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P0DMA5

- SCNAA_ONYTO

UniProt

P0DMA5 - SCNAA_ONYTO

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
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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        10         20         30         40         50
MEFPIGSVGT TNFRRFTPES LAEIEKQIAA HGAAKKARAK HGERKGQDEK
60 70 80 90 100
PRPQLDLKAC NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKGRT
110 120 130 140 150
ISRFSATWAL WLFSPFNLIR RTAIKVSVHA WFSIFITITI LFNCVCMTQN
160 170 180 190 200
DLPEKIEYAF TVIYTFEALI KILARGFCLN EFTYLRDPWN WLDFSVITLA
210 220 230 240 250
YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVRKLADVT
260 270 280 290 300
ILTVFCLSVF ALVGLQLFKG NLKNKCIKRS TDPHNAYNFS SQMADNFYIK
310 320 330 340 350
NGTTEPLLCG NGSDAGHCPS GYICLKTSDN PDFNYTSFDS FAWAFLSLFR
360 370 380 390 400
LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE
410 420 430 440 450
EQNQATIAEI EAKEKKFQEA LEVLQKEQEV LAALGIDTTS LHSHNGSPLA
460 470 480 490 500
PKNANERKHR IKSRVSEGST DDNRSPQSDP YNQRRMSFLG LSSGRRRASH
510 520 530 540 550
SSVFHFRAPS QDVSFPDGIT DDGVFHGDHE SHRSSLLLAR GAGQAGPLPR
560 570 580 590 600
SPLASSPNPG PGHREEGQLT APTGELTTGA PEDLALEAAG QKKNFLSAEY
610 620 630 640 650
LNEPFRAQRA MSVVSIMTSV IEELEESKLR CPPCLINLAQ KYLIWECCPK
660 670 680 690 700
WMKFKMVLFE LVTDPFAELT ITLCIVVNTI FMAMEHYPMT DAFDAMLQAG
710 720 730 740 750
NIVFTVFFTM EMAFKIIAFD PYYYFQKKWN VFDCVIVTVS LLELSIAKKG
760 770 780 790 800
SLSVLRTFRL LRVFKLAKSW PTLNTLIKII GNSVGALGNL TFILAIIVFI
810 820 830 840 850
FALVGKQLLG EDYGCRKDGT ALWNEGQLRW HMCDFFHSFL VIFRILCGEW
860 870 880 890 900
IENMWVCMQV SEKSICLILF LTVMVLGNLV VLNLFIALLL NSFSADNLTA
910 920 930 940 950
PEDDGEVNNL QVALARTQAF GQRASQAISS YFSSHCRLRW PKVGSQLGVK
960 970 980 990 1000
PSLTSSKAEH HITADAVNTA VGTSAKPALS GPKEDPRDFI TDANVWVSVP
1010 1020 1030 1040 1050
IAEGESDLDE LEEDIEQNSQ SSWREESPKG QQDQLWQIQR CEDHQVPNSP
1060 1070 1080 1090 1100
GSGMSSEDLA SYLGERWKSE ATPQVPAEGV DDTSSSEGST VDCPDPEEIL
1110 1120 1130 1140 1150
KKIPELADDL EEPDDCFTEG CTRHCPCCKV STSKFPWTTG WQVRKTCYRI
1160 1170 1180 1190 1200
VEHSWFESFI IFMILLSSGA LAFEDNYLEQ KPRVKSMLEY TDRVFTFIFV
1210 1220 1230 1240 1250
FEMLLKWVAY GFKKYFTNAW CWLDFLIVNI SLTSLIAKIL DYSDVASLKA
1260 1270 1280 1290 1300
LRTLRALRPL RALSRFEGMR VVVDALVGAI PSIMNVLLVC LIFWLIFSIM
1310 1320 1330 1340 1350
GVNLFAGKFS RCIDTSNNPF SVVNSTIVNN KSECRNQNHT GHFFWVNVKV
1360 1370 1380 1390 1400
NFDNVAMGYL ALLQVATFKG WMDIMYAAVD SREINSQPQW EDNLYMYLYF
1410 1420 1430 1440 1450
VVFIIFGGFF TLNLFVGVII DNFNQQKKKL GGQDIFMTEE QKKYYNAMKK
1460 1470 1480 1490 1500
LGSKKPQKPI PRPLNKYQGF VFDIVTRQAF DIIIMVLICL NMITMMVETD
1510 1520 1530 1540 1550
GQSEEKTKIL GRINQFFVAV FTGECVMKMF ALRQYYFTNG WNVFDFIVVI
1560 1570 1580 1590 1600
LSIGSLVFSA ILKSLESYFS PTLFRVIRLA RIGRILRLIR AAKGIRTLLF
1610 1620 1630 1640 1650
ALMMSLPALF NIGLLLFLVM FIYSIFGMAS FANVVEEAGI DDMFNFQTFG
1660 1670 1680 1690 1700
NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLSNNNTS KGNCGSPTVG
1710 1720 1730 1740 1750
IVFFTTYIII SFLIVVNMYI AVILENFNVA TEESTEPLSE DDFDMFYETW
1760 1770 1780 1790 1800
EKFDPEATQF IAFSALSDFA DTLSGPLRIP KPNQNILIQM DLPLVPGDKI
1810 1820 1830 1840 1850
HCLDILFAFT KNVLGESGEL DSLKTNMEEK FMATNLSKAS YEPIATTLRW
1860 1870 1880 1890 1900
KQEDISATVI QKAYRSYVLQ RSLTLSNPLR VPRAEDDDAP LPGEGYVTFM
1910 1920 1930 1940 1950
ANDSGRLPDK SETTSATSFP PSYDSVTRGL SDRVNISTSN SMHNEDEVTS

KEGDSPGPQ
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 29, 2014
This is version 9 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