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Database: UniProt
Entry: CAC1B_RABIT
LinkDB: CAC1B_RABIT
Original site: CAC1B_RABIT 
ID   CAC1B_RABIT             Reviewed;        2339 AA.
AC   Q05152;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-SEP-2017, entry version 120.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
DE   AltName: Full=Brain calcium channel III;
DE            Short=BIII;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
GN   Name=CACNA1B; Synonyms=CACH5, CACNL1A5;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8386525; DOI=10.1016/0896-6273(93)90162-K;
RA   Fujita Y., Mynlieff M., Dirksen R.T., Kim M.-S., Niidome T., Nakai J.,
RA   Friedrich T., Iwabe N., Miyata T., Furuichi T., Furutama D.,
RA   Mikoshiba K., Mori Y., Beam K.G.;
RT   "Primary structure and functional expression of the omega-conotoxin-
RT   sensitive N-type calcium channel from rabbit brain.";
RL   Neuron 10:585-598(1993).
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   -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta
CC       and delta subunits in a 1:1:1:1 ratio. The channel activity is
CC       directed by the pore-forming and voltage-sensitive alpha-1
CC       subunit. In many cases, this subunit is sufficient to generate
CC       voltage-sensitive calcium channel activity. The auxiliary subunits
CC       beta and alpha-2/delta linked by a disulfide bridge regulate the
CC       channel activity. Interacts with RIMS1. Interacts with FMR1 (via
CC       C-terminus); this interaction induces a deacrease in the number of
CC       presynaptic functional CACNA1B channels at the cell surface.
CC       {ECO:0000250|UniProtKB:O55017}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widespread expression throughout the brain.
CC       Highest levels in corpus striatum and midbrain.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino 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. CACNA1B subfamily. {ECO:0000305}.
DR   EMBL; D14157; BAA03202.1; -; mRNA.
DR   RefSeq; NP_001075660.1; NM_001082191.1.
DR   UniGene; Ocu.2138; -.
DR   PDB; 3DVE; X-ray; 2.35 A; B=1855-1875.
DR   PDB; 3DVJ; X-ray; 2.80 A; B=1853-1873.
DR   PDBsum; 3DVE; -.
DR   PDBsum; 3DVJ; -.
DR   ProteinModelPortal; Q05152; -.
DR   SMR; Q05152; -.
DR   DIP; DIP-29592N; -.
DR   STRING; 9986.ENSOCUP00000010930; -.
DR   iPTMnet; Q05152; -.
DR   GeneID; 100008979; -.
DR   KEGG; ocu:100008979; -.
DR   CTD; 774; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; Q05152; -.
DR   KO; K04849; -.
DR   EvolutionaryTrace; Q05152; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006816; P:calcium ion transport; IDA:UniProtKB.
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   PANTHER; PTHR10037:SF246; PTHR10037:SF246; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   2339       Voltage-dependent N-type calcium channel
FT                                subunit alpha-1B.
FT                                /FTId=PRO_0000053923.
FT   TOPO_DOM      1     95       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     96    114       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    115    132       Extracellular. {ECO:0000255}.
FT   TRANSMEM    133    152       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    153    163       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    164    183       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    184    187       Extracellular. {ECO:0000255}.
FT   TRANSMEM    188    206       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    207    225       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    226    245       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    246    331       Extracellular. {ECO:0000255}.
FT   TRANSMEM    332    356       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    357    483       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    484    502       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    503    517       Extracellular. {ECO:0000255}.
FT   TRANSMEM    518    537       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    538    545       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    546    563       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    564    574       Extracellular. {ECO:0000255}.
FT   TRANSMEM    575    593       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    594    612       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    613    632       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    633    685       Extracellular. {ECO:0000255}.
FT   TRANSMEM    686    710       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    711   1156       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1157   1174       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1175   1190       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1191   1210       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1211   1222       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1223   1241       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1242   1251       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1252   1270       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1271   1289       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1290   1309       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1310   1396       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1397   1421       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1422   1476       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1477   1495       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1496   1510       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1511   1530       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1531   1538       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1539   1557       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1558   1566       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1567   1585       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1586   1604       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1605   1624       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1625   1686       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1687   1711       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1712   2339       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       82    359       I.
FT   REPEAT      469    713       II.
FT   REPEAT     1142   1424       III.
FT   REPEAT     1461   1714       IV.
FT   DOMAIN     1727   1762       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND     452    459       ATP. {ECO:0000255}.
FT   CA_BIND    1740   1751       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   REGION      379    396       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   COMPBIAS   2051   2055       Poly-His.
FT   COMPBIAS   2119   2123       Poly-Ser.
FT   COMPBIAS   2319   2324       Poly-Gly.
