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Database: UniProt
Entry: CAC1A_APIME
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ID   CAC1A_APIME             Reviewed;        1904 AA.
AC   C9D7C2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   27-SEP-2017, entry version 40.
DE   RecName: Full=Voltage-dependent calcium channel type A subunit alpha-1;
DE   AltName: Full=Cacophony protein;
GN   Name=CAC;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; Apidae; Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yang Z., Qiao M., Jin Y.;
RT   "Coding region for CAC.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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, neurotransmitter release, gene expression, cell
CC       motility, cell division and cell death. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CATSPER1 and CATSPER2, leading to suppress
CC       T-type calcium channel activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1I subfamily. {ECO:0000305}.
DR   EMBL; GQ202019; ACV86997.1; -; mRNA.
DR   RefSeq; NP_001159376.1; NM_001165904.1.
DR   UniGene; Ame.1428; -.
DR   ProteinModelPortal; C9D7C2; -.
DR   STRING; 7460.GB18730-PA; -.
DR   PaxDb; C9D7C2; -.
DR   PRIDE; C9D7C2; -.
DR   GeneID; 408764; -.
DR   KEGG; ame:408764; -.
DR   CTD; 12285; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   InParanoid; C9D7C2; -.
DR   PhylomeDB; C9D7C2; -.
DR   Proteomes; UP000005203; 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   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Complete proteome;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1904       Voltage-dependent calcium channel type A
FT                                subunit alpha-1. {ECO:0000250}.
FT                                /FTId=PRO_0000404525.
FT   TOPO_DOM     30    168       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    169    187       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    188    205       Extracellular. {ECO:0000255}.
FT   TRANSMEM    206    225       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    226    237       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    238    259       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    260    264       Extracellular. {ECO:0000255}.
FT   TRANSMEM    265    283       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    284    302       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    303    322       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    323    419       Extracellular. {ECO:0000255}.
FT   TRANSMEM    420    444       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    445    568       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    569    587       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    588    602       Extracellular. {ECO:0000255}.
FT   TRANSMEM    603    622       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    623    630       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    631    649       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    650    658       Extracellular. {ECO:0000255}.
FT   TRANSMEM    659    677       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    678    696       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    697    716       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    717    769       Extracellular. {ECO:0000255}.
FT   TRANSMEM    770    794       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    795    895       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    896    914       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    915    930       Extracellular. {ECO:0000255}.
FT   TRANSMEM    931    950       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    951    962       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    963    981       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    982    994       Extracellular. {ECO:0000255}.
FT   TRANSMEM    995   1013       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1014   1032       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1033   1052       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1053   1141       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1142   1166       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1167   1221       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1222   1250       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1251   1255       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1256   1275       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1276   1283       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1284   1302       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1303   1309       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1310   1328       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1329   1347       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1348   1367       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1368   1431       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1432   1456       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1457   1904       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      155    447       I.
FT   REPEAT      554    797       II.
FT   REPEAT      890   1177       III.
FT   REPEAT     1214   1470       IV.
FT   DOMAIN     1476   1511       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND    1489   1500       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   REGION     1430   1471       Phenylalkylamine binding. {ECO:0000250}.
FT   COMPBIAS    132    144       Poly-Gly.
FT   COMPBIAS    807    813       Poly-Glu.
