ID H2QY88_PANTR Unreviewed; 2312 AA.
AC H2QY88;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 28-MAR-2018, entry version 43.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1B {ECO:0000313|Ensembl:ENSPTRP00000037005};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000037005, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000037005, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the
RT human genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136134; DOI=10.1038/nature04101;
RA Hughes J.F., Skaletsky H., Pyntikova T., Minx P.J., Graves T.,
RA Rozen S., Wilson R.K., Page D.C.;
RT "Conservation of Y-linked genes during human evolution revealed by
RT comparative sequencing in chimpanzee.";
RL Nature 437:100-103(2005).
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000037005}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC entry of calcium ions into excitable cells and are also involved
CC in a variety of calcium-dependent processes, including muscle
CC contraction, hormone or neurotransmitter release, gene expression,
CC cell motility, cell division and cell death. The isoform alpha-1B
CC gives rise to N-type calcium currents. N-type calcium channels
CC belong to the 'high-voltage activated' (HVA) group and are blocked
CC by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
CC IIIA (omega-Aga-IIIA). They are however insensitive to
CC dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
CC Calcium channels containing alpha-1B subunit may play a role in
CC directed migration of immature neurons.
CC {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR EMBL; AACZ04062170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04062179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9598.ENSPTRP00000037005; -.
DR PaxDb; H2QY88; -.
DR Ensembl; ENSPTRT00000040047; ENSPTRP00000037005; ENSPTRG00000021608.
DR eggNOG; KOG2301; Eukaryota.
DR eggNOG; ENOG410XNP6; LUCA.
DR GeneTree; ENSGT00830000128247; -.
DR InParanoid; H2QY88; -.
DR OMA; THAWASI; -.
DR OrthoDB; EOG091G0TKO; -.
DR TreeFam; TF312805; -.
DR Proteomes; UP000002277; Chromosome 9.
DR Bgee; ENSPTRG00000021608; -.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 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; PTHR10037:SF161; PTHR10037:SF161; 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU003808};
KW Calcium channel {ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|RuleBase:RU003808};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000002277};
KW Ion channel {ECO:0000256|RuleBase:RU003808};
KW Ion transport {ECO:0000256|RuleBase:RU003808};
KW Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 96 113 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 134 155 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167 187 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 222 244 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299 320 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332 354 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 484 504 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 510 527 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 609 631 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 687 709 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1146 1164 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1184 1204 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1216 1234 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1277 1299 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1389 1414 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1470 1488 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1500 1523 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1535 1559 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1580 1609 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1675 1694 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 1813 1847 Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT COILED 362 382 {ECO:0000256|SAM:Coils}.
FT COILED 712 738 {ECO:0000256|SAM:Coils}.
FT COILED 989 1014 {ECO:0000256|SAM:Coils}.
SQ SEQUENCE 2312 AA; 259505 MW; 626DD14154B6A9C8 CRC64;
MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPYPYMI LATIIANCIV LALEQHLPDG
DKTPMSERLD DTEPYFIGIF CFEAGIKIIA LGFVFHKGSY LRNGWNVMDF VVVLTGILAT
AGTDFDLRTL RAVRVLRPLK LVSGIPSLQV VLKSIMKAMV PLLQIGLLLF FAILMFAIIG
LEFYMGKFHK ACFPNSTDAE PVGDFPCGKE APARLCEGDT ECREYWPGPN FGITNFDNIL
FAILTVFQCI TMEGWTDILY NTNDAAGNTW NWLYFIPLII IGSFFMLNLV LGVLSGEFAK
ERERVENRRA FLKLRRQQQI ERELNGYLEW IFKAEEVMLA EEDRNAEEKS PLDAVLKRAA
TKKSRNDLIH AEEGEDRFAD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
AQSFYWVVLC VVALNTLCVA MVHYNQPRRL TTTLYFAEFV FLGLFLTEMS LKMYGLGPRS
YFRSSFNCFD FGVIVGSVFE VVWAAIKPGS SFGISVLRAL RLLRIFKVTK YWSSLRNLVV
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
RASCEALYSE MDPEERLRFA TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE
APEGVDPPRR HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPHR SHSKEAAGPP
EARSERGRGP GPEGGRRHHR RGSPEEAAER EPRRHRAHRH QDPSKECAGA KGERRARHRG
GPRAGPREAE SGEEPARRHR ARHKAQPAHE AVEKEATEKE AEIVEADKEK ELRNHQPREP
HCDLETSGTV TVGPMHTLPS TCLQKVEEQP EDADNQRNVT RMGSQPPDPN TIVHIPVMLT
GPPGEATVVP SGNVDLESQA EGKKEVEADD VMRSGPRPIV PYSSMFCLSP TNLLRRFCHY
IVTMRYFEMV ILVVIALSSI ALAAEDPVRT DSPRNNALKY LDYIFTGVFT FEMVIKMIDL
GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIN TIKSLRVLRV LRPLKTIKRL
PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI FAVIAVQLFK GKFFYCTDES KELERDCRGQ
YLDYEKEEVE AQPRQWKKYD FHYDNVLWAL LTLFTVSTGE GWPMVLKHSV DATYEEQGPS
PGYRMELSIF YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN ERACIDFAIS
AKPLTRYMPQ NRQSFQYKTW TFVVSPPFEY FIMAMIALNT VVLMMKFYDA PYEYELMLKC
LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG SITDILVTEI ANNFINLSFL
RLFRAARLIK LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIALD
DDTSINRHNN FRTFLQALML LFRCVVRSAQ ANLSCLSNQA CDEQAHATEC GSDFAYFYFV
SFIFLCSFLV LTHLDEFIRV WAEYDPAACC RIHYKDMYSL LRCIAPPVGL GKNCPRRLAY
KRLVRMNMPI SNEDMTVHFT STLMALIRTA LEIKLAPAAT SKHQCDEISF VGPIMPQIVN
FCWTWLGYHP NKPDEMTVGK VYAALMIFDF YKQNKTTRDQ MQQAPGGLSQ MGPVSLFHPL
KATVEQTQPA VLRGARVFLR QKSSTSLSNG GESVCLLCHR QNQESGIKES VSWGTQRTQD
APHEARPPLE RGHSTEIPVG RSGALAVDVQ MQSITRRGPD GEPQPGLESQ GRAASMPRLA
AETQPVTDAS PMKRSISTLA QRPRGTHLCS TTPDRPPPSQ ASHHHHHRCH RRRDRKQRSL
EKGPSLSADM DGAPSSAAGP GLPPGEGPTG CRRERERRQE RGRSQERRQP SSSSSEKQRF
YSCDRFGGRE PPKPKPSLSS HPTSPTAGQE PGPHPQGSGS VNGSPLLSTS GASTPGRGGR
RQLPQTPLTP RPSITYKTAN SSPIHFAGAQ TSLPAFSPGR LSRGLSEHNA LLQRDPLSQP
LAPGSRIGSD PYLGQRLDSE ASVHALPEDT LTFEEAVATN SGRSSRTSYV SSLTSQSHPL
RRVPNGYHCT LGLSSGGRAR HSYHHPDQDH WC
//
