ID A0A1S3LXF7_SALSA Unreviewed; 2421 AA.
AC A0A1S3LXF7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E-like isoform X3 {ECO:0000313|RefSeq:XP_013995617.1};
GN Name=LOC106569134 {ECO:0000313|RefSeq:XP_013995617.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013995617.1};
RN [1] {ECO:0000313|RefSeq:XP_013995617.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013995617.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {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}.
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DR RefSeq; XP_013995617.1; XM_014140142.1.
DR GeneID; 106569134; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
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; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
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:SF5; VOLTAGE-DEPENDENT R-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1E; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
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 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 747..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1328..1346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1366..1386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1395..1413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1459..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1571..1596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1683..1705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1711..1729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1773..1791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1870..1893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2034..2068
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2365..2394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2160..2177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2186..2214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2365..2387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2421 AA; 273526 MW; 1BE1C49C9A6A2519 CRC64;
MLTSSDKSLS LMPDHCAPVG MASVPKGSTS SRGMHGTRSS LSLPEPEPWR RTPSPGTTRQ
GGLVQESRSC SLQVPHSGLE TLDLPPRAAS FDVAYRVEEA GSDTGSGSVS PCSMQRRRGG
IVDQRDVIRA HESHKMQSTP QARRKDWEMA RFGDEVQMTM DSRDSGDPER GEDGGDTASG
TGSGTLKQTK AARARTMALY NPIPHRQNCL TVNRSLFIFA EDNLIRKTAK RIIEWPPFEW
VILATITANC IVLALEQHLP GEDKTPMAKR LECTEPYFIG IFCFEFGIKL VALGFVFHKG
SYLRNGWNIM DFIVVVSGIL ATAGAHMNIP VDLRTLRAVR VLRPLKLVSG IPSLQIVLKS
IMKAMVPLLQ IGLLLFFAIL MFAIIGLEFY SGKLHHTCLP TADILENETM DTTEVEFACG
VRKCPEKYDC VGSWIGPNDG ITQFDNILFA VLTVFQCITM EGWTAVLYNT NDALGFMWNW
MYFIPLIIIG SFFVLNLVLG VLSGEFAKER ERVENRRAFM KLRRQQQVER ELNGYRAWID
RAEEVMLAEE NKKSGRSALD VLKRATSKNA KRRGGPGDAE ISTVGAPRMR IRTVRRGPVA
YMRRKERMLR ISLRRMVKTD TFYWTVLSLV FLNTICVAIV HHNQPDWLST FLYYAEFVFL
GLFLAEMFLK MYGLGFRLYF HSSFNCFDCG VIVGSIFEVV WGFFRPGMSF GISVLRALRL
LRIFKITKYW ASLRNLVVSL MSSMKSIISL LFLLFLFIVV FALLGMQLFG GRFIFEDYTP
TNFDTFPAAI MTVFQILTGE DWNEVMYNGI RSQGGVQYGM WSSIYFIVLT LFGNYTLLNV
FLAIAVDNLA NAQELTKDEE EEEEFFNARY ARGTDGPMSE YRRRRRPYLR RKKAIHRGRM
AVPEEEEEST AGGGADQPPN GTNAFSNRRD RRRRGGGGGR GGRSVWEQRA NQLRKRRQME
SQEVLFGGSP TEDTTDTPTT AYRAPTLSPD ASPGHLPESP MSGIMPMPEP PMSIAIPLPE
PPDSEPVPLF TLAEERAVNH RLTGGERRHR VARKSRPGPG GAEEGGAARH RRHRHREARA
EAKSRESPHE EVSESGSRER KILEEREEKE EKEEKEDKGE FAEVEGGVSG KDEGGALIIN
LESEEEHLRV CIADIPEPPL CDDFPEYLAT PLLEPPPQME EGEVGETGQC EPLSQDPPVE
PAPEQFADPS ELQAAAGVSD SENNQASLIL EEGKESEQGP DSQTSVIIEM SGAQPLLEVT
PMTALHSSKE VEVYHHERKE KKEEESQMEK EEEEEASPPK PVPPGSMFLF KASNPIRRIC
HYVVTMRYFE MTILLVIVAS SIALAAEDPV CTNSDRNRVL RYFDYVFTGV FTFEMIIKMT
DLGLLLHDGS YFRDLWNILD FIVVVGALIA FALTNNKGRD IKTIKSLRVL RVLRPLKTIK
RLPKLKAVFD CVVTSLKNVF NILIVYQLFM FIFAVIAVQL FKGKFFYCTD SSMDTEKECQ
GYYIDYARDK KEVKKREWKR HEFHYDNVCW ALLTLFTVST GEGWPQVLQH SVDVTEEDMG
PSRGNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE KNERACIDFT
ISAKPLTRYM PQNRQTFQYR LWHFVASPSF EYTVMVMIAL NTVVLMMKYY SAPAAYDTVL
KHLNTAFTVL FSLECILKIM AFGFVNYFRD TWNIFDFITV LGSITEIIVD LQSINTFNMS
FLKLFRAARL IKLLRQGYTI RILLWTFVQS FKALPYVCLL IAMLFFIYAI IGMQVFGNIK
LNDENHINQH NNFKTFSGAL MLLFRSATGE SWQEIMLSCL GGQECEPDSS MAPMTMSPDH
EGGCGTDFAY CYFVSFIFFS SFLMLNLFVA VIMDNFEYLT RDSSILGPHH LDEFVRVWGE
YDRAACGRIH YTAMYEMLTH MSPPLGLGKK CPRGMAYKRL VLMNMPVDED MSVHFTSTLM
SLIRTALEIK IARGQGMSGE DRVALDTELQ KEISVIWPYL PQKTLDVLVP INKDSDMTVG
KIYASMMIMD YFKQNKAKKL RAQLEAQKAS LMPFQRLDAS TLSEDILSNA QPLPCMSHSA
GSALTRGGLV ALSPLSPQDL LNMQPMTSDT DTRSQHSRTE MASGSMKRSS STVADQRVNG
LWQEEKKSPD RLYRPRHKSY KAAVSRSERK RHLDTEKERG RSKERRHLLS PDTSRCTSEE
RSLQPSRSPS RERTHPLDKQ GNSSDSPIPT SESSTPSRRP LSQTSTRSHP HISYSPLVCR
THPPSGDDDD DRGSPETQRR GEASREGAGG EGQSGARGRR QQQGSPLRRY PSEPYLALQE
DEHSLDPTGF METLTFEAAV ATSLGRANTV SSTSSSSFSS ARRGSRSGWQ VPNGHFRKRL
AQTVSVAGCE PLSDTEEDDR C
//
