CAC1S_CYPCA
ID CAC1S_CYPCA Reviewed; 1852 AA.
AC P22316;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dihydropyridine-sensitive L-type skeletal muscle calcium channel subunit alpha-1;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=1846962; DOI=10.1073/pnas.88.3.727;
RA Grabner M., Friedrich K., Knaus H.-G., Striessnig J., Scheffauer F.,
RA Staudinger R., Koch W.J., Schwartz A., Glossmann H.;
RT "Calcium channels from Cyprinus carpio skeletal muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:727-731(1991).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, gene
CC expression, cell motility, cell division and cell death. The isoform
CC alpha-1S gives rise to L-type calcium currents. Long-lasting (L-type)
CC calcium channels belong to the 'high-voltage activated' (HVA) group.
CC They are blocked by dihydropyridines (DHP), phenylalkylamines, and by
CC benzothiazepines. Calcium channels containing the alpha-1S subunit play
CC an important role in excitation-contraction coupling in skeletal muscle
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and
CC delta subunits in a 1:1:1:1 ratio. The channel activity is directed by
CC the pore-forming and voltage-sensitive alpha-1 subunit. In many cases,
CC this subunit is sufficient to generate voltage-sensitive calcium
CC channel activity. The auxiliary subunits beta and alpha-2/delta linked
CC by a disulfide bridge regulate the channel activity. An additional
CC gamma subunit is present only in skeletal muscle L-type channel (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Skeletal muscle.
CC -!- PTM: May be non-phosphorylated.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M62554; AAA49205.1; -; mRNA.
DR PIR; A37860; A37860.
DR AlphaFoldDB; P22316; -.
DR SMR; P22316; -.
DR PRIDE; P22316; -.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR002048; EF_hand_dom.
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.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; 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..1852
FT /note="Dihydropyridine-sensitive L-type skeletal muscle
FT calcium channel subunit alpha-1"
FT /id="PRO_0000053948"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..86
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 87..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..127
FT /note="Helical; Name=S2 of repeat I"
FT TOPO_DOM 128..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..155
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 156..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..195
FT /note="Helical; Name=S4 of repeat I"
FT TOPO_DOM 196..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..234
FT /note="Helical; Name=S5 of repeat I"
FT TOPO_DOM 235..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..351
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 352..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..466
FT /note="Helical; Name=S1 of repeat II"
FT TOPO_DOM 467..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..501
FT /note="Helical; Name=S2 of repeat II"
FT TOPO_DOM 502..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..528
FT /note="Helical; Name=S3 of repeat II"
FT TOPO_DOM 529..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..557
FT /note="Helical; Name=S4 of repeat II"
FT TOPO_DOM 558..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..596
FT /note="Helical; Name=S5 of repeat II"
FT TOPO_DOM 597..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..675
FT /note="Helical; Name=S6 of repeat II"
FT TOPO_DOM 676..815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..834
FT /note="Helical; Name=S1 of repeat III"
FT TOPO_DOM 835..850
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 851..870
FT /note="Helical; Name=S2 of repeat III"
FT TOPO_DOM 871..882
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..901
FT /note="Helical; Name=S3 of repeat III"
FT TOPO_DOM 902..908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..927
