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Database: UniProt
Entry: U3JSJ5_FICAL
LinkDB: U3JSJ5_FICAL
Original site: U3JSJ5_FICAL 
ID   U3JSJ5_FICAL            Unreviewed;      1559 AA.
AC   U3JSJ5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   25-OCT-2017, entry version 30.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
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:ENSFALP00000005749, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000005749}
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:ENSFALP00000005749}
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-1B
CC       gives rise to N-type calcium currents. N-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
CC       IIIA (omega-Aga-IIIA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing alpha-1B subunit may play a role in
CC       directed migration of immature neurons.
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:ENSFALP00000005749}.
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DR   EMBL; AGTO01001411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTO01011530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTO01011531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTO01021650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTO01021651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSFALT00000005776; ENSFALP00000005749; ENSFALG00000005517.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; DSPRNNA; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Proteomes; UP000016665; Unplaced.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF161; PTHR10037:SF161; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
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     55     77       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    131    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    164    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    339    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    365    382       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    464    486       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    542    564       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1004   1023       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1043   1064       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1076   1094       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1137   1159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1249   1274       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1330   1348       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1360   1386       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1454   1481       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1540   1557       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    177       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      337    573       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1005   1280       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1326   1556       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED      573    600       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1559 AA;  177286 MW;  3D24FB33781D4D72 CRC64;
     MDFVVVLTGI LATAGTDFDL RTLRAVRVLR PLKLVSGIPS LQVVLKSIMK AMVPLLQIGL
     LLFFAIVMFA IIGLEFYMGK FHKTCFSNET GEEVGDFPCG EEPPARQCES GTTCREYWQG
     PNYGITNFDN ILFAVLTVFQ CITMEGWTDI LYNTNDAAGN TWNWLYFIPL IIIGSFGIER
     FPGVVQWEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK
     SPLDGRAASE GPIPQGTAPA ETGSGSSYNM LKRAAIKKSK NDLIHAEEGE DHFTDICSVG
     SPFARASLKS GKNESSSYFR RKEKMFRFFI RRMVKAQSFY WVVLCVVALN TLCVAMVHYD
     QPEKLTTALY FAEFVFLGLF LTEMSLKMYG LGPRNYFHSS FNCFDFGVIV GSIFEVIWAA
     VKPGTSFGIS VLRALRLLRI FKVTKYWNSL RNLVVSLLNS MKSIISLLFL LFLFIVVFAL
     LGMQLFGGQF NFQDETPTTN FDTFPAAILT VFQILTGEDW NAVMYHGIES QGGVHSGMFS
     SIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEEEM EEATNQKLAL QKAKEVAEVS
     PMSAANISIA AKQQNSSKSK SVWEQRTSQI RMHNFRASCE ALYNELDPEE RVRYATTLHI
     RPDMKTHLDR PLVVEPRGEG RNNISKLSPG DAQEVVEHPK PTAGDGAEAP RKHHRHRDKE
     KLGEQEKGDG TKDESGDAGA GGKEERHRQH RSRSKEVEGK SDRSRGQEGG KRHHRRGSVE
     EGADKEHRRH RSHRHPSERP GKDGNGNGSR GERRSRHRGA PRSAHRDGEP RAESGDEPHR
     RHRLRNRALA ACEALEKDGG DKEGEAGDKE HRNHQPKENQ CELEASGSGS GPGSVPVHTL
     PSTYLQKVPE QPEDADNQKN VTRMIQPPLD KTTTVNIPVT ITAPPGDTTV IPMNNVEFES
     KTEEKKDVDD LTKNGPKPIL PYSSMFILSP TNPIRRLFHY IVNLRYFEMV ILIVIALSSI
     ALAAEDPVQA ESPRNDALKY LDYIFTGVFT FEMVIKMIDL GLLLHPGSYF RDLWNILDFI
     VVSGALVAFA FSGTKGKDIN TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLKNVLNI
     LIVYMLFMFI FAVIAVQLFK GRFFYCTDES KELEKDCRGQ YLDYEKNEVE AQPREWKKYE
     FHYDNVLWAL LTLFTVSTGE GWPTVLKHSV DATYEEQGPS PGYRMEMSIF YVVYFVVFPF
     FFVNIFVALI IITFQEQGDK VMSECSLEKN ERACIDFAIS AKPLTRYMPQ NKQSFQYKMW
     KFVVSPPFEY FIMVMIALNT IVLMMKFYDA PEAYEEMLKC LNIVFTSMFS MECVLKIIAF
     GVLNYFRDAW NVFDFVTVLG SITDILVTEI AVKDNFINLS FLRLFRAARL IKLLRQGYTI
     RILLWTFVQS FKALPYVCLL IAMLFFIYAI IGMQVFGNIA LDDETSINRH NNFRTFLQAL
     MLLFRSATGE AWHEIMLSCL SNRACDPLSG LTKKECGSDF AYFYFVSFIF LCSFLVSQS
//
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