CAC1S_RAT
ID CAC1S_RAT Reviewed; 1850 AA.
AC Q02485; B3XZL8; P70484; Q01553; Q62817;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle;
DE AltName: Full=ROB1;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
GN Name=Cacna1s; Synonyms=Cach1, Cacn1, Cacnl1a3, Cchl1a3;
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] {ECO:0000312|EMBL:BAG54980.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Wistar {ECO:0000312|EMBL:BAG54980.1};
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:BAG54980.1};
RX PubMed=20101487; DOI=10.1007/s12576-010-0085-z;
RA Tanaka N., Ishii H., Yin C., Koyama M., Sakuma Y., Kato M.;
RT "Voltage-gated Ca2+ channel mRNAs and T-type Ca2+ currents in rat
RT gonadotropin-releasing hormone neurons.";
RL J. Physiol. Sci. 60:195-204(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 714-1850 (ISOFORM 1).
RX PubMed=1335956; DOI=10.1016/s0888-7543(05)80134-x;
RA Chin H., Krall M., Kim H.-L., Kozak C.A., Mock B.A.;
RT "The gene for the alpha-1 subunit of the skeletal muscle dihydropyridine-
RT sensitive calcium channel (Cchl1a3) maps to mouse chromosome 1.";
RL Genomics 14:1089-1091(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1310-1404.
RC TISSUE=Kidney;
RX PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
RA Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
RT "Molecular characterization and nephron distribution of a family of
RT transcripts encoding the pore-forming subunit of Ca2+ channels in the
RT kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1072-1371 (ISOFORM ROB1).
RC TISSUE=Osteosarcoma;
RX PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
RA Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
RT "Multiple calcium channel transcripts in rat osteosarcoma cells: selective
RT activation of alpha 1D isoform by parathyroid hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
RN [5]
RP PHOSPHORYLATION BY PKA.
RX PubMed=2174428; DOI=10.1016/s0021-9258(17)45292-6;
RA Lai Y., Seagar M.J., Takahashi M., Catterall W.A.;
RT "Cyclic AMP-dependent phosphorylation of two size forms of alpha 1 subunits
RT of L-type calcium channels in rat skeletal muscle cells.";
RL J. Biol. Chem. 265:20839-20848(1990).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-397; SER-1575;
RP THR-1579 AND SER-1617, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium
CC channel that gives rise to L-type calcium currents in skeletal muscle.
CC Calcium channels containing the alpha-1S subunit play an important role
CC in excitation-contraction coupling in skeletal muscle via their
CC interaction with RYR1, which triggers Ca(2+) release from the
CC sarcplasmic reticulum and ultimately results in muscle contraction.
CC Long-lasting (L-type) calcium channels belong to the 'high-voltage
CC activated' (HVA) group. {ECO:0000250|UniProtKB:P07293}.
CC -!- ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines
CC (DHP), phenylalkylamines, and by benzothiazepines.
CC {ECO:0000250|UniProtKB:P07293, ECO:0000305}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC CACNB1 or CACNB2 (By similarity). CACNA1S channel activity is modulated
CC by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1).
CC Interacts with DYSF and JSRP1 (By similarity). Interacts with RYR1.
CC Interacts with STAC, STAC2 and STAC3 (via their SH3 domains) (By
CC similarity). Interacts with CALM (By similarity).
CC {ECO:0000250|UniProtKB:P07293, ECO:0000250|UniProtKB:Q02789,
CC ECO:0000250|UniProtKB:Q13698}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:P07293}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02485-1; Sequence=Displayed;
CC Name=ROB1;
CC IsoId=Q02485-2; Sequence=VSP_000939;
CC -!- TISSUE SPECIFICITY: Skeletal muscle specific.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position. {ECO:0000250|UniProtKB:P07293}.
CC -!- DOMAIN: The loop between repeats II and III interacts with the
CC ryanodine receptor, and is therefore important for calcium release from
CC the endoplasmic reticulum necessary for muscle contraction.
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- PTM: The alpha-1S subunit is found in two isoforms in the skeletal
CC muscle: a minor form of 212 kDa containing the complete amino acid
CC sequence, and a major form of 190 kDa derived from the full-length form
CC by post-translational proteolysis close to Phe-1690.
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- PTM: Phosphorylated. Phosphorylation by PKA activates the calcium
CC channel. Both the minor and major forms are phosphorylated in vitro by
CC PKA. Phosphorylation at Ser-1575 is involved in beta-adrenergic-
CC mediated regulation of the channel. {ECO:0000250|UniProtKB:P07293}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1S subfamily. {ECO:0000305}.
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DR EMBL; AB374360; BAG54980.1; -; mRNA.
DR EMBL; L04684; AAA40844.1; -; mRNA.
DR EMBL; M99220; AAA40894.1; -; mRNA.
DR EMBL; U31816; AAA89158.1; -; mRNA.
DR PIR; A46422; A46422.
DR RefSeq; NP_446325.1; NM_053873.1. [Q02485-1]
DR AlphaFoldDB; Q02485; -.
DR SMR; Q02485; -.
DR CORUM; Q02485; -.
DR STRING; 10116.ENSRNOP00000067264; -.
