ID A0A2K5EPA9_AOTNA Unreviewed; 2270 AA.
AC A0A2K5EPA9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1B {ECO:0000313|Ensembl:ENSANAP00000035035.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000035035.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000035035.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSANAT00000053102.1; ENSANAP00000035035.1; ENSANAG00000034894.1.
DR GeneTree; ENSGT00940000155275; -.
DR OMA; DPNKECA; -.
DR Proteomes; UP000233020; 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; 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.
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};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
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 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1109..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1240..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1352..1377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1433..1451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1463..1486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1498..1522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1543..1572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1641..1664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1680..1715
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2251..2270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..944
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..1995
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2270 AA; 254722 MW; C0768BD6533FEB5E CRC64;
MVSGGGERRP GRRGRRGGGP RPGGLQPGQR VLYKQSIAQR ARTMALYNPI PVKQNCFTVN
REDNVVRKYA KRITEWPYPY MILATIIANC IVLALEQHLP DGDKTPMSER LDDTEPYFIG
IFCFEAGIKI IALGFVFHKG SYLRNGWNVM DFVVVLTGIL ATAGTDFDLR TLRAVRVLRP
LKLVSGIPSL QVVLKSIMKA MVPLLQIGLL LFFAILMFAI IGLEFYMGKF HKACFPNSTD
AEPVGDFPCG KEAPARLCEG DTECREYWPG PNFGITNFDN ILFAILTVFQ CITMEGWTDI
LYNTNDAAGN TWNWLYFIPL IIIGSFFMLN LVLGVLSGEF AKERERVENR RAFLKLRRQQ
QIERELNGYL EWIFKAEEVM LAEEDRNAEE KSPLDVLKRA ATKKSRNDLI HAEEGEDRFA
DLCAVGSPFA RASLKSGKTE SSSYFRRKEK MFRFFIRRMV KAQSFYWVVL CVVALNTLCV
AMVHYNQPRR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR SYFRSSFNCF DFGVIVGSVF
EVVWAAIKPG SSFGISVLRA LRLLRIFKVT KYWSSLRNLV VSLLNSMKSI ISLLFLLFLF
IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI LTGEDWNAVM YHGIESQGGV
SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT KDEEEMEEAA NQKLALQKAK
EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN LRASCEALYS EMDPEERLRF
ATTRHLRPDM KTHLDRPLVV ELGRDGARGT VGGKARPEVG GRHHRHRDKD RAPAAGDQDR
AEAPKAESGE PGAREERPRP HRSHSKEAAG PRKRGARAPR AAGGTIGAAP RRRWPSGSPT
PPAHRHQDPG KEGAGAKGER RRASPRRPRT GPREPARRHR ARTRPPSAHE AAEKEAAEKE
AAEKEASWKA DKEKELRNHQ ASPHCDLETG GTVTVGPVHT LPSTCLQKVE EQPEDADNQR
NVTRMGGQPP DSSTVVHIPV MLTGPPGEAT VVPSGNVDPE SQAEGKKEVE ADDVMRSGPR
PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF EMVILVVIAL SSIALAAEDP VRTDSPRNNA
LKYLDYIFTG VFTFEMVIKM IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSGSKGK
DINTIKSLRV LRVLRPLKTI KRLPKLKAVF DCVVNSLKNV LNILIVYMLF MFIFAVIAVQ
LFKGKFFYCT DESKELERDC RGQYLDYEKE EVEAQPRQWK KYDFHYDNVL WALLTLFTVS
TGEGWPMVLK HSVDATYEEQ GPSPGYRMEL SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ
GDKVMSECSL EKNERACIDF AISAKPLTRY MPQNRQSFQY KTWTFVVSPP FEYFIMAMIA
LNTVVLMMKF YDAPYEYELM LKCLNIVFTS MFSMECVLKI IAFGVLNYFR DAWNVFDFVT
VLGSITDILV TEIANNFINL SFLRLFRAAR LIKLLRQGYT IRILLWTFVQ SFKALPYVCL
LIAMLFFIYA IIGMQVFGNI ALDDDTSINR HNNFRTFLQA LMLLFRSATG EAWHEIMLSC
LSSQACDEQA NATECGSDFA YFYFVSFIFL CSFLMLNLFV AVIMDNFEYL TRDSSILGPH
HLDEFIRVWA EYDPAACGRI SYNDMFEMLK HMSPPLGLGK KCPARVAYKR LVRMNMPISN
EDMTVHFTST LMALIRTALE IKLAPAGTKQ HQCDAELRKE ISIVWANLPQ KTLDLLVPPH
KPDEMTVGKV YAALMIFDFY KQNKSTRDQT QQAPGGLSQM GPVSLFHPLK ATLEQTQPAV
LRGARVFLRQ KSSASLSNGG AIQNQEGGIK ESVSWGTQRT QDAPLDARPP LERGTHRIQC
GAVRNPGEPA LRPCAHRVLC LQPVADASPM KRSISTLAQR PHGAHLCSTT PDRPPPSQAP
HHHHHRCHRR RDRKQRSLEK GPSLSAETDG APSSAAGPGL PLGEGPTGCR RERERRQERG
RSQERRQPSS SSSEKQRFYS CDRFGGREPP KPKPSLSSHP TSPTAGQEPG PHPQGSGSVN
GSPLLSTSGA STPGRGGRRQ LPQTPLTPRP SITYKTANSS PVHFAGAQTS LPAFSPGRLS
RGLSEHNALL QRDPLSQPLA PGSRIGSDPY LGQRLDGEAS VHALPEDTLT FEEAVATNSG
RSSRTSYVSS LTSQSHPLRR VPNGYHCTLG LSSGGRARHS YPHPDQDHWC
//
