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Database: UniProt
Entry: A0A087VD45_BALRE
LinkDB: A0A087VD45_BALRE
Original site: A0A087VD45_BALRE 
ID   A0A087VD45_BALRE        Unreviewed;      1726 AA.
AC   A0A087VD45;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   18-JUL-2018, entry version 22.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N312_08842 {ECO:0000313|EMBL:KFO10537.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO10537.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO10537.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO10537.1};
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-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}.
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DR   EMBL; KL488872; KFO10537.1; -; Genomic_DNA.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 3.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF161; PTHR10037:SF161; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
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:UP000053309};
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:UP000053309};
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}.
FT   TRANSMEM     35     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     96    118       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    174    196       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    640    659       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    679    700       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    712    730       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    773    795       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    885    910       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    966    984       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    996   1019       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1088   1115       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1175   1199       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1337   1371       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      205    232       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFO10537.1}.
FT   NON_TER    1726   1726       {ECO:0000313|EMBL:KFO10537.1}.
SQ   SEQUENCE   1726 AA;  195783 MW;  F58D165A24B7CF5F CRC64;
     LDFAEFVFLG LFLTEMSLKM YGLGPRNYFH SSFNCFDFGV IVGSIFEVIW AAVKPGTSFG
     ISVLRALRLL RIFKVTKYWN SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG
     QFNFQDETPT TNFDTFPAAI LTVFQILTGE DWNAVMYHGI ESQGGVRSGM FSSIYFIVLT
     LFGNYTLLNV FLAIAVDNLA NAQELTKDEE EMEEATNQKL ALQKAKEVAE VSPMSAANIS
     IAAKQQNSSK SKSVWEQRTS QIRMHNFRAS CEALYNELDP EERVRYATTL HIRPDMKTHL
     DRPLVVEPRG DGRNNISKLS PVDVQEVEQT KVSSTDGAEA PRKHHRHRDK DKLGEQEKGD
     VTKDENGESG INNKEERHRQ HRSRSKEVEG GSKEGKSDRS RGQEGGKRHH RRGSVEEGVE
     KEHRRHRTHR HSAERQGKEG NGTINGARSE RRSRHRGGSR SGNREGEPGS KGENGEEPHR
     RHRFRNRALS TYDSVEKENG EKEGEAGEKE HRNHQPKENQ CEIEASGSVS VPVHTLPSTY
     LQKVPEQPED ADNQKNVTRM IQPPLDKTTT VNIPVTITAP PGETTVIPMN NVEFESKTEE
     KKDVDDLTKN GPKPILPYSS MFILSPTNPI RRLFHYIVNL RYFEMVILIV IALSSIALAA
     EDPVQAESPR NDALKYLDYI FTGVFTFEMV IKMIDLGLLL HPGSYFRDLW NILDFIVVSG
     ALVAFAFSGT KGKDINTIKS LRVLRVLRPL KTIKRLPKLK AVFDCVVNSL KNVLNILIVY
     MLFMFIFAVI AVQLFKGRFF YCTDESKELE KDCRGQYLDY EKNEVEAQPR EWKKYEFHYD
     NVLWALLTLF TVSTGEGWPT VLKHSVDATY EEQGPSPGYR MEMSIFYVVY FVVFPFFFVN
     IFVALIIITF QEQGDKVMSE CSLEKNERAC IDFAISAKPL TRYMPQNKQS FQYKMWKFVV
     SPPFEYFIMV MIALNTIVLM MKFYDAPEAY EEMLKCLNIV FTSMFSMECV LKIIAFGVLN
     YFRDAWNVFD FVTVLGSITD ILVTEIADNF INLSFLRLFR AARLIKLLRQ GYTIRILLWT
     FVQSFKALPY VCLLIAMLFF IYAIIGMQVF GNIALDDETS INRHNNFRTF LQALMLLFRS
     ATGEAWHEIM LSCLSNRACD PLSGLTKNEC GSDFAYFYFV SFIFLCSFLM LNLFVAVIMD
     NFEYLTRDSS ILGPHHLDEF VRVWAEYDPA ACCRIHYKDM YNLLRVIAPP LGLGKKCPHR
     VAYKRLVRMN MPISPEDLTV HFTSTLMALI RTALEIKLAS GGVKQHQCDA ELRKEISLVW
     PNLSQKTLDL LVPPHKPDEM TVGKVYAALM IFDFYKQNKN SREQVHQPPG GLCQPGPVSL
     FHPLKATLEQ TQSTAFNNAK AFLRQKSSAS LNNGGALPAP EGGIKESSSW GTQRTQDVFY
     ETRTPGFERG HSEEIPIERV VEMREISPTL ANGEHQPGLD GGGAPSMPRL AAETQRSKAR
     SPGSYLAPIP DTSPMKRSVS TLTPQRPHAM HLYEYSLERM PPEQGHHHHH HRCHRRKEKK
     QKSLDRSPHQ MADGEAVAQS GESSSKDKKQ ERGRSQERKQ HSSSSSEKQR FYSCDRYGSR
     DRSHPKSADQ SRPTSPNGGP EQGPHRQGSG SVNGSPLLST SGASTPCRGR RQLPQTPLTP
     RPSITYKTAN SSPVHFTSFQ TGLPTFSPGR LSRGLSEHNA LLRGDQ
//
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