDRVNISTSN SMHNEDEVTS 1950
    KEGDSPGPQ 1959
    Length:1,959
    Mass (Da):220,523
    Last modified:January 22, 2014 - v1
    Checksum:iFE84EC9345B5EB74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    KF717604 mRNA. Translation: AHA38158.1.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    A pain soothed - Issue 157 of January 2014

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    KF717604 mRNA. Translation: AHA38158.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR000048. IQ_motif_EF-hand-BS.
    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.
    SMARTi SM00015. IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Voltage-gated sodium channel in grasshopper mice defends against bark scorpion toxin."
      Rowe A.H., Xiao Y., Rowe M.P., Cummins T.R., Zakon H.H.
      Science 342:441-446(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF 746-ILE-ALA-747; GLN-859 AND GLU-862.

    Entry informationi

    Entry nameiSCNAA_ONYTO
    AccessioniPrimary (citable) accession number: P0DMA5
    Secondary accession number(s): U6BRW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 22, 2014
    Last sequence update: January 22, 2014
    Last modified: October 1, 2014
    This is version 8 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    O.torridus is resistant to the pain-inducing components of the venom of its prey, the bark scorpion (Centruroides sculpturatus). It is most probably due to the unique inhibition by some venom components of the Scn10a sodium-channel in those rodents. Inhibition of Snc10a would, in turn, inhibit sodium currents, block action potential propagation and induce analgesia. Glu-862 plays a central role in that inhibition and its replacement by a Gln, the corresponding amino acid found in the M.musculus ortholog, prevents the inhibition of Snc10a. This would explain why the venom induces pain in M.musculus but not in O.torridus (PubMed:24159039).1 Publication

    Documents

    1. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3