FT   SITE        402    402       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        748    748       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1117   1117       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1405   1405       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES    1471   1471       Phosphoserine; by PKA. {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    367    367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    782    782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    993    993       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   1904 AA;  215891 MW;  CBE8C7AE704FF84B CRC64;
     MLGGVGGRHM STRRRGSSPL VRGGAGLTGY AGPGASGNSN DVAAIPPDMQ RYAGRRRRAV
     TTSDHKSCAL VQTRIKLGDI MLAAQEAAQR DPGYASQYRR RPRLAGLSFG DWTSFGGEVP
     GLVDMAPGRD QGGGAGGGGG GGKGTTSLFI LSEDNCIRKH TRFIIEWPPF EYAVLLTIIA
     NCVVLALEEH LPKQDKTILA QKLEATEIYF LGIFCVEASL KILALGFVLH RGSYLRNIWN
     IMDFFVVVTG FITAFSQGIE LDMDLRTLRA IRVLRPLKLV SGIPSLQVVL KSIIKAMAPL
     LQIGLLVLFA IVIFAIIGLE FYSGTLHKTC YSIRDINVIV KEGEQASPCN TDNKSEAPFG
     AHVCDANIST CMDHWEGPNF GITSFDNIGF AMLTVFQCIT MEGWTAILYW TNDALGSTYN
     WIYFIPLIVL GSFFMLNLVL GVLSGEFAKE REKVENRQSF LKLRRQQQLE HELYCYLNWI
     CKAEEVILAE ERTTEEEKKH ILEGRKRAEA KKKKLGKSKS TDTEEEEGDD DQDDGELSSS
     TKEKGPCKQF WLAEKRFRYW IRKSVKSQKF YWFVIVLVFF NTVCVAVEHY GQPQWLTDFL
     YFAEFVFLAL FMLEMFIKVY ALGPRTYFDS SFNRFDCVVI SGSIFEVIWS EVKSGSFGLS
     VLRALRLLRI FKVTKYWKSL RNLVISLLSS MRSIISLLFL LFLFILIFAL LGMQLFGGQF
     NFDSGTPPTN FNTFPIALLT VFQILTGEDW NEVMYQGIES QGGHKKGMIY SLYFIVLVLF
     GNYTLLNVFL AIAVDNLANA QELSAAENEE EEEDKQKQAQ EIEKEIQSLQ NPKDGGAPKV
     EICPPNGKGG KQSSEEEKKQ DEDDDTGPKP MLPYSSMFIL SPTNPVRRAA HWVVNLRYFD
     FFIMVVISLS SIALAAEDPV WEDSPRNEVL NYFDYAFTGV FTVEMILKII DLGIILHPGS
     YLREFWNIMD AVVVICAAVS FAFDMTGSSA GQNLSTIKSL RVLRVLRPLK TIKRVPKLKA
     VFDCVVNSLK NVINILIVYI LFQFIFAVIA VQLFNGKFFY CSDESKYTQQ DCQGQYFVFE
     DGALLPEPKK REWQSQFFHY DNVMAAMLTL FAVQTGEGWP QILQNSMAAT YEDKGPIQNF
     RIEMSIFYIV YFIVFPFFFV NIFVALIIIT FQEQGEAELQ DGEIDKNQKS CIDFTIQARP
     LERYMPKERN SVKYKIWRIV VSTPFEYFIM GLIVLNTVLL MMKFHRQSDA YKNTLKYMNM
     CFTGMFTVEC ILKIAAFGVR NFFKDAWNTF DFITVIGSIV DALVIEFGEN FINVGFLRLF
     RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIALDADT
     SITKHNNFQS FIQGLMLLFR CATGEAWPNI MLSCVKGRPC DAKAGKQEGG CGSNIAYAYF
     VSFIFFCSFL MLNLFVAVIM DNFDYLTRDS SILGAHHLDE FVRIWAEYDP NATGKIHYTE
     MYDMLKNMDP PLGFGNKCPN RLAYKKLIRM NMPVDVDLKV NFTTTLFALI RENLNIKVRR
     ASERNQANEE LRDTIRSIWP LQAKKMLDLL IPRNEEIGRG KMTVGKIYVC LLILESWRTT
     RFGQIESAGQ PIMELQDVVV SDSRAGSLES LTHTGKRLHP PVQPVRHPSR SPSLRHSPGR
     PGYDHHGHYY HEGPGFSDTV SNVVEIQRHT HHPHPSQYNH RHRMRGPWSA STSPARTPSP
     IHHIDRGRHY GTTSLEQRSR SPSPIGGRQP PHTHQHYHRH HPHQHSYPVL VTRRGRGRRL
     PPTPNKPSTL QLKPANINFP KLNASPTHGS HIHVPIPAGM QHPPPGQHLP PMQPSHCPLS
     FEQAVAMGRG GRLLPSPVPN GYKPQPQAKQ RTPRHSDSDE DDWC
//
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