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Database: UniProt
Entry: G3S178_GORGO
LinkDB: G3S178_GORGO
Original site: G3S178_GORGO 
ID   G3S178_GORGO            Unreviewed;      1974 AA.
AC   G3S178;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   20-JUN-2018, entry version 47.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1F {ECO:0000313|Ensembl:ENSGGOP00000021823};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000021823, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000021823, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000021823}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) 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-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in
CC       opposite effects on the channel function.
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; CABD030124454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030124455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018874854.1; XM_019019309.1.
DR   STRING; 9593.ENSGGOP00000021823; -.
DR   Ensembl; ENSGGOT00000034163; ENSGGOP00000021823; ENSGGOG00000000907.
DR   GeneID; 101131714; -.
DR   KEGG; ggo:101131714; -.
DR   CTD; 778; -.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G3S178; -.
DR   KO; K04853; -.
DR   OMA; LNQTECR; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000001519; Chromosome X.
DR   Bgee; ENSGGOG00000000907; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF184; PTHR10037:SF184; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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:UP000001519};
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:UP000001519};
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    133    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    164    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    237    260       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    349    371       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    530    548       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    563    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    659    678       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    728    750       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    869    887       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    907    927       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    939    965       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    985   1014       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1110   1137       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1188   1209       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1221   1240       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1323   1341       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1414   1438       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1572   1606       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      798    822       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1974 AA;  220370 MW;  295657DE2C66378C CRC64;
     MSESEGGKDT TPEPSPANGA GPGPEWGLCP GPPAVEGESS GASGLGTPKR RNQHSKHKTV
     AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
     NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
     EQGPGRPGDA PHTGGKPGGF DVKALRAFRV LRPLRLVSGV PSLHIVLNSI MKALVPLLHI
     ALLVLFVIII YAIIGLELFL GRMHKTCYFL GSDMEAEEDP SPCASSGSGR ACTLNQTECR
     GRWPGPNGGI TNFDNFFFAM LTVFQCITME GWTDVLYWMQ DAMGYELPWV YFVSLVIFGS
     FFVLNLVLGV LSGEFSKERE KAKARGDFQK QREKQQMEED LRGYLDWITQ AEELDMEDPS
     ADGNLGSMAE EGRAGHRPQL AELTNRRRGR LRWFSHSTRS THSTSSHASL PASDTGSMTE
     TQGDEDEEEG ALASCTRCLN KIMKTRVCRR LRRANRVLRA RCRRAVKSNA CYWAVLLLVF
     LNTLTIASEH HGQPVWLTQI QEYANKVLLC LFTVEMLLKL YGLGPSAYVS SFFNRFDCFV
     VCGGILETTL VEVGAMQPLG ISVLRCVRLL RIFKVTRHWA SLSNLVASLL NSMKSIASLL
     LLLFLFIIIF SLLGMQLFGG KFNFDQTHTK RSTFDTFPQA LLTVFQILTG EDWNVVMYDG
     IMAYGGPFFP GMLVCIYFII LFICGNYILL NVFLAIAVDN LASGDAGTAK DKGGEKSNEK
     DLPQENEGLV PGVEKEEEEG ARREGADMEE EEEEEEEEEE EEGAGGVELL QEVVPKEKVV
     PIPEGSAFFC LSQTNPLRKG CHTLIHHHVF TNLILVFIIL SSVSLAAEDP IRAHSFRNHI
     LGYFDYAFTS IFTVEILLKM TVFGAFLHRG SFCRSWFNML DLLVVSVSLI SFGIHSSAIS
     VVKILRVLRV LRPLRAINRA KGLKHVVQCV FVAIRTIGNI MIVTTLLQFM FACIGVQLFK
     GKFYTCTDEA KHTPQECKGS FLVYPDGDVS RPLVRERLWV NSDFNFDNVL SAMMALFTVS
     TFEGWPALLY KAIDAYAEDH GPIYNYRVEI SVFFIVYIII IAFFMMNIFV GFVIITFRAQ
     GEQEYQNCEL DKNQRQCVEY ALKAQPLRRY IPKNPHQYRV WATVNSAAFE YLMFLLILLN
     TVALAMQHYE QTAPFNYAMD ILNMVFTGLF TIEMVLKIIA FKPKHYFTDA WNTFDALIVV
     GSIVDIAVTE VNNGGHLGES SEDSSRISIT FFRLFRVMRL VKLLSKGEGI RTLLWTFIKS
     FQALPYVALL IAMIFFIYAV IGMQMFGKVA LQDGTQINRN NNFQTFPQAV LLLFRCATGE
     AWQEIMLASL PGNRCDPESD FGPGEEFTCG SNFAIAYFIS FFMLCAFLII NLFVAVIMDN
     FDYLTRDWSI LGPHHLDEFK RIWSEYDPGA KGRIKHLDVV ALLRRIQPPL GFGKLCPHRV
     ACKRLVAMNM PLNSDGTVTF NATLFALVRT SLKIKTEGNL EQANQELRIV IKKIWKRMKQ
     KLLDEVIPPP DEEEVTVGKF YATFLIQDYF RKFRRRKEKG LLGNEAAPST SSALQAGLRS
     LQDLGPEMRQ ALTCDTEEEE EEGQEGVEEE DEKDLETNKA TVVSQPSTRQ GSRISVSPPV
     GDRLPDSLSF GPSDDDRGTP TSSQPSVPQA GSNTHRRGSG ALIFTIPEEG NSQPKGTKGQ
     NKQDEDKEVP DRLSYLDEQA GTPPCSVLLP PHRAQRYMDG HLVPRRRLLP PTPAGRKPSF
     TIQCLQRQGS CEDLPIPGTY HRGRNSGPNR AQGSWATPPQ RGRLLYAPLL LVEEGAAGEG
     YLGRSSGPLR TFTCLHLPGT HSDPSHGKRG SADSLVEAVL ISEGLGLFAR DPRFVALAKQ
     EIADACRLTL DEMDNAASDL LAQGTSSLYS DEESILSRFD EEDLGDEMAC VHNL
//
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