ID A0A2Y9KXX8_ENHLU Unreviewed; 2143 AA.
AC A0A2Y9KXX8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=LOC111159674 {ECO:0000313|RefSeq:XP_022377953.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022377953.1};
RN [1] {ECO:0000313|RefSeq:XP_022377953.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022377953.1};
RG RefSeq;
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: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000256|ARBA:ARBA00024012}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density membrane
CC {ECO:0000256|ARBA:ARBA00034112}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000256|ARBA:ARBA00024028}.
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DR RefSeq; XP_022377953.1; XM_022522245.1.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF10; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C; 1.
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; PR01635; LVDCCALPHA1C.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW 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 Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
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 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 899..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1145..1172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1223..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1252..1274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1286..1303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1362..1385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1455..1479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1613..1647
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1862..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1944..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1969
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2143 AA; 240517 MW; F2DF6693EDBD7F2D CRC64;
MVNENTRMYI PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGSTTATRP PRALLCLTLK NPIRRACISI
VEWKYPLPFE IIILLTIFAN CVALAIYIPF PEDDSNATNS NLERVEYLFL IIFTVEAFLK
VIAYGLLFHP NAYLRNGWNL LDFIIVVVGL FSAILEQATK ADGANALGGK GAGFDVKALR
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFMGKMHKT
CYNQEGIADV PAEDDPSPCA LETGHGRQCQ NGTVCKPGWD GPKHGITNFD NFAFAMLTVF
QCITMEGWTD VLYWVNDAVG RDWPWIYFVT LIIIGSFFVL NLVLGVLSGE FSKEREKAKA
RGDFQKLREK QQLEEDLKGY LDWITQAEDI DPENEDEGMD EEKPRNMSMP TSETESVNTE
NVAGGDIEGE NCGARLAHRI SKSKFSRYWR RWNRFCRRKC RAAVKSNVFY WLVIFLVFLN
TLTIASEHYN QPHWLTEVQD TANKALLALF TAEMLLKMYS LGLQAYFVSL FNRFDCFIVC
GGILETILVE TKIMSPLGIS VLRCVRLLRI FKITRYWNSL SNLVASLLNS VRSIASLLLL
LFLFIIIFSL LGMQLFGGKF NFDEMQTRRS TFDNFPQSLL TVFQILTGED WNSVMYDGIM
AYGGPSFPGM LVCIYFIILF ICGNYILLNV FLAIAVDNLA DAESLTSAQK EEEEEKERKK
LARTASPEKK QEVVEKPAVE ETKEEKIELK SITADGESPP TTKINMDDLQ PNENEDKSPY
PNPENTGEED EEEPEMPVGP RPRPLSELHL KEKAVPMPEA SAFFIFSPNN RFRLQCHRIV
NDTIFTNLIL FFILLSSISL AAEDPVQHTS FRNHILGNAD YVFTSIFTLE IILKMTAYGA
FLHKGSFCRN YFNILDLLVV SVSLISFGIQ SSAINVVKIL RVLRVLRPLR AINRAKGLKH
VVQCVFVAIR TIGNIVIVTT LLQFMFACIG VQLFKGKLYT CSDSSKQTEA ECKGNYITYK
DGEVDHPIIQ PRSWENSKFD FDNVLAAMMA LFTVSTFEGW PELLYRSIDS HTEDKGPIYN
YRVEISIFFI IYIIIIAFFM MNIFVGFVIV TFQEQGEQEY KNCELDKNQR QCVEYALKAR
PLRRYIPKNQ HQYKVWYVVN STYFEYLMFV LILLNTICLA MQHYGQSCLF KIAMNILNML
FTGLFTVEMI LKLIAFKPKG YFSDPWNVFD FLIVIGSIID VILSETNPAE HTQCSPFMNA
EENSRISITF FRLFRVMRLV KLLSRGEGIR TLLWTFIKSF QALPYVALLI VMLFFIYAVI
GMQVFGKIAL NDTTEINRNN NFQTFPQAVL LLFRCATGEA WQDIMLACMP GKKCAPESEP
SNSTEGETPC GSSFAVFYFI SFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF
KRIWAEYDPE AKGRIKHLDV VTLLRRIQPP LGFGKLCPHR VACKRLVSMN MPLNSDGTVM
FNATLFALVR TALRIKTEGN LEQANEELRA IIKKIWKRTS MKLLDQVVPP AGDDEVTVGK
FYATFLIQEY FRKFKKRKEQ GLVGKPSQRN ALSLQAGLRT LHDIGPEIRR AISGDLTAEE
ELDKAMKEAV SAASEDDIFR RAGGLFGNHV SYYQSDSRNA FPQTFTTQRP LHINKAANSQ
GDTESPSHEK LVDSTFTPSS YSSTGSNANI NNANNTALGR FPRPAGYPSA VSTVEGHGPP
LSPAVRVQEA AWKLSSKRCH SRESQIAMVC QEEVSQDETY EVKLSEDTEY CSEPSLISTE
LISYQDDENR QLTPPEEDRR DIRQSPKRGF LRSASLGRRA SFHLECLKRQ KNQGGDISQK
TVLPLHLVHH QALAVAGLSP LLQRSHSPST FPRPCATPPA TPGSQGWPPQ PIPTLRLEGA
ESSEKLNSSF PSIHCSSWSG EPAPCGGGSS ALRRARPVSL TVPSQAGARG RPFYGSASSL
VGAVLISEGL GQFAQDPKFI EVTTQELADA CDMTIEEMEN AADNILSGGT QQSPNGTLLP
FVNCRDPGQD RAGGQEGESC AGARACRKSE EERQDSRAHT GSL
//
