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Database: UniProt
Entry: U3JKP9_FICAL
LinkDB: U3JKP9_FICAL
Original site: U3JKP9_FICAL 
ID   U3JKP9_FICAL            Unreviewed;      2159 AA.
AC   U3JKP9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   25-OCT-2017, entry version 35.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSFALP00000003353};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae;
OC   Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003353, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000003353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N.,
RA   Kawakami T., Kunstner A., Makinen H., Nadachowska-Brzyska K.,
RA   Qvarnstrom A., Uebbing S., Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula
RT   flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000003353}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2013) 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 an
CC       opposit 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}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSFALP00000003353}.
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DR   EMBL; AGTO01011855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSFALT00000003366; ENSFALP00000003353; ENSFALG00000003063.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Proteomes; UP000016665; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; IEA:Ensembl.
DR   GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IEA:Ensembl.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0002520; P:immune system development; IEA:Ensembl.
DR   GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005451; VDCC_L_a1csu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01635; LVDCCALPHA1C.
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:UP000016665};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     64     81       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    132    148       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    204    226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    286    307       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    319    341       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    462    480       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    500    523       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    592    611       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    664    691       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    842    860       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    872    891       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    898    920       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    932    958       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    979   1012       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1104   1130       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1181   1202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1214   1232       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1244   1261       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1348   1371       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1441   1465       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1599   1633       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      694    717       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2159 AA;  243319 MW;  2AF5C87D31FE2F14 CRC64;
     MGSAGNATIS TASSTQRKRQ QYGKQKKQGS TTATRPPRAL LCLTLKNPIR RACISIVEWK
     PFEIIILLTI FANCVALAIY IPFPEDDSNA TNSNLERVEY LFLIIFTVEA FLKVIAYGLL
     FHPNAYLRNG WNLLDFIIVV VGLFSAILEQ ATKADGGNSI GGKGAGFDVK ALRAFRVLRP
     LRLVSGVPSL QVVLNSIIKA MVPLLHIALL VLFVIIIYAI IGLELFMGKM HKTCYHVQGG
     LIDTPAEDDP SPCAPQSAHG RQCQNGTECK AGWEGPKHGI TNFDNFAFAM LTVFQCITME
     GWTDVLYWVN DAIGRDWPWI YFVTLIIIGS FFVLNLVLGV LSGEFSKERE KAKARGDFQK
     LREKQQLEED LKGYLDWITQ AEDIDPENED EGMDEEKPRN MSMPTSETES VNTDNVPGAD
     MEGENCGARL AHRISKSKFS RYWRRWNRFC RRKCRAAVKS NVFYWLVIFL VFLNTLTIAS
     EHYNQPDWLT EVQGDTANKV LLALFTAEML LKMYSLGLQA YFVSLFNRFD CFIVCGGILE
     TILVETKIMS PLGISVLRCV RLLRIFKITR YWNSLSNLVA SLLNSVRSIA SLLLLLFLFI
     IIFSLLGMQL FGGKFNFDEM QTRRSTFDNF PQSLLTVFQI LTGEDWNSVM YDGIMAYGGP
     SFPGMLVCIY FIILFICGNY ILLNVFLAIA VDNLADAESL TSAQKEEEEE KERKKLARIA
     RTASPEKKQE MEKTAVEEET KEEKIELKSI TADGESPPAT KINVDDYQPN ENEEKSPYPT
     TEAPAEEDEE EPEMPVGPRP RPMSELHLKE KAVPMPDASA FFIFSPNNRF RVHCHRIVND
     NIFTNLILFF ILLSSISLAA EDPVRHLSFR NQILFYFDIV FTVIFTIEIA LKILGNADYV
     FTSIFTLEII LKMTAYGAFL HKGSFCRNYF NILDLLVVSV SLISFGIQSS AINVVKILRV
     LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI GNIVIVTTLL QFMFACIGVQ LFKGKLYSCT
     DSSKQTEAEC RGYYITYKDG EVSQPMIQPR SWENSKFDFD NVLTAMMALF TVSTFEGWPE
     LLYRSIDSHM EDVGPIYNHR VEISIFFIIY IIIIAFFMMN IFVGFVIVTF QEQGEQEYKN
     CELDKNQRQC VEYALKARPL RRYIPKNQYQ YKVWYVVNST YFEYLMFVLI LLNTICLAMQ
     HYGQSCMFKE AMNILNMLFT GLFTVEMVLK LIAFKPKGYF SDPWNVFDFL IVIGSIIDVI
     LSETNHYFCD AWNTFDALIV VGSIVDIAIT EVNPAEHTQC SSSMNAEENS RISITFFRLF
     RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT
     EINRNNNFQT FPQAVLLLFR CATGEAWQEI MLACLPDKKC DPESEPANST EADHSCGSSF
     AVFYFISFYM LCAFLIINLF VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR
     IKHLDVVTLL RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR
     IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF
     KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS
     EDDIFRRAGG LFGNHVSYYQ SDGRSGFPQT FTTQRPLHIN KSGNNHGDTE SPSHEKLVDS
     TFTPSSYSSS GSNANINNAN NTALCRFPSP PSYPSTVSTV EGHGTPLSPT ICVQEAPWKL
     PAKRGHQRHS GRREDTLLRD TGTPGCQTHS VTLLKLQVPS NADSRDSQLA IVCQEEVSQD
     ETYDENLNED IEYCSEPSLL STEMLAYQDD ENRQLTLPES SKGEDTRHSP KKGFLCSSAL
     GRRASFHLEC LKRQKNQGVD VSQKTVLPLH LVHHQALAVA GLSPLLQRSH SPTSFSRLCA
     TPPATPCNRG WAQQTIPTLR LDGAESSEKL NSSLPSVHCG SRCPESGGSP RRARPVSLTV
     PSPSAGSSRQ LHGSASSLVE AVLISEGLMQ FAQDPKFIEV TTQELADACD MTIEEMENAA
     DNILNGNSKQ SPNGNLLPFA NCRDPGQDSA GEEEEEVQNP DCRISQEELK DSRIYISSL
//
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