CAC1C_CAVPO
ID CAC1C_CAVPO Reviewed; 2169 AA.
AC O35505; Q9Z305;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
GN Name=CACNA1C; Synonyms=CACH2, CACN2, CACNL1A1, CCHL1A1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1] {ECO:0000312|EMBL:BAA34185.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Heart {ECO:0000312|EMBL:BAA34185.2};
RX PubMed=10101289; DOI=10.1093/oxfordjournals.jbchem.a022346;
RA Ding S., Kuroki S., Kameyama A., Yoshimura A., Kameyama M.;
RT "Cloning and expression of the Ca2+ channel alpha1C and beta2a subunits
RT from guinea pig heart.";
RL J. Biochem. 125:750-759(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1198-1484 (ISOFORM 2), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Uterus;
RX PubMed=11058528; DOI=10.1095/biolreprod63.5.1262;
RA Collins P.L., Moore J.J., Lundgren D.W., Choobineh E., Chang S.M.,
RA Chang A.S.;
RT "Gestational changes in uterine L-type calcium channel function and
RT expression in guinea pig.";
RL Biol. Reprod. 63:1262-1270(2000).
CC -!- FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium
CC channel that gives rise to L-type calcium currents (PubMed:10101289).
CC Mediates influx of calcium ions into the cytoplasm, and thereby
CC triggers calcium release from the sarcoplasm (By similarity). Plays an
CC important role in excitation-contraction coupling in the heart (By
CC similarity). Required for normal heart development and normal
CC regulation of heart rhythm (By similarity). Required for normal
CC contraction of smooth muscle cells in blood vessels and in the
CC intestine (By similarity). Essential for normal blood pressure
CC regulation via its role in the contraction of arterial smooth muscle
CC cells (By similarity). Long-lasting (L-type) calcium channels belong to
CC the 'high-voltage activated' (HVA) group (By similarity).
CC {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815,
CC ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:10101289}.
CC -!- ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as
CC isradipine (By similarity). Inhibited by nifedipine (PubMed:10101289).
CC Channel activity is regulated by Ca(2+) and calmodulin (By similarity).
CC Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the
CC calmodulin binding site inhibits channel inactivation by Ca(2+) and
CC calmodulin (By similarity). Binding of calmodulin or CABP1 at the same
CC regulatory sites results in opposite effects on the channel function
CC (By similarity). Shear stress and pressure increases calcium channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P15381,
CC ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:10101289}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta
CC subunits. The channel complex contains alpha, beta, gamma and delta
CC subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of
CC subunit. CACNA1C channel activity is modulated by ancillary subunits,
CC such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity).
CC Interacts with CACNB1 (By similarity). Interacts with CACNB2.
CC Identified in a complex with CACNA2D4 and CACNB3. Interacts with
CC CACNB3. Interacts with CACNA2D1. Interacts with CACNA2D4 (By
CC similarity). Interacts with the gamma subunits CACNG4, CACNG6, CACNG7
CC and CACNG8 (By similarity). Interacts with CALM1. Interacts (via the N-
CC terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits
CC Ca(2+)-dependent channel inactivation. The binding via the C motif is
CC calcium independent whereas the binding via IQ requires the presence of
CC calcium and is mutually exclusive with calmodulin binding (By
CC similarity). The binding to the cytoplasmic N-terminal domain is
CC calcium independent but is essential for the channel modulation.
CC Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent
CC manner. Interacts with CIB1; the interaction increases upon
CC cardiomyocytes hypertrophy (By similarity). Interacts with STAC2 and
CC STAC3; this inhibits channel inactivation (By similarity).
CC {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815,
CC ECO:0000250|UniProtKB:Q13936}.
