ID A0A3Q3WTC7_MOLML Unreviewed; 1683 AA.
AC A0A3Q3WTC7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000012474.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000012474.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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 Ensembl; ENSMMOT00000012679.1; ENSMMOP00000012474.1; ENSMMOG00000009542.1.
DR Proteomes; UP000261620; 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 Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
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 PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF9; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1S; 1.
DR Pfam; PF08763; Ca_chan_IQ; 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602077-
KW 3}; Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1040..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1112..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1153..1171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1268..1291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1359..1383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1399..1434
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 731..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1015
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1683 AA; 192013 MW; 25C572529C2B87D6 CRC64;
MADSNSPPLS SYIMDEETLK RKQKEKLKKL MATGGNPRPA RSLLFLTLMN PFRKACISIV
EWKPFEIIIL LAIFANCVAL AVYLPMPEED SNNTNSNLEN LEYIFLIIFS IECFLKIVAY
GFLFHADAYL RNCWNILDFV CVSVGLFTVA VDAINHISGV EAPVGEKGGG FDMKALRAFR
VLRPLRLVSG VPSLQVVMNS ILKSMLPLFH ITLLVLFMVT IYSIMGLELF KCKMHKTCYY
TGTNIIATLE NEKPAPCAQA GNGRRCTING TECRASWPGP NHGITHFDNL GFSMLTVYQC
ITTQGWTDVL YWVNDAIGME WPWIYFTTLI LVGSFFVLNL VLGVLSGEFT KEREKAKSRG
EFQKLRETQQ LDEDLKGYME WITQAEAIDN EQEGHGLSSN LLIFLLFNSK LARKWNRWLR
CKCRVFVKSR LFYWWVIMLV FFNTLAIATE HHKQTERLTN WQDNANKLLL SMFALEMLMK
MYALSFPSYF MSLFNRFDCF VVSTGIMELI LVHMAVMSVM GISVLRCIRL LRLLKITRYW
TSLSNLVASL LNSVRSIACL LLLLFLFIVI FSLLGMQVFG GKFNFPDQTK PRSTFDSFPQ
ALITVFQILT GEDWNAVMYD GIMAHGGPSM PGILVSFYFI ILFVCGNFIL LNVFLAIAVD
NLAEAESLTL AQKEKAEEKK RKKAVRANMP EKISEEKANL AKKLAEQRAK GVEGIPTTAK
LKIDEFESNV NEIKDPFPPA DFPGDDEEEE PEIPESPRPR PMADLQLKEE AVPMPEASSF
FIFGPQNKFR KLCHRIINAT TFTNIILLFI LLSSISLAAE DPIDPMSFRN RVLAYADIVF
TSVFTAEIVL KMTTYGAILH KGSFCRNSFN ILDLLVVSVS LLSMGMESSA ISVVKILRVL
RVLRPLRAIN RAKGLKHVVQ CVFVAVKTIG NIVLVTMLLD FMFACIGVQL FKGKFYCCTD
PDKMSEETCK GWYTKYREGA LHEMEVHERK WTNSELNFDN ILNGMLALFT ISTFEGWPKI
LYKAIDSNVE DKGPVYNNRV AISIFFIIYL ILIAFFMMNI FVGFVIVTFQ EQGEQEYKNC
ELDKNQRQCV QYALKARPLR CYIPKNPYQY QVWYIVTSCY FEYLMFLLIM LNTMCLGIQH
CNQSDHITHL SDMLNVIFTV LFTVEMILKL MAFKAKGYFG DPWNVFDFII VVGSVVDVML
SEIDAALASS GGLYCLQGCN VTILLSTENM SVSVTFFRLF RVMRLVKLLN RSEGIRNLLW
TFIKSLQALP YVALLILMVF FIYAVVGMQI FGKIALVDGT YINRNNNFQT FPQAVLLLFR
CATGEAWHEV MLACMYGKKC DAKSDYLPGE EDTCGSNFAI IYFMSFYMLC AFLIINLFVA
VIMDNFDYLT RDWSILGPQH LDEFKKIWAE YDPEATGRIK HLDVVTLLRR IPPPLGFGKF
CPHRIACKRL VSMNMPLNSD GTVTFNATLF ALVRTALKIK TEGNFEQANE ELRGIIKKIW
KRTSMKLLDQ VIPPIGDDEV TVGKFYATFL IQDYFRKLKK RQEEYYGYRP TRKNATHEIQ
AGLRNIEEEA APELHRTISG DLMTEEEMER ATDEAAEEGI FKRQGSLFVN HMDPFSVEIE
AVIISQATNQ LPLQEAEGAD KNNKNITRES THRYVFCLVL VSFSCQVLMY IASLFITHVV
QVH
//
