ID A0A1S3NL94_SALSA Unreviewed; 2420 AA.
AC A0A1S3NL94;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=LOC106579993 {ECO:0000313|RefSeq:XP_014015976.1};
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_014015976.1};
RN [1] {ECO:0000313|RefSeq:XP_014015976.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014015976.1};
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. This alpha-1B subunit gives rise to N-type
CC calcium currents. N-type calcium channels belong to the 'high-voltage
CC activated' (HVA) group. They are involved in pain signaling. Calcium
CC channels containing alpha-1B subunit may play a role in directed
CC migration of immature neurons. {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. CACNA1B subfamily. {ECO:0000256|ARBA:ARBA00005685}.
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DR RefSeq; XP_014015976.1; XM_014160501.1.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
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; 6.10.250.2500; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR005447; VDCC_N_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:SF6; VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 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; PR01631; NVDCCALPHA1.
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 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 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 89..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1182..1200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1252..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1313..1335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1425..1450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1506..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1537..1559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1878..1912
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1941..2190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2210..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2142
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2167..2190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2210..2257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2420 AA; 272684 MW; E9802849E17CCABA CRC64;
MARFEEELSN RRGGVCQAGP PRGAGRPAGP PSGPRVYKQS MAQRARTMAI YNPIPVKQSC
LTVNRSVFIF SEDCIIRKYA KKITEWPPFE YLILATIIAN CIVLALEQHL PAGDKTPMSE
RLDDTEPYFI GIFCFEAGIK IIALGFAFHK GSYLRNGWNV MDFVVVLTGM LATVGADFDL
RTLRAVRVLR PLKLVSGIPS LQVVLKSIMK AMVPLLQIGM LLFFAILMFA IIGLDFYMGK
FHRTCFRTDT GEQAAEFPCG MEAPARTCEN GTVCQEYWIG PNYGITNFDN ILFAILTVFQ
CITMEGWVDI LYNANDASGN TWNWLYFIPL IIIGSFFMLN LVLGVLSGEF AKERERVEKR
QEFLKLRRQQ QIERELTGYL EWICKAEEVM LAEEDKHAEE KSPLDGVWYK RKHNNPVLKR
AKKSKNDLIN AEEGEDHFTD ISSVVPPGSP FARASLKSSK NGSASYFRRK EKRLRFTIRH
LVKAQSFYWT VLCLVGLNTL CVAIVHYDQP EWLTYALYLA EFVFLGLFLT EMSMKMYGLG
PMSYFHSSFN CFDFGVIIGS IFEVIWAVVK PGASFGISVL RALRLLRIFK VTKYWNSLRN
LVVSLLNSMK SIISLLFLLF LFIVVFALLG MQLFGGLFNF DEETPTTNFD TFPAAILTVF
QILTGEDWNA VMYHGIESQG GVRRGMFSSI YFIVLTLFGN YTLLNVFLAI AVDNLANAQE
LTKDEEEQEV AITKKMALQK AKEVKEVSPM SAANISITAL HSILYTGQHG AERAMPASFV
KQSQGALSSS SSVCSVNSLS YVCSPVHHYL SKEQQKSLKM MSVWEQRTTQ LRRHNLRASS
EALYSELDPE ERLRMSSALH IRPDMKTHLD RPLVVESHDG PGPMGQHKPR TPEETDTPED
PAGPQPRRHH RHRDRERPID EANENGDPGK EGRHHVHHSR SKDPDGTRGK EGKSERSRSR
EGGRRHHHQT LVDEGGGGGT GEREHRHHHS HRQAREGNGT VNSGGKGERR SRHKDGRSGE
RCSRGENGAN GERRRHKTHG SRGQSTLEGE DHSEREKGRG HRDRYVESEG DSLAISPQQD
PGDQRWGTEG PEDSDNQRNV RRTGQTAVNI PPVTITPPPG ETTLIPMNSI DCETMPMNEE
KKTLEERTQS GPRPILPYSS MFVFGQANVV RRLCHYIVSL RYFEMCILVV ISMSSIALAA
EDPVQANAPR NNVLKYLDYV FTGVFTFEMV IKMVDLGLLL HPGSYFRDLW NILDFIVVSG
ALVAFAFSGS KGKDISTIKS LRVLRVLRPL KTIKRLPKLK AVFDCVVNSL KNVFNILIVY
MLFMFIFAVI AVQLFKGKFF YCTDESKGLE KDCRGNFLDY DKDEVAAQPR VWKKYEFHYD
NVLWAFLTLF TVSTGEGWPD VLKHSVDATF EDQGPSPGYR IEISIFYVVY FVVFPFFFVN
IFVALIIITF QEQGDKAMSE CSLEKNERAC IDFAINAKPL TRYMPENVQS FQYRMWKFVV
SPPFEYSIMI MIALNTVVLM MKFHGAPDFY EAMLKHFNIV FTALFSLECI LKIIAFGPLN
YLKDAWNVFD FVTVLGSITD IVVTEINTTD RLLNLSFLRL FRAARLIKLL RQGYTIRILL
WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIELNED TAITHHNNFR TFLQALMLLF
RSATGEAWHE IMLSCLSHRA CDERSGNLGK ECGSDFAYFY FVSFIFLCSF LMLNLFVAVI
MDNFEYLTRD SSILGPHHLD EFIRVWAEYD PAACGRIRYN DMYNLLRIIS PPLGLGKNCP
NRVAYKRLVK MNMPIADDNT VHFTSTLMAL IRTALEIKLS SGMVAQRLSD AELKKELSTV
WPSLSQKTMD LLVTPHKPNE LTVGKVYAAL MIFDYYKQNR AKRLKEQQQQ QQQQNAAGSQ
GKVGALFKPI LPLTYNMEPP CELLPQPQPQ ALPRPSPTLL NNMEPPCELL PQPQPQALPR
PSPTLLNNGG TLPGHDGIMK GSSTWVSEKS REVHRPRNNR PVQRGQSEDV PDTTLPQESV
EMRKMDTSDS TVPGPGSGLE SQGRAVSMPR LNAELQRSQS RHSPGTLLAP VPDCSPMKRS
ASTHAPQRPQ EVNLRDYTLE TPSIQERPHH HHHHRCHHRR ERDKKQRSLD RTPSTAGTPG
DPAAEPSSRD RVQDRGRSHE RKHHSTAGEK QRYYSCDRYG SREHCHTTKS ATASCATSPS
EVQDPSINKQ GSGSVKCSPV MMTSGASTPS RGRRQLPQTP LTPRPGVAYK TANSSPVHFV
SAQCGSGLPT LSPGRLSRGL SEHNALLHSG SSHIPSPVTR ISSEPFLGYS HREAQGQGSL
YCSLRDELLS PYAARARSPR TALPQMGPGP LHLPPAPQQS RAVPNGYHFT FGGIGNASPG
SGSGARAPRY YHEADEDEWC
//
