ID A0A2K5ZXA0_MANLE Unreviewed; 1975 AA.
AC A0A2K5ZXA0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1B {ECO:0000313|Ensembl:ENSMLEP00000032412.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000032412.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000032412.1}
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; ENSMLET00000055989.1; ENSMLEP00000032412.1; ENSMLEG00000040234.1.
DR GeneTree; ENSGT00940000155275; -.
DR OMA; EGGRKHH; -.
DR Proteomes; UP000233140; Unplaced.
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; 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 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:UP000233140};
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 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 885..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1016..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1274..1298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1319..1348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1417..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1578..1612
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 670..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1795
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1099
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1975 AA; 222106 MW; E849FB39BC7AF748 CRC64;
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 EWIFKAGEGP
WEPLRPEEKD PVLKRAATKK SRNDLIHAEE GEDRFADLCA VGSPFARASL KSGKTESSSY
FRRKEKMFRF FIRRMVKAQS FYWVVLCVVA LNTLCVAMVH YNQPRRLTTA LYFAEFVFLG
LFLTEMSLKM YGLGPRSYFR SSFNCFDFGV IVGSVFEVVW AAIKPGSSFG ISVLRALRLL
RIFKVTKYWS SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFQDETPT
TNFDTFPAAI LTVFQILTGE DWNAVMYHGI ESQGGVSKGM FSSFYFIVLT LFGNYTLLNV
FLAIAVDNLA NAQELTKDEE EMEEAANQKL ALQKAKEVAE VSPMSAANIS IAGSRHLVAH
AVRTEPRPLA IPGAGGLRGP CSGSAPSGGR GSPSSRERRA LVATGGGISS LRPDFWHKAQ
PAHEAVEKEA TEKEATEKEA EIVEADKEKE LRNHQPREPH CDLETSGTVT VGPMHTLPST
CLQKVEEQPE DADNQRNVTR MGSQPPDPST VVHIPVMLTG PPGEATVVPS GNVDLESQAE
GKKEVEADDV MRSGPRPIVP YSSMFCLSPT NLLRRFCHYI VTMRYFEMVI LVVIALSSIA
LAAEDPVHTD SPRNNALKYL DYIFTGVFTF EMVIKMIDLG LLLHPGAYFR DLWNILDFIV
VSGALVAFAF SGSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVLNIL
IVYMLFMFIF AVIAVQLFKG KFFYCTDESK ELERDCRGQY LDYEKEEVEA QPRQWKKYDF
HYDNVLWALL TLFTVSTGEG WPMVLKHSVD ATYEEQGPSP GYRMELSIFY VVYFVVFPFF
FVNIFVALII ITFQEQGDKV MSECSLEKNE RACIDFAISA KPLTRYMPQN RQSFQYKTWT
FVVSPPFEYF IMAMIALNTV VLMMKFYDAP YEYELMLKCL NIVFTSMFSM ECVLKIIAFG
VLNYFRDAWN VFDFVTVLGS ITDILVTEIA NNFINLSFLR LFRAARLIKL LRQGYTIRIL
LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIALDD DTSINRHNNF RTFLQALMLL
FRSATGEAWH EIMLSCLSNQ ACDEQANATE CGSDFAYFYF VSFIFLCSFL MLNLFVAVIM
DNFEYLTRDS SILGPHHLDE FIRVWAEYDP AACCRIHYKD MYSLLRCIAP PVGLGKNCPR
RLAYKRLVRM NMPISSEDMT VHFTSTLMAL IRTALEIKLA PAGTKQHQCD AELRKEISVV
WANLPQKTLD LLVPPHKPDE MTVGKVYAAL MIFDFYKQNK TTRDQMHQAP GGLSQMGPVS
LFHPLKATLE QTQPAVLRGA RVFLRQKSST SLSNGGAIQN QESGIKESVS WGTQRTQDGP
HEARPPLERG HSTEIPVGQS GALAVDVQMQ SMTRRGPDGE PQPGLESQGR AASMPRLAAE
TQPVTDASPM KRSISTLAQR PRGTHLCSTT PDRPPPSQAP HHHHHRCHRR RDRKQRSLEK
GPSLSADTDG APSSAAGPGL PPGEGPTGCR RERERRQERG RSQERRQPSS SSSEKQRFYS
CDRFGGREPP KPKPSLSSHP TSPTAGQEPG PHPQVRAQLP LPWPTVGFLN TTPCCRKTPS
ASPWPLVLES ALTLTWGSVW TARPLSTPCL RTRSLSRRLW PPTQAAPPGL PTCPP
//
