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Database: UniProt
Entry: F7HTP7_CALJA
LinkDB: F7HTP7_CALJA
Original site: F7HTP7_CALJA 
ID   F7HTP7_CALJA            Unreviewed;      2236 AA.
AC   F7HTP7;
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:ENSCJAP00000008352, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000008352, 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:ENSCJAP00000008352}
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; ENSCJAT00000008831; ENSCJAP00000008352; 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; -; 3.
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; 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; 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   2236 AA;  252874 MW;  2E1B6878CD96AED6 CRC64;
     MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
     NCFTVNRSLF IFGEDNIVRK YYMILATIIA NCIVLALEQH LPEDDKTPMS RRLEKTEPYF
     IGIFCFEAGI KIVALGFIFH KGSYLRNGWN VMDFIVVLSG ILATAGTHFN THVDLRTLRA
     VRVLRPLKLV SGIPSLQIVL KSIMKAMVPL LQIGLLLFFA ILMFAIIGLE FYSGKLHRAC
     FMNNSGILEG FDPPHPCGVQ GCPAGYECKD WIGPNDGITQ FDNILFAVLT VFQCITMEGW
     TTVLYNTNDA LGATWNWLYF IPLIIIGSFF VLNLVLGVLS GEFAKERERV ENRRAFMKLR
     RQQQIERELN GYRAWIDKAE EVMLAEENKN AGTSALEVLR RATIKRSRTE AMTRDSSDEH
     CVDISSVGTP LARASIKSTK VDGVSYFRHK ERLLRISIRH MVKSQVFYWI VLSLVALNTA
     CVAIVHHNQP QWLTHLLYYA EFLFLGLFLL EMSLKMYGMG PRLYFHSSFN CFDFGVTVGS
     IFEVVWAIFR PGTSFGISVL RALRLLRIFK ITKYWASLRN LVVSLMSSMK SIISLLFLLF
     LFIVVFALLG MQLFGGRFNF NDGTPSANFD TFPAAIMTVF QILTGEDWNE VMYNGIRSQG
     GVSSGMWSAI YFIVLTLFGN YTLLNVFLAI AVDNLANAQE LTKDEQEEEE AFNQKHALQK
     AKEVSPMSAP NMPSIERERR RRHHMSVWEQ RTSQLRKHMQ MSSQEALNRE EAPPMNPLNP
     LNPLSPLNPL NAHPSLYRRP RAIEGLALGL ALEKFDEERI SRGGSLKGEG GDRSSTLDNQ
     RTPLSLGQRE LPWLPRSCHG NCDPTQQEAG GGEAVVTFED RARHRQSQRR SRHRRVRTEG
     KESSSASRSR SASQERSLDE AVPAEGEKEH ELRGNHSAKE PTIQEERAQD LRRTNSLMLS
     RGSGLAGALD EANTPLVLPH PELEVGKDAV LTEQEPEGSS EQALLGDVQL DMGRVISHSE
     PDLSCITANT DKAITESTSV TVAIPDVGPL VDSTVVHISN KTDGEASPLK EAEIRDDEEE
     VENKKQKKEK RETGKAMVPH SSMFIFSTTN PIRRACHYIV NLRYFEMCIL LVIAASSIAL
     AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE MVIKMIDQGL ILQDGSYFRD LWNILDFVVV
     VGALVAFALA TNKGRDIKTI KSLRVLRVLR PLKTIKRLPK LKAVFDCVVT SLKNVFNILI
     VYKLFMFIFA VIAVQLFKGK FFYCTDSSKD TEKECIGNYV DHEKNKMEVK GREWKRHEFH
     YDNIIWALLT LFTVSTGEGW PQVLQHSVDV TEEDRGPSRS NRMEMSIFYV VYFVVFPFFF
     VNIFVALIII TFQEQGDKMM EECSLEKNER ACIDFAISAK PLTRYMPQNR HTFQYRVWHF
     VVSPSFEYTI MAMIALNTVV LMMKYYSAPC TYELALKYLN IAFTMVFSLE CVLKVIAFGF
     LNYFRDTWNI FDFITVIGSI TEIILTDSKL VNTSGFNMSF LKLFRAARLI KLLRQGYTIR
     ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIKL DEESHINRHN NFRSFFGSLM
     LLFRSATGEA WQEIMLSCLG EKGCEPDTTA PSGQNENERC GTDLAYVYFV SFIFFCSFLM
     LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF VRVWAEYDRA ACGRIPYKDM YKLVRVISPP
     LGLGENCPYR VACKRLVLMN MPVAEDMTVH FTSTLMALIR TALDIKIAKG GADRQQLDSE
     LQKETLAIWP HLSQKMLDLL VPMPKASDLT VGKIYAAMMI MDYYKQSKVK KQRQQLEEQK
     NAPMFQRMEP SSLPQEIIAN AKALPYLQQD TVSGLSGRTG YPSMSPLSPQ EIFQLACMDP
     ADDGQFQEQQ SLVVTDPSSM RRSFSTIRDK RSNSSWLEEF SMERSSENTY KSRRRSYHSS
     LRLSAHRLNS DSGHKSDTHR SGGRERGRSK ERKHLLSPDV SRCNSEERGT QADWESPERR
     QSRSPSEGRS QTPNQQGTGS LSESSIPSVS DTSTPRRSRR QLPPVPPKPR PLLSYSSLIR
     HAGSISPPAD GSQEGSPLTS QALESNNACL TESSNSPHPQ QGQHISPQRY ISEPYLAQHE
     DSHASDCGEE ETLTFEAAVA TSLGRSNTIG SAPPLRHSWQ MPNGHYRRRR RGGPGSGMMC
     GAVNNLLSDT EEDDKC
//
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