CAC1B_DIPOM
ID CAC1B_DIPOM Reviewed; 2326 AA.
AC P56698;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable voltage-dependent N-type calcium channel subunit alpha-1B;
DE AltName: Full=DOE-4;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC TISSUE=Electric lobe;
RX PubMed=7683405; DOI=10.1073/pnas.90.9.3787;
RA Horne W.A., Ellinor P.T., Inman I., Zhou M., Tsien R.W., Schwarz T.L.;
RT "Molecular diversity of Ca2+ channel alpha 1 subunits from the marine ray
RT Discopyge ommata.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3787-3791(1993).
CC -!- FUNCTION: The isoform alpha-1B gives rise to N-type calcium currents.
CC N-type calcium channels belong to the 'high-voltage activated' (HVA)
CC group (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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P56698-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56698-2; Sequence=VSP_000884;
CC -!- TISSUE SPECIFICITY: Expression is higher in the electric lobe than in
CC the forebrain.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000305}.
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DR EMBL; L12532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B47447; B47447.
DR AlphaFoldDB; P56698; -.
DR SMR; P56698; -.
DR PRIDE; P56698; -.
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; IPR002048; EF_hand_dom.
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:SF6; PTHR45628:SF6; 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 PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Repeat; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..2326
FT /note="Probable voltage-dependent N-type calcium channel
FT subunit alpha-1B"
FT /id="PRO_0000053926"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 84..107
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 108..124
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 125..145
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 157..175
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 176..180
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 181..204
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 205..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 215..237
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 238..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 324..348
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 349..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 473..491
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 492..501
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 502..524
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 525..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 535..556
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 557..563
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 564..576
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 577..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 595..620
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 621..672
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 673..699
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 700..1148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1149..1167
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1168..1175
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1176..1200
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1201..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1215..1235
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1236..1241
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1242..1262
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1263..1280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1281..1300
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1301..1387
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1388..1413
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1414..1468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1469..1487
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1488..1495
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1496..1520
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1521..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1531..1552
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1553..1558
