SCNAA_RAT
ID SCNAA_RAT Reviewed; 1956 AA.
AC Q62968; Q63554; Q6EWG6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sodium channel protein type 10 subunit alpha;
DE AltName: Full=Peripheral nerve sodium channel 3;
DE Short=PN3;
DE AltName: Full=Sensory neuron sodium channel;
DE AltName: Full=Sodium channel protein type X subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.8;
GN Name=Scn10a; Synonyms=Sns;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND FUNCTION IN
RP VOLTAGE-EVOKED DEPOLARIZATION.
RC TISSUE=Spinal ganglion;
RX PubMed=8538791; DOI=10.1038/379257a0;
RA Akopian A.N., Sivilotti L., Wood J.N.;
RT "A tetrodotoxin-resistant voltage-gated sodium channel expressed by sensory
RT neurons.";
RL Nature 379:257-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX PubMed=8626372; DOI=10.1074/jbc.271.11.5953;
RA Sangameswaran L., Delgado S.G., Fish L.M., Koch B.D., Jakeman L.B.,
RA Stewart G.R., Sze P., Hunter J.C., Eglen R.M., Herman R.C.;
RT "Structure and function of a novel voltage-gated, tetrodotoxin-resistant
RT sodium channel specific to sensory neurons.";
RL J. Biol. Chem. 271:5953-5956(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND INTERACTION WITH SCN1B; SCN2B AND
RP SCN3B.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX PubMed=15178439; DOI=10.1016/j.bbrc.2004.05.026;
RA Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.;
RT "Role of auxiliary beta1-, beta2-, and beta3-subunits and their interaction
RT with Na(v)1.8 voltage-gated sodium channel.";
RL Biochem. Biophys. Res. Commun. 319:531-540(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 963-1097 (ISOFORMS 1 AND 2).
RC STRAIN=Wistar; TISSUE=Spinal ganglion, and Trigeminal ganglion;
RX PubMed=15047701; DOI=10.1074/jbc.m401281200;
RA Kerr N.C.H., Holmes F.E., Wynick D.;
RT "Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced by a
RT conserved mechanism in mouse and rat.";
RL J. Biol. Chem. 279:24826-24833(2004).
RN [5]
RP INDUCTION.
RX PubMed=9450690; DOI=10.1016/s0169-328x(97)00239-8;
RA Oaklander A.L., Belzberg A.J.;
RT "Unilateral nerve injury down-regulates mRNA for Na+ channel SCN10A
RT bilaterally in rat dorsal root ganglia.";
RL Brain Res. Mol. Brain Res. 52:162-165(1997).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11487631; DOI=10.1523/jneurosci.21-16-06077.2001;
RA Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.;
RT "Developmental expression of the TTX-resistant voltage-gated sodium
RT channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons.";
RL J. Neurosci. 21:6077-6085(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH S100A10.
RX PubMed=12050667; DOI=10.1038/nature00781;
RA Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V.,
RA Wood J.N.;
RT "Annexin II light chain regulates sensory neuron-specific sodium channel
RT expression.";
RL Nature 417:653-656(2002).
RN [8]
RP INTERACTION WITH FSTL1; PRX; DYNLT1 AND PDZD2, AND IDENTIFICATION IN
RP COMPLEXES WITH PRX; DYNLT1 AND PDZD2.
RX PubMed=12591166; DOI=10.1016/s0169-328x(02)00661-7;
RA Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
RT "Sensory neuron proteins interact with the intracellular domains of sodium
RT channel NaV1.8.";
RL Brain Res. Mol. Brain Res. 110:298-304(2003).
RN [9]
RP FUNCTION IN PAIN.
RX PubMed=12514212; DOI=10.1523/jneurosci.23-01-00158.2003;
RA Gold M.S., Weinreich D., Kim C.-S., Wang R., Treanor J., Porreca F.,
RA Lai J.;
RT "Redistribution of Na(V)1.8 in uninjured axons enables neuropathic pain.";
RL J. Neurosci. 23:158-166(2003).