CC -!- INTERACTION:
CC O35505; P62158: CALM3; Xeno; NbExp=2; IntAct=EBI-9084208, EBI-397435;
CC O35505; P20810: CAST; Xeno; NbExp=2; IntAct=EBI-9084208, EBI-1268770;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15381};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell
CC membrane, sarcolemma {ECO:0000250|UniProtKB:P15381}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P15381}. Perikaryon
CC {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:Q01815}. Note=Colocalizes with ryanodine
CC receptors in distinct clusters at the junctional membrane, where the
CC sarcolemma and the sarcoplasmic reticulum are in close contact. The
CC interaction between RRAD and CACNB2 promotes the expression of CACNA1C
CC at the cell membrane. {ECO:0000250|UniProtKB:P15381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35505-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35505-2; Sequence=VSP_060907;
CC -!- TISSUE SPECIFICITY: Expressed in heart (PubMed:10101289). Expressed in
CC uterus (PubMed:11058528). {ECO:0000269|PubMed:10101289,
CC ECO:0000269|PubMed:11058528}.
CC -!- DEVELOPMENTAL STAGE: During gestation, expression in the uterus is
CC relatively constant between 34 and 47 days, increases by approximately
CC threefold relative to the expression level of 34 days by 54 days and
CC persists at the elevated levels through term.
CC {ECO:0000269|PubMed:11058528}.
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.
CC -!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
CC inhibits the opening of the channel. {ECO:0000250|UniProtKB:P15381}.
CC -!- PTM: Phosphorylation by PKA at Ser-1927 activates the channel. Elevated
CC levels of blood glucose lead to increased phosphorylation by PKA.
CC {ECO:0000250|UniProtKB:Q01815}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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DR EMBL; AB016287; BAA34185.2; -; mRNA.
DR EMBL; AF005938; AAB62890.1; -; mRNA.
DR RefSeq; NP_001166394.1; NM_001172923.1. [O35505-1]
DR AlphaFoldDB; O35505; -.
DR SMR; O35505; -.
DR IntAct; O35505; 2.
DR MINT; O35505; -.
DR BindingDB; O35505; -.
DR ChEMBL; CHEMBL2366456; -.
DR DrugCentral; O35505; -.
DR GeneID; 100135490; -.
DR KEGG; cpoc:100135490; -.
DR CTD; 775; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; O35505; -.
DR OrthoDB; 172471at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB.
DR GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:UniProtKB.
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; IPR005451; VDCC_L_a1csu.
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; 2.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01635; LVDCCALPHA1C.
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; Cell projection; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2169
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1C"
FT /id="PRO_0000053927"
FT TOPO_DOM 1..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..172
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 173..187
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 209..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 239..261
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..280
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 281..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..319
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 320..379
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 380..401
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 402..409
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 431..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 554..572
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 573..583
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 584..604
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 605..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 616..635
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 636..644
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 645..663
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 664..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 683..702
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 703..722
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 723..744
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 745..754
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 755..774
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 775..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 930..948
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 949..960
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 961..980
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 981..996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 997..1015
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1016..1022
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1023..1041
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1042..1060
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1061..1080
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1081..1130
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1131..1151
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1152..1168
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1169..1190
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1191..1248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1249..1270
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1271..1278
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1279..1300
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1301..1310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1311..1330
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1331..1353
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1354..1372