DR BindingDB; Q02485; -.
DR ChEMBL; CHEMBL4108; -.
DR DrugCentral; Q02485; -.
DR GuidetoPHARMACOLOGY; 528; -.
DR GlyGen; Q02485; 1 site.
DR iPTMnet; Q02485; -.
DR PhosphoSitePlus; Q02485; -.
DR PaxDb; Q02485; -.
DR GeneID; 682930; -.
DR KEGG; rno:682930; -.
DR CTD; 779; -.
DR RGD; 70983; Cacna1s.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q02485; -.
DR OrthoDB; 172471at2759; -.
DR PRO; PR:Q02485; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; B3XZL8; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0031674; C:I band; ISO:RGD.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0002074; P:extraocular skeletal muscle development; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0001503; P:ossification; NAS:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0043501; P:skeletal muscle adaptation; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005450; VDCC_L_a1ssu.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01634; LVDCCALPHA1S.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1850
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1S"
FT /id="PRO_0000053946"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..70
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 71..85
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 107..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..179
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 180..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..218
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 219..279
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 280..301
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 302..309
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 310..330
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 331..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..451
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 452..462
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 463..483
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 484..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..514
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 515..523
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..542
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 543..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..581
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 582..601
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 602..623
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 624..633
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 634..653
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 654..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 800..818
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 819..830
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 831..850
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 851..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 867..885
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 886..892
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 893..911
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 912..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 931..950
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 951..1000
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1001..1021
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1022..1038
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1039..1060
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1061..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1119..1140
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1141..1148
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1149..1170
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1171..1180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1181..1200
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1201..1231
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1232..1250
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1251..1268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1269..1289
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1290..1311
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1312..1330
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1331..1356
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1357..1381
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1382..1850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 38..337
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 418..664
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 786..1068
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1105..1384
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..374
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250|UniProtKB:Q02789"
FT REGION 673..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1077
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1337..1403
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1349..1391
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1522..1542
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:Q13698"
FT REGION 1697..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..293
FT /note="Selectivity filter of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 612..615
FT /note="Selectivity filter of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 1012..1015
FT /note="Selectivity filter of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 1321..1324
FT /note="Selectivity filter of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1014
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOD_RES 1575
FT /note="Phosphoserine; by PKA and CAMK2"
FT /evidence="ECO:0000250|UniProtKB:P07293,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 1579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1617
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P07293,
FT ECO:0007744|PubMed:22673903"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..254
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT DISULFID 245..261
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT DISULFID 957..968
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT DISULFID 1338..1352
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT VAR_SEQ 1204..1222
FT /note="Missing (in isoform ROB1)"
FT /evidence="ECO:0000303|PubMed:7479909"
FT /id="VSP_000939"
FT CONFLICT 714
FT /note="I -> V (in Ref. 2; AAA40844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="I -> T (in Ref. 4; AAA89158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1323
FT /note="E -> A (in Ref. 4; AAA89158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1845..1850
FT /note="AMPREP -> PCPGSLEPKVLPWAA (in Ref. 2; AAA40844)"
SQ SEQUENCE 1850 AA; 210396 MW; 309E38319F53FF23 CRC64;
MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLQNPL RKACISVVEW KPFETIILLT
IFANCVALAV YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
GWNVLDFIIV FLGVFTAILE QVNIIQTNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE
KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIS MEGWTDVLYW
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
EDLRGYMSWI TQGEVMDVDD LREGKLSLDE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV
FRWKCHDLVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDVANRV LLALFTIEML
MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRLFKITK
YWTSLSNLVA SLLNSIRSIA SLLLLLFLFM IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
PQALISVFQV LTGEDWNSVM YNGIMAYGGP SYPGVLVCIY FIILFVCGNY ILLNVFLAIA
VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PDKSEEERST MTKKLEQKPK GEGIPTTAKL
KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPASPRPRP LAELQLKEKA VPIPEASSFF
IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILEYFDYVFT
AVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSAI SVVKILRVLR
VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFYSCNDL
SKMTEEECRG YYYIYKDGDP TQIELRPRQW IHNDFHFDNV LSAMMSLFTV STFEGWPQLL
YKAIDSNEED TGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
NQSEQMNHIS DILNVAFTII FTLEMILKLI AFKPRGYFGD PWNVFDFLIV IGSIIDVILS
EIDTLLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIAMVDGTQI NRNNNFQTFP QAVLLLFRCA
TGEAWQEILL ACSYGKRCDP ESDYAPGEEY ACGTNFAYYY FISFYMLCAF LIINLFVAVI
MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTVQIQAGLR
TIEEEAAPEI HRAISGDLTA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP
VMANQRPLQF AEMEMEELES PVFLEDFPQN PGTHPLARAN TNNANANVAY GNSSHRNSPV
FSSIRYEREL LEEAGRPVTR EGPFSQPCSV SGVNSRSHVD KLERQMSQRR MPKGQVPPSP
CQLSQEKHPV HEEGKGPRSW STETSDSESF EERVPRNSAH KCTAPATTML IQEALVRGGL
DSLAADANFV MATGQALADA CQMEPEEVEV AATELLKRES PKGGAMPREP
