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Database: UniProt
Entry: A0A093HKW3_STRCA
LinkDB: A0A093HKW3_STRCA
Original site: A0A093HKW3_STRCA 
ID   A0A093HKW3_STRCA        Unreviewed;      1999 AA.
AC   A0A093HKW3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N308_02204 {ECO:0000313|EMBL:KFV80095.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV80095.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV80095.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV80095.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL206226; KFV80095.1; -; Genomic_DNA.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
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   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   PANTHER; PTHR10037:SF57; PTHR10037:SF57; 3.
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:UP000053584};
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:UP000053584};
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     38     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     80    101       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    133       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    172    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    246    267       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    279    301       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    428    448       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    454    472       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    554    576       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    632    654       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1021   1039       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1091   1108       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1174       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1264   1289       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1345   1363       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1375   1398       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1404   1422       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1469   1487       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1562   1586       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1602   1637       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      650    677       {ECO:0000256|SAM:Coils}.
FT   COILED      966    988       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFV80095.1}.
FT   NON_TER    1999   1999       {ECO:0000313|EMBL:KFV80095.1}.
SQ   SEQUENCE   1999 AA;  225998 MW;  851484F7B5A7CB10 CRC64;
     ALYNPIPVRQ NCFTVNRSLF LFGEENIVRK YAKKLIDWPY PFCYMILATI IANCIVLALE
     QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFV FHKGSYLRNG WNVMDFIVVL
     SGILATAGTH FNTHVDLRTL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF
     FAILMFAIIG LEFYSGKLHR ACYTNNSGEL EELDPPHPCG VQGCPPGYEC REWIGPNDGI
     TQFDNILFAV LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV
     LSGEFAKERE RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNTGTSALEV
     LRRATIKRNR TDAMNRDSSD EHCVDIASVG NPLTCSSIKG ARFSGASYFR HKERLLRISV
     RHMVKSQVFY WIVLSLVALN TACVAIVHHN QPAWLTHFLY YAEFLFLGLF LLEMSLKMYG
     MGPRLYFHSS FNCFDCGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL
     RNLVVSLMSS MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFIDGTPSAN FDTFPAAIMT
     VFQILTGEDW NEVMYNGIRS QGGVRSGMWS SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
     QELTKDEQEE EEAFNQKHAL QKAKEVSPMS APNMPAIDVG KLSFAALRME MQSEPLKLGQ
     PQLAVGLPAH LGKKAVPARA DSLSGCFSED GWLCEWAPPR QPCLSERQGC GRKKGSLGSS
     SVGNLPQAPS LIANAVMRNG TGRTEGKEPA GALESRSASQ ETGLEEAGPA EGAQDGDRHG
     AAATEDLIQG EPEASQETAR TNGVPAAELV GTAKEGSPLQ AASELGQGKN GSLTEQDCSS
     LDTSEQALLG SLQLEASRAV SRSEPDLSSI TANTEKATES TTIMIDVQDS TVVQISNKTD
     GEASPLKEAE TKEDEEEMEK KKRKKEKSET GKAMVPHSSM FIFSTTNPVR RACHYIVNLR
     YFEMCILLVI AASSIALAAE DPVLTNSDRN KVLRYFDYVF TGVFTFEMVI KMIDQGLILQ
     DGSYFRDLWN ILDFIVVVGA LVAFALATNK GRDIKTIKSL RVLRVLRPLK TIKRLPKLKA
     VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY CTDSSKDTEK DCIGNYVDHE
     KNKMEVKCRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV LQHSVDVTEE DRGPSRSNRM
     EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC SLEKNERACI DFAISAKPLT
     RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM KYYSAPYTYE LALKYLNIAF
     TMVFSLECVL KIIAFGFLNY FRDTWNIFDF ITVIGSITEI ILTDTKLVNT SSFNMSFLKL
     FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIKLDEE
     SHINRHNNFR SFLGSLMLLF RSATGEAWQE IMLSCLEGKG CEPDTTATSG QNENERCGTD
     LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFVRI WAEYDRAACG
     RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV AEDMTVHFTS TLMALIRTAL
     DIKIAKGGAD WQQLDSELQK EILTIWPHLS QKVLDLLVPM PKTSDLTVGK IYAAMMIMDY
     YKQSKAKKQR QQLEEQKNAP MFQRMEPSSL PQEIISNAKA LPYLQQDTIS GLSSRSGFPS
     LSPLSPQEIF QLACMDSTHG QFQEHQSLVV TDTSSMRRSF STIRDKRTNS SWLDEFSMER
     SSENTYKSRR RSYHSSLQLS ARRLNADSGH RSDGHRSGGR ERGRSKERKH LLSPDISRCN
     SEERSPQAHD ESPERRRESR SPSEGRSQTP NRQGTGSLSE SSIPSISDTS TPRRGRRQLP
     PVPPKPRPLL SYASMLRHA
//
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