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Database: UniProt
Entry: G3WM56_SARHA
LinkDB: G3WM56_SARHA
Original site: G3WM56_SARHA 
ID   G3WM56_SARHA            Unreviewed;      2075 AA.
AC   G3WM56;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-SEP-2017, entry version 41.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1B {ECO:0000313|Ensembl:ENSSHAP00000016511};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000016511, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000016511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E.,
RA   Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q.,
RA   Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A.,
RA   Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S.,
RA   Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y.,
RA   Kreiss A., Woods G.M., Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered
RT   marsupial Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000016511}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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-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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
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:ENSSHAP00000016511}.
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DR   EMBL; AEFK01023236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01023242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9305.ENSSHAP00000016511; -.
DR   Ensembl; ENSSHAT00000016649; ENSSHAP00000016511; ENSSHAG00000014048.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G3WM56; -.
DR   OMA; DSPRNNA; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR   GO; GO:0048265; P:response to pain; IEA:Ensembl.
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; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF246; PTHR10037:SF246; 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; PR01631; NVDCCALPHA1.
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:UP000007648};
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:UP000007648};
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     46     68       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    126    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    159    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    311    331       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    337    354       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    375    393       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    436    458       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    514    536       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1020   1038       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1058   1078       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1090   1107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1153   1175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1265   1290       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1346   1365       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1377   1399       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1411   1435       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1456   1485       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1554   1578       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1594   1629       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      539    572       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2075 AA;  234198 MW;  EB56C90E056B1F8B CRC64;
     ILATAGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMVPLLQIG LLLFFAIVMF
     AIIGLEFYMG KFHKACFPNN TVSPYGPSPG DFPCGTDASA RQCENGYICR EYWRGPNFGI
     TNFDNILFAI LTVFQCITME GWTDILYNTN DAAGNTWNWL YFIPLIIIGS FFMLNLVLGV
     LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYLEWIFK AEEVMLAEED KNADEKSPLD
     AVLKRAATKK SKNDLIHAEE GDDRFADLCS VGSPFARASL KSGKNDSSSY FRRKEKMFRF
     FIRRMVKAQT FYWIVLCVVA LNTLCVAMVH YDQPQRLTNA LYFAEFVFLG LFLTEMSLKM
     YGLGPRNYFH SSFNCFDFGV IVGSIFEVIW AAIKPGTSFG ISVLRALRLL RIFKVTKYWN
     SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFRDETPN TNFDTFPAAI
     LTVFQILTGE DWNVVMYHGI ESQGGVSKGM FSSFYFIILT LFGNYTLLNV FLAIAVDNLA
     NAQELTKDEE ELEEAANQKL ALQKAKEVAE VSPLSAANIS IAAKNKQQNS AKARSVWEQR
     TSQIRLHNFQ ASCEALYSEM APEERLRYTT TLHIRPDMKT HLDRPLVVEP RREEGVRAPG
     GKAGTGEGLE ASEPTKVSPS AAAEGPEMPR KHHRHREKEK EKEKTGAGEQ EKGEXGRRHH
     RRGSVEDVTA EKEHRRHRAH RHSAEPPGKE GNGTVSGAKP ERRARHRGGS RSGTREGEPG
     PKGENGEEPP RRHKTRHKAL SMYDSVEKEP GERERRHLEN QCEAEASGGM VTIPIHTLPS
     TCLQKVSEQP EDADNQKNVH RMTQPSLETL TIRIPVTLTA PGETTVVPRL FETYPPSLKG
     HDPRNRVGNP FQPPPQKTTT TTTTTATTKS KQKSSKLIPH TCIICPLPSP CPVNHFIVNL
     QASKLVDGLP ISKMEEKKDV EAGDVTRSGP RPILPYSSMF CLSPTNLLRR ACHYIVNMRY
     FEMVILGVIA LSSIALAAED PVQADSPRNN VLKYMDYIFT GVFTFEMVIK MIDLGLLLHP
     GSYFRDLWNI LDFIVVSGAL VAFAFSFNSR KGKDISTIKS LRVLRVLRPL KTIKRLPKLK
     AVFDCVVNSL KNVLNILIVY MLFMFIFAVI AVQLFKGKFF YCTDESKELQ RDCRGQYLDY
     EKDEVEAQPR QWKKYDFHYD NVLWALLTLF TVSTGEGWPT VLKHSVDATY EEQGPSPGFR
     MELSIFYVVY FVVFPFFFVN IFVALIIITF QEQGDKVMSE CSLEKNERAC IDFAISAKPL
     TRYMPQNKQS FQYKTWTFVV SPPFEYFIMA MIALNTAVLM MKFYGAPYEY EMMLKGLNIV
     FTSMFSMECV LKIIAFGVLN YFRDAWNVFD FVTVLGSITD ILVTEIANNF INLSFLRLFR
     AARLIKLLRQ GYTIRILLWT FVQSFKALPY VCLLIAMLFF IYAIIGMQVF GNIALDDETN
     INRHNNFRTF LQALMLLFRS ATGEAWHEIM LSCLSDRPCD PETKLKDECG SDFAYFYFVS
     FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYSDMF
     EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR TALDIKLAPG
     SIAGMKQHQC DAELRKEIAS VWANLPQKTL DLLVPPHKPD EMTVGKVYAA LMIFDFYKQN
     KNTRDQGHQP PLQTGPVSLF HTQGQPAVLR GARVFLKQKS STSLSNGGAF RPHPGSGIKE
     SVSWGTQRTQ DICYETRMPL ERGHSAEIPV GQPSKQAVEM QEMAQDATSG EPQPGLESQG
     RAASMPRLAA EMQRSQARSP GSYLAPIPDT SPMKRSISTL APQRPHGSHL YEYGLERVSS
     GQPQHHHHHR CHRRRDKKQK SLDKCTSQSA DGDGAPNHSV GMAAPSGEGP APCKHERKQE
     RGRSQERKQL SSSSSEKQRF YSCDRFGSRD PSQPKSSNGS RPTSPPGQEP GPHRQGSGSV
     NGSPLLSTSG ASTPGRGGRR QLPQTPLTPR PSITY
//
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