CC -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-
CC dependent sodium ion permeability of excitable membranes. Assuming
CC opened or closed conformations in response to the voltage difference
CC across the membrane, the protein forms a sodium-selective channel
CC through which sodium ions may pass in accordance with their
CC electrochemical gradient. Plays a role in neuropathic pain mechanisms.
CC {ECO:0000269|PubMed:12514212, ECO:0000269|PubMed:8538791,
CC ECO:0000269|PubMed:8626372}.
CC -!- SUBUNIT: The channel consists of an ion conducting pore forming alpha-
CC subunit regulated by one or more associated auxiliary subunits SCN1B,
CC SCN2B and SCN3B; electrophysiological properties may vary depending on
CC the type of the associated beta subunits. Found in a number of
CC complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as
CC FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others. Interacts with
CC NEDD4 and NEDD4L. {ECO:0000269|PubMed:12050667,
CC ECO:0000269|PubMed:12591166, ECO:0000269|PubMed:15178439}.
CC -!- INTERACTION:
CC Q62968; Q9Z336: Dynlt1; NbExp=2; IntAct=EBI-1800320, EBI-920359;
CC Q62968; Q63425: Prx; NbExp=2; IntAct=EBI-1800320, EBI-1800492;
CC Q62968; P05943: S100a10; NbExp=4; IntAct=EBI-1800320, EBI-1800351;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can
CC be translocated to the cell membrane through association with S100A10.
CC {ECO:0000269|PubMed:12050667}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62968-1; Sequence=Displayed;
CC Name=2; Synonyms=Nav1.8c;
CC IsoId=Q62968-2; Sequence=VSP_012258;
CC -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglia, trigeminal
CC ganglia, nodose ganglia and sciatic nerve.
CC {ECO:0000269|PubMed:11487631, ECO:0000269|PubMed:8538791,
CC ECO:0000269|PubMed:8626372}.
CC -!- DEVELOPMENTAL STAGE: Expressed in dorsal root ganglia at 15 dpc
CC onwards. {ECO:0000269|PubMed:11487631}.
CC -!- INDUCTION: Down-regulated after axotomy in dorsal root ganglia.
CC {ECO:0000269|PubMed:9450690}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC This cysteine (position 815) is speculated in other sodium channel
CC subunits alpha to be implied in covalent binding with the sodium
CC channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.8/SCN10A subfamily. {ECO:0000305}.
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DR EMBL; X92184; CAA63095.1; -; mRNA.
DR EMBL; U53833; AAC52619.1; -; Genomic_DNA.
DR EMBL; AJ623271; CAF25041.1; -; mRNA.
DR PIR; S68453; S68453.
DR RefSeq; NP_058943.1; NM_017247.1. [Q62968-1]
DR AlphaFoldDB; Q62968; -.
DR SMR; Q62968; -.
DR BioGRID; 248204; 2.
DR CORUM; Q62968; -.
DR ELM; Q62968; -.
DR IntAct; Q62968; 23.
DR STRING; 10116.ENSRNOP00000047944; -.
DR BindingDB; Q62968; -.
DR ChEMBL; CHEMBL4017; -.
DR DrugCentral; Q62968; -.
DR GuidetoPHARMACOLOGY; 585; -.
DR TCDB; 1.A.1.10.6; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q62968; 8 sites.
DR iPTMnet; Q62968; -.
DR PhosphoSitePlus; Q62968; -.
DR PaxDb; Q62968; -.
DR PRIDE; Q62968; -.
DR ABCD; Q62968; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000046864; ENSRNOP00000047944; ENSRNOG00000032473. [Q62968-1]
DR GeneID; 29571; -.
DR KEGG; rno:29571; -.
DR UCSC; RGD:3629; rat. [Q62968-1]
DR CTD; 6336; -.
DR RGD; 3629; Scn10a.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154992; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; Q62968; -.
DR OMA; CCKVDTT; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q62968; -.
DR TreeFam; TF323985; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:Q62968; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000032473; Expressed in testis.
DR Genevisible; Q62968; RN.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0044299; C:C-fiber; ISO:RGD.
DR GO; GO:0071439; C:clathrin complex; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR GO; GO:0086016; P:AV node cell action potential; ISO:RGD.