FT   SITE        314    314       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        663    663       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1370   1370       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1658   1658       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES      22     22       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES     411    411       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES     746    746       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES     749    749       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES     784    784       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES    1074   1074       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES    1722   1722       Phosphoserine; by PKA. {ECO:0000255}.
FT   MOD_RES    2067   2067       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES    2224   2224       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES    2233   2233       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   MOD_RES    2256   2256       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O55017}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1566   1566       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1678   1678       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   HELIX      1855   1869       {ECO:0000244|PDB:3DVE}.
SQ   SEQUENCE   2339 AA;  261181 MW;  0413DA93794C8B34 CRC64;
     MVRFGDELGG RYGGAGGAER ARGGGAGGAG GPGPGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKIL ALGFVLHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDP DPVGDFPCGK EAPARLCEGD TECREYWAGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDRNAEEK SPLDAVLKRA
     AAKKSRSDLI QAEEGEGRLT GLCAPGSPFA RASLKSGKTE SSSYFRRKEK MFRFFIRRMV
     KAQSFYWTVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
     SYFRSSFNCF DFGVIVGSIF EVVWAAVKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
     VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFKD ETPTTNFDTF PAAILTVFQI
     LTGEDWNAVM YHGIESQGGV SRGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
     KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
     LRASCEALYS EMDPEERLRY ATARHLRPDV KTHLDRPLVV EPGRDAPRGP PGGKSRPDGS
     EAPEGADPPR RHHRHRDKDK APATVPSAGE QDRAEALRAE GGELGPREER GRPRRSRSKE
     APGAPEVRSD RGRGPCPEGG RRHHRRGSPE EAAEREPRRH RAHRHGPDPG KEGPASGTRG
     ERRARHRTGP RACPREAESS EEPARRHRAR HKAPPTQETA EKDKEAAEKG GEATEAEKDK
     EARNHQPKEL PCDLEAIGML GVGAVHTLPS TCLQKVEEQP EDADNQRNVT RMGSQPPDTS
     TTVHIPVTLT GPPGETTVVP SGNVDLESQA EGKKEVETSD VMRSGPRPIV PYSSMFCLSP
     TNLLRRCCHY IVTMRYFEMV ILVVIALSSI ALAAEDPVRT DSPRNNALKY MDYIFTGVFT
     FEMVIKMIDL GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIS TIKSLRVLRV
     LRPLKTIKRL PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI FAVIAVQLFK GKFFYCTDES
     KELERDCRGQ YLDYEKEEVE AQPRQWKKYD FHYDNVLWAL LTLFTVSTGE GWPMVLKHSV
     DATYEEQGPS PGYRMELSIF YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN
     ERACIDFAIS ARPLTRYMPQ NKQSFQYKTW TFVVSPPFEY FIMAMIALNT VVLMMKFYDA
     PYEYELMLKC LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG SITDILVTEI
     ANNFINLSFL RLFRAARLIK LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG
     MQVFGNIALD DDTSINRHNN FRTFLQALML LFRSATGEAW HEIMLSCLSS RACDEHSNAS
     ECGSDFAYFY FVSFIFLCSF LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EFIRVWAEYD
     PAACGRISYS DMFEMLKHMS PPLGLGKKCP ARVAYKRLVR MNMPISSEDM TVHFTSTLMA
     LIRTALDIKL APAGTKQHQC DAELRKEISC VWANLPQKTL DLLVPPHKPD EMTVGKVYAA
     LMIFDFYKQN KTSRDQTQQA PGGLSQLGPV SLFHPLKATL EQTQPALRGA RAFLRQKSSA
     SLSNGGAVQT QESGIKESVS WGTQRTQDVL CEARAPLERG HSAEIPVGQP GTLAVDVQMQ
     NMTLSGPDAE PQPGLESQGR AASMPRLAAE TQPAPDASPM KRSISTLAPR PHTARLGSTA
     LDRPAPSQAP HHHHHRCHRR RDRKQRSLEK GPSLSADTDG APDSTVGPGL PTGEGPPGCR
     RERERRQERG RSQERRQPSS SSSEKHRFYS CDRFGGREPP QPKPSLSSHP TSPTAGQEPG
     PHPQGSGSVH GSPLLSTSGA STPGRGRRQL PQTPLTPRPS VTYKTANSSP VHFAGAPSGL
     PAFSPGRLSR GLSEHNALLQ RDPLSRPLAP GSRIGSDPYL GQRLDSEAPA RALPEDAPAF
     EETAASNSGR SSRTSYVSSL TSQPPPLRRV PNGYHCTLGL GGGGRARRGC HHPDRDRRC
//
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