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1373..1390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1391..1411
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1412..1433
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1434..1452
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1453..1480
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1481..1505
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TOPO_DOM 1506..2169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 140..437
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 539..785
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 916..1198
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1235..1508
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 76..97
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT REGION 98..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..474
FT /note="AID/alpha-interaction domain; mediates interaction
FT with the beta subunit"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT REGION 478..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..905
FT /note="Interaction with STAC2"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT REGION 1118..1207
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1459..1527
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1473..1515
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REGION 1640..1667
FT /note="Important for interaction with STAC1, STAC2 and
FT STAC3"
FT /evidence="ECO:0000250|UniProtKB:P15381"
FT REGION 1646..1666
FT /note="Calmodulin-binding IQ region"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT REGION 1680..1699
FT /note="Important for localization in at the junctional
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P15381"
FT REGION 1761..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..393
FT /note="Selectivity filter of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 733..736
FT /note="Selectivity filter of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 1142..1145
FT /note="Selectivity filter of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT MOTIF 1443..1446
FT /note="Selectivity filter of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT COMPBIAS 793..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 735
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT BINDING 1144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 1699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 1720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01815"
FT MOD_RES 1927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13936"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 345..361
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT DISULFID 1087..1098
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT DISULFID 1460..1476
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT VAR_SEQ 1234..1352
FT /note="KNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNM
FT LFTGLFTVEMILKLIAFKPKHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSM
FT NAEENSRI -> I (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060907"
FT CONFLICT 1460
FT /note="C -> R (in Ref. 2; AAB62890)"
FT /evidence="ECO:0000305"
FT CONFLICT 1465
FT /note="D -> E (in Ref. 2; AAB62890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2169 AA; 242638 MW; 8B212C3D74ED2DC3 CRC64;
MVPLVQPTTP AYRPLPSHLS ADTEVRGRGT LVHEAQLNCF YISPGGSNYG SPRPAHANIN
ANAAAGLAPE HIPTPGAALS WQAAIDAGRQ AKLMGSAGNT TISTVSSTQR KRQQYGKPKK
QSGTTATRPP RALLCLTLKN PIRRACISIV EWKPFEIIIL LTIFANCVAL AIYIPFPEDD
SNATNSNLER VEYLFLIIFT VEAFLKVIAY GLLFHPNAYL RNGWNLLDFI IVVVGLFSAI
LEQATKADGA NALGGKGAGF DVKALRAFRV LRPLRLVSGV PSLQVVLNSI IKAMVPLLHT
ALLVLFVIII YAIIGLELFM GKMHKTCYNQ EGITDVPAEE DPSPCALESG HGRQCQNGTV
CKPGWDGPKH GITNFDNFAF AMLTVFQCIT MEGWTDVLYW MQDAMGYELP WVYFVSLVIF
GSFFVLNLVL GVLSGEFSKE REKAKARGDF QKLREKQQLE EDLKGYLDWI TQAEDIDPEN
EDEGVDEEKP RNMSMPTSET ESVNTENVAG GDIEGENCGA RLAHRISKSK FSRYWRRWNR
FCRRKCRAAV KSNVFYWLVI FLVFLNTLTI ASEHYNQPHW LTEVQDTANK ALLALFTAEM
LLKMYSLGLQ AYFVSLFNRL DCFIVCGGIL ETILVETKIM SPLGISVLRC VRLLRIFKIT
RYWNSLSNLV ASLLNSVRSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE MRTRRSTFDN
FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG PSFPGMLVCI YFIILFICGN YILLNVFLAI
AVDNLADAES LTSAQKEEEE EKERKKLART ASPEKKQEVV EKPAVEETKE EKIELKSITA
DGESPPTTKI NMDDLQPNEN EDKSPYPNPD AAGEEDEEEP EMPVGPRPRP LSELHLKEKA
VPMPEASAFF IFSPNNRFRL QCHRIVNDTI FTNLILFFIL LSSISLAAED PVQHTSFRNH
ILFYFDIVFT TIFTIEIALK MTAYGAFLHK GSFCRNYFNI LDLLVVSVSL ISFGIQSSAI
NVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF
KGKLYTCSDS SKQTEAECKG NYITYKDGEV DQPIIQPRSW ENSKFDFDNV LAAMMALFTV
STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL
NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV
VGSIVDIAIT EVNPAEHTQC SPSMNAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW
TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR
CATGEAWQDI MLACMPGKKC APESDPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
VAVVMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG
KLCPHRVACK RLVSMNMPLN SDGTAMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK
IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL
QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFGRAGG LFGNHVSYYQ
SDSRSTFPQT FTTQRPLHIN KAGNNQGDTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
NTALGRFPHP AGYPSTVSTV EGHRPPSSPA TWAQEATRKL GAMRCHSRES QIAVVCQEEP
SQDKTYDVEL NKDAEYCSEP SLLSTEMLSY KDDENRQLTP PEEDKGDTRP SPKKGFLRSA
SLGRRASFHL ECLKRQKNHG GDISQKTVLP LHLVHHQALA VAGLSPLLQR SHSPTAIPRP
CATPPATPGS RGWPPKPIPT LRLEGAESCE KLNSSFPSIH CSSWSEEPSP CGGGSSAARR
ARPVSLMVPS QAGAPGRQFH GSASSLAEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
IGEMENAADN ILSGGAPQSP NGTLLPFVNC RDPGQDRAGG DEDEGCACAL GRGWSEEELA
DSRVHVRSL