DR GO; GO:0086043; P:bundle of His cell action potential; ISO:RGD.
DR GO; GO:0061337; P:cardiac conduction; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028809; Na_channel_a10su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF208; PTHR10037:SF208; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1956
FT /note="Sodium channel protein type 10 subunit alpha"
FT /id="PRO_0000048509"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..149
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..174
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..206
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..212
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..232
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..272
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..340
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 341..365
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 366..372
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..398
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 659..683
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..718
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 727..746
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..752
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 753..772
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 789..809
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..833
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 834..854
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 855..863
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 864..889
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..1148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1149..1172
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1173..1185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1186..1211
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1212..1217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1218..1239
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1240..1243
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1244..1265
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1266..1284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1285..1312
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1313..1354
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1355..1376
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1377..1392
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1393..1419
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1420..1472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1473..1496
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1497..1507
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1508..1531
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1532..1537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1538..1561
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1562..1573
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1574..1595
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1596..1610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1611..1633
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1634..1647
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1648..1670
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1671..1698
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1699..1723
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1724..1956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 116..404
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 646..910
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1141..1450
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1459..1758
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1852..1881
FT /note="IQ"
FT REGION 31..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1906..1956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 1452
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 276..318
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 856..865
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VAR_SEQ 1030
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15047701"
FT /id="VSP_012258"
FT CONFLICT 59
FT /note="A -> D (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="A -> E (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="T -> TP (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="D -> H (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="F -> L (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="R -> H (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
FT CONFLICT 1896
FT /note="V -> I (in Ref. 1; CAA63095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1956 AA; 219733 MW; 8FC58EDAD263AC67 CRC64;
MELPFASVGT TNFRRFTPES LAEIEKQIAA HRAAKKARTK HRGQEDKGEK PRPQLDLKAC
NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKSRT ISRFSATWAL WLFSPFNLIR
RTAIKVSVHS WFSIFITITI LVNCVCMTRT DLPEKVEYVF TVIYTFEALI KILARGFCLN
EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIRNG TDPHKADNLS SEMAEYIFIK
PGTTDPLLCG NGSDAGHCPG GYVCLKTPDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFQEA
LEVLQKEQEV LAALGIDTTS LQSHSGSPLA SKNANERRPR VKSRVSEGST DDNRSPQSDP
YNQRRMSFLG LSSGRRRASH GSVFHFRAPS QDISFPDGIT DDGVFHGDQE SRRGSILLGR
GAGQTGPLPR SPLPQSPNPG RRHGEEGQLG VPTGELTAGA PEGPALDTTG QKSFLSAGYL
NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISFAQK YLIWECCPKW RKFKMALFEL
VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP
YYYFQKKWNI FDCVIVTVSL LELSASKKGS LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG
NSVGALGNLT FILAIIVFIF ALVGKQLLSE DYGCRKDGVS VWNGEKLRWH MCDFFHSFLV
VFRILCGEWI ENMWVCMEVS QKSICLILFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
EDDGEVNNLQ LALARIQVLG HRASRAIASY ISSHCRFRWP KVETQLGMKP PLTSSEAKNH
IATDAVSAAV GNLTKPALSS PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDMEQASQS
SWQEEDPKGQ QEQLPQVQKC ENHQAARSPA SMMSSEDLAP YLGESWKRKD SPQVPAEGVD
DTSSSEGSTV DCPDPEEILR KIPELADDLD EPDDCFTEGC TRRCPCCNVN TSKSPWATGW
QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR
ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSK CVDTRNNPFS
NVNSTMVNNK SECHNQNSTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS
GEINSQPNWE NNLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMVLICLN MITMMVETDE
QGEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SIGSLLFSAI
LKSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
IYSIFGMASF ANVVDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
PNLPNSNGSR GNCGSPAVGI IFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED
DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRWK QEDLSATVIQ
KAYRSYMLHR SLTLSNTLHV PRAEEDGVSL PGEGYVTFMA NSGLPDKSET ASATSFPPSY
DSVTRGLSDR ANINPSSSMQ NEDEVAAKEG NSPGPQ