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1559..1577
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1578..1596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1597..1616
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1617..1680
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1681..1704
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1705..2326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT REPEAT 75..351
FT /note="I"
FT REPEAT 458..702
FT /note="II"
FT REPEAT 1134..1416
FT /note="III"
FT REPEAT 1453..1708
FT /note="IV"
FT DOMAIN 1721..1756
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 17..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..388
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 793..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1897..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2271..2326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2056
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2203..2242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 574
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 577
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 1734
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1745
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 306
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 653
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1362
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1650
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 406
FT /note="D -> DDGLGIIYEPEQKPEDIQSVY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000884"
SQ SEQUENCE 2326 AA; 264517 MW; D58DEAA09E819B6B CRC64;
MARLGNDVPA CYGGSPAGGG RGANRHAGPQ AGQRGMYGSK SLAQRARTMA LYNPIPVRQN
CLTVNRSLFI FSEDNIIRKY AKRITEWPPF EYMILATIIA NCIVLALEQH LPDGDKTPMS
ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG ILTTIGTDFD
LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMVPLLQIG LLLFFAILMF AIIGLEFYMG
KFHKTCFSEE TNEPVEEFPC GTKYPSRLCP NGTVCKGYWN GPNFGITNFD NILFAVLTVF
QCITMEGWTD MLYTANDALG NTWNWLYFIP LIVIGSFFML NLVLGVLSGE FAKERERVEN
RRAFLKLRRQ QQVEQEFNRY LRWIHIAEEV MLAEEDKNAE DKCALDVLKR ATTKKSKNDL
INAEEGEDHF TDISSVGFNR PSLKSVKNER SSYFRRKEKR FRFFIRRMVK SQSFYWIVLC
LVGLNTLCVA IVHYDQPPLL TDALYFAEFV FLGLFLTEMS LKMYGLGPRN YFHSSFNCFD
FGVIVGSIFE VVWTAVKPDT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV SLLNSMKSII
SLLFLLFLFI VVFALLGMQL FGGQFNFEDG TPPTNFDTFP AAILTVFQIL TGEDWNEVMY
YGIEAHGGVK KGMFSSVYFI ILTLFGNYTL LNVFLAIAVD NLANAQELTK DEEEMEEANI
QKNTIQKAME VADVSPISAT NLSIAAKDQQ KSFKSMSIWE QRTSQLRRQH ILTSQEALFN
ELDDEQRRMY VSSHQIRPDM KTHLDRPLVV EPRNSTRKSA DKVCPSDCQE GEQERLVQPE
SCEAPRRSHR HRDKLGEQDK GDGALDTGEP RANSKDDKRC SHRSHSKETE KERDEKGRKG
ERSRSHEGGR RHHHAQSSLD DAPEREHRRH RSHRHGTEQQ HREANGTKGE RHSRAKDGSR
SGGREGEAVS RSHHAEGAER RRKHRQKVAS TNESEEKREI GEKERETVLR ERRVHRVKET
QPSQDSGTQG NVSLPPIGLQ HLPQQPEDAD NQKNIKLVTL PTGDAQNPAT VNIPVTVTTP
AAEMTLLPIN NVAVDLENVM KPEEKKAENG DDLNEDGPRQ IPPFNSMFLF STTNPVRRAC
HYIVNLRYFE MCILLVITMS SIALAAEDPV QGDAPRNNVL KYLDYVFTGV FTFEMVIKMI
NLGLILHPGS YFRDLWNILD FIVVSGALVA FAFTGSRGKD LNTIKSLRVL RVLRPLKTIK
RLPKLKAVFD CVVNSLKNVL NILIVYMLFM FIFAVIAVQL FKGKFFYCTD ESKDLEKDCR
GQYLVYDNDE IEAEPREWKK CDFHYDNVLW ALLTLFTVST GEGWPTVLKN SIDATEEDQG
PSPSYRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKVMSDCSLE KNERACIDFA
ISAKPLTRYM PQNKQTFQYK MWKFVVSPPF EYLIMALIAL NTIVLMMKFY NAPDPYDRML
QYLNILFTFL FSMECVLKLI GFGVLNYFRD AWNVFDFVTV LGSITDILVT ELADSFINLS
FLRLFRAARL IKLLRQGYTI RILLWTFVQS FKALPYVCLL IAMLFFIYAI IGMQVFGNIE
LDDDGAINRH NNFRTFLQAV MLLLRSATGE GWQEIMLACL NQSPCDARSG IDGDECGSNF
AYFYFVSFIF FSSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEFIRVW AEYDPGARGR
ITYNDMYEML RHMCPPLGLG KKCPARVAYK RLVRMNMPIA EDGSVHFTST LMALIRTALD
VKISPGGAYQ QQCDAELRKE ITAVWPNLSQ KFLDILVPPQ RASELTVGKV YAALMIYDYY
KQNKSKKVQQ QQQLSGLSQT RKSFFQRVVG VLAATQEEPS SYSTSHKNSV NPLYQGGRQK
EPFSWLRSRD TCAEGKKEVP ESHPEEAGVT KSSSQAVEMR EMGSDLNHAD QSSLENYGRA
ASMPRLTAET QKISRPSGRV RAPIADTSPM KRSVSTLTPQ RSHVMPDYSL ERVIPVQMPH
HHHHHHRCHH RREKKQRSLE RATNRHADEE AGQLDAQLRD QSSKERERGR SQERRPPSSA
EKQRYYSCDR YGSREPPQPR STDHSRSASP STGTEQGFHR QGSGSVNDSP LQSASGSSTP
SRGRRQLPRT PLTPRPSVTY KTANSSPAHF GNLHDALPPS SPGRLSRGQS EHNHLLSGES
QNRPYAGGDS RQPMGTRISS DPYLGFRSSC GSEDLELLEE TLTFEVAVAA TTATGRSPRT
SSFTTQPPQS RRVPNGYHCN LGRSTGPSTA ASKRKYYRET DEDDWC