FT /note="Helical; Name=S4 of repeat III"
FT TOPO_DOM 928..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..966
FT /note="Helical; Name=S5 of repeat III"
FT TOPO_DOM 967..1056
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1057..1081
FT /note="Helical; Name=S6 of repeat III"
FT TOPO_DOM 1082..1134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1153
FT /note="Helical; Name=S1 of repeat IV"
FT TOPO_DOM 1154..1168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1169..1188
FT /note="Helical; Name=S2 of repeat IV"
FT TOPO_DOM 1189..1196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1197..1215
FT /note="Helical; Name=S3 of repeat IV"
FT TOPO_DOM 1216..1252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1253..1271
FT /note="Helical; Name=S4 of repeat IV"
FT TOPO_DOM 1272..1290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1291..1310
FT /note="Helical; Name=S5 of repeat IV"
FT TOPO_DOM 1311..1377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1378..1402
FT /note="Helical; Name=S6 of repeat IV"
FT TOPO_DOM 1403..1852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 57..354
FT /note="I"
FT REPEAT 433..679
FT /note="II"
FT REPEAT 802..1084
FT /note="III"
FT REPEAT 1121..1405
FT /note="IV"
FT DOMAIN 1418..1453
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 374..391
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 1004..1093
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1358..1424
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1370..1413
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1820..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 309
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 628
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1030
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1344
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1852 AA; 210098 MW; 7D5FAE83501D6CDB CRC64;
MESGSGGGGG GGVAALASFI MNEEELKRKQ REKLKKLQAT GGNPRPPRSL FFFTLKNPFR
KTCINIVEWK PFEIIILLTI FANCVALAVF LPMPEEDTNN TNLTLESLEY IFLVIFTLEC
FLKIVAYGLL FHEGAYLRNC WNILDFVIVF MGLFTLVVDT INTIAGVPTE KGGGFDMKAL
RAFRVLRPLR LVSGVPSLQV VMSSILKSML PLFHIALLVF FMVHIYAIMG LELFKCKMHK
TCYYQGTNII AVREGNEKPS PCAQAGHGRR CTINGTECRA GWPGPNFGIT HFDNSCFAML
TVFQCITTES WTDVLYWIND AMGNDWPWIY FLTLILVGSF FILNLVLGAL SGEFTKEREE
SRSRGEYQKL RERQQMDEDL EGYMEWITHA EVMDGDSEAL LLLRKDTDSE SDSLYQMLDQ
QVIYFYRLAR RWNVVLRRKC HVWVKSKFFN WWVLLVVLLN TLVIAMEHHN QTEGLTSFQD
TANVILLACF TIEMVMKMYA FGPRAYFMSI FNRFDCFVVT IGILEIILVV SNIMTPLGIS
VMRCIRLLRL FKLTRYWTSL NNLVASLLNS VKSIASLLLL LFLFIVIFAL LGMQVFGGKF
NFPDRVIQRS NFDNFPQALI SVFQVLTGEE WDSIMYNGIM AHGGPQSPGI LVSIYFIILY
VCGNFVLLNV FLAIAVDNLA EAESLTAAQK EKAEEKARRK LMRTLPEKSE EEKALMAKRL
MESRSKAEGM PTTAKLKIDE FESNVNEVKD PFPPADFPGD HEEVEPEIPI SPRPRPMADL
QLKETVVPIA EASSFFIFGP QHKFRKLCHR IVNHTTFTNI ILLFILLSSI SLAAEDPIDP
RSFRNKVLAY ADIVFTTVFT IEIVLKMTVY GAFLHTGSFC RNSFNILDLI VVGVSLLSMG
MESSTISVVK ILRVLRVLRP LRAINRAKGL KHVVQCMFVA IKTIGNIVLV TMLLDFMFAC
IGVQLFKGKL YYCTDPLQKT AEECQGTFLK HVPNSLHDIE VHQRMWVNSD FNFDNVLNGM
LALFTISTFE GWPEILYKAI DSNAVDTGPL YNNRVGISIF FIIYIIIIAF FMMNIFVGFV
IVTFQKQGEQ EYKDCELDKN QRQCVQYALK ARPLKCYIPK NPHQYRVWYF VTSCYFEYLM
FFLIMLNTLC LGIQHCNQSD HITKLSDTLN LIFTVLFTGE MIVKLIAFKA KGYFGDPWNV
FDFIIVVGSI VDVVLSEVDA ALEARGGLWC LHGCAEVNPM QAIAEAENVR VSITFFRLFR
VLRLIKLLNR SEGIRNLLWT FIKSFQALPH VGLLIVMLFF IYAVIGMQMF GKVALVDGTE
INRNNNFQTF PQAVLLLFRV ATGEQWPKVI LASMYGKLCD AKSDYGPGEE YTCGSSIAVF
YFLSFYILCA FLIINLFVAI IMDNVDYLTR DWSILGPHHL DEFKKIWAEY DPEATGRIKH
LDVVTLLRRI QPPLGFGKFC PHRSACKRLI SMNMPLNSDG TVTFNATLFA LVRTALKIKT
EGNFEQANEE LRAIIKSIWK RTSMKLLDQV IPPIGEDEVT VGKFYATFLI QEHFRKFMQR
QEEYYGYRPT KKNADEIKAG LRSIEEEAAP ELHRAISGDL IAEDDMERAL EAGEEGIYRR
TGGLFGLHTD PFSSEPSSPL STQMTSQRPL QFVETRLEDI ESPPDSVFLP NTEFFPDNMP
TTTNTNNNAN FVEDMSSRFT FENESLSAAA TRNYSYEDIR GSSSYVGGAS SVDDRRLSDF
TVRTNITQFP YNPSYGPSKN QTATEASPAT DKLIQQALRD GGLDSLAEDP KFVSVTRKEL
AEAINIGMED MEGMAQGIVN RQSGKVTKRK RRPIPVPPGT KSTKPKENTS AV
