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Database: UniProt
Entry: F7IHV2_CALJA
LinkDB: F7IHV2_CALJA
Original site: F7IHV2_CALJA 
ID   F7IHV2_CALJA            Unreviewed;      2294 AA.
AC   F7IHV2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   20-JUN-2018, entry version 43.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000008406, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000008406, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000008406}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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-1E
CC       gives rise to R-type calcium currents. R-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA).
CC       They are however insensitive to dihydropyridines (DHP), omega-
CC       conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-
CC       Aga-IVA). Calcium channels containing alpha-1E subunit could be
CC       involved in the modulation of firing patterns of neurons which is
CC       important for information processing.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
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DR   Ensembl; ENSCJAT00000008890; ENSCJAP00000008406; ENSCJAG00000004426.
DR   eggNOG; ENOG410INF5; Eukaryota.
DR   eggNOG; ENOG410YD06; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008225; 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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
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; IPR005449; VDCC_R_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF57; PTHR10037:SF57; 2.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01633; RVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   PROSITE; PS50222; EF_HAND_2; 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:UP000008225};
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:UP000008225};
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}.
SQ   SEQUENCE   2294 AA;  259222 MW;  DD45967BF7C06832 CRC64;
     MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
     NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
     SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
     NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
     EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
     TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
     VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT
     EAMTRDSSDE HCVDISSVGT PLARASIKST KVDGVSYFRH KERLLRISIR HMVKSQVFYW
     IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
     NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
     KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
     EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
     EAFNQKHALQ KAKEVSPMSA PNMPSIERER RRRHHMSVWE QRTSQLRKHM QMSSQEALNR
     EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRAIEGLALG LALEKFDEER ISRGGSLKGE
     GGDRSSTLDN QRTPLSLGQR ELPWLPRSCH GNCDPTQQEA GGGEAVVTFE DRARHRQSQR
     RSRHRRVRTE GKESSSASRS RSASQERSLD EAVPAEGEKE HELRGNHSAK EPTIQEERAQ
     DLRRTNSLML SRGSGLAGAL DEANTPLVLP HPELEVGKDA VLTEQEPEGS SEQALLGDVQ
     LDMGRVISHS EPDLSCITAN TDKAITESTS VTVAIPDVGP LVDSTVVHIS NKTDGEASPL
     KEAEIRDDEE EVENKKQKKE KRETGKAMVP HSSMFIFSTT NPIRRACHYI VNLRYFEMCI
     LLVIAASSIA LAAEDPVLTN SERNKVLRYF DYVFTGVFTF EMVIKMIDQG LILQDGSYFR
     DLWNILDFVV VVGALVAFAL ANALGTNKGR DIKTIKSLRV LRVLRPLKTI KRLPKLKAVF
     DCVVTSLKNV FNILIVYKLF MFIFAVIAVQ LFKGKFFYCT DSSKDTEKEC IGNYVDHEKN
     KMEVKGREWK RHEFHYDNII WALLTLFTVS TGEGWPQVLQ HSVDVTEEDR GPSRSNRMEM
     SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ GDKMMEECSL EKNERACIDF AISAKPLTRY
     MPQNRHTFQY RVWHFVVSPS FEYTIMAMIA LNTVVLMMKY YSAPCTYELA LKYLNIAFTM
     VFSLECVLKV IAFGFLNYFR DTWNIFDFIT VIGSITEIIL TDSKLVNTSG FNMSFLKLFR
     AARLIKLLRQ GYTIRILLWT FVQSFKALPY VCLLIAMLFF IYAIIGMQVF GNIKLDEESH
     INRHNNFRSF FGSLMLLFRS ATGEAWQEIM LSCLGEKGCE PDTTAPSGQN ENERCGTDLA
     YVYFVSFIFF CSFLMLNLFV AVIMDNFEYL TRDSSILGPH HLDEFVRVWA EYDRAACGRI
     HYTEMYEMLT LMSPPLGLGK RCPSKVAYKR LVLMNMPVAE DMTVHFTSTL MALIRTALDI
     KIAKGGADRQ QLDSELQKET LAIWPHLSQK MLDLLVPMPK ASDLTVGKIY AAMMIMDYYK
     QSKVKKQRQQ LEEQKNAPMF QRMEPSSLPQ EIIANAKALP YLQQDTVSGL SGRTGYPSMS
     PLSPQEIFQL ACMDPADDGQ FQEQQSLEPE VSEFKSVQPA NHGIYLPSDT QEHAGSGRAS
     SMPRLTVDPQ VVTDPSSMRR SFSTIRDKRS NSSWLEEFSM ERSSENTYKS RRRSYHSSLR
     LSAHRLNSDS GHKSDTHRSG GRERGRSKER KHLLSPDVSR CNSEERGTQA DWESPERRQS
     RSPSEGRSQT PNQQGTGSLS ESSIPSVSDT STPRRSRRQL PPVPPKPRPL LSYSSLIRHA
     GSISPPADGS QEGSPLTSQA LESNNACLTE SSNSPHPQQG QHISPQRYIS EPYLAQHEDS
     HASDCGEEET LTFEAAVATS LGRSNTIGSA PPLRHSWQMP NGHYRRRRRG GPGSGMMCGA
     VNNLLSDTEE DDKC
//
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