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Database: UniProt
Entry: L8YDQ4_TUPCH
LinkDB: L8YDQ4_TUPCH
Original site: L8YDQ4_TUPCH 
ID   L8YDQ4_TUPCH            Unreviewed;      2195 AA.
AC   L8YDQ4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-SEP-2017, entry version 27.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=TREES_T100011192 {ECO:0000313|EMBL:ELV13105.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV13105.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) 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}.
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; KB362898; ELV13105.1; -; Genomic_DNA.
DR   ProteinModelPortal; L8YDQ4; -.
DR   InParanoid; L8YDQ4; -.
DR   Proteomes; UP000011518; 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; 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:UP000011518};
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:UP000011518};
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     57       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     69     87       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    199    220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    254       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    384    402       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    414    434       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    509    531       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    587    609       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1045   1070       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1090   1111       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1123   1141       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1184   1206       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1296   1321       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1377   1395       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1407   1430       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1442   1466       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1487   1516       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1585   1608       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1624   1659       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      612    638       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2195 AA;  245220 MW;  9316DBB2CC456534 CRC64;
     MILATIIANC IVLALEQHLP DGDKTPMSER LDDTEPYFIG IFCFEAGMKI VALGFALHRG
     SYLRNGWNVM DFVVVLTGIL ATAGTDFDLR TLRAVRVLRP LKLVSGIPSL QVVLKSIMKA
     MVPLLQIGLL LFFAILMFAI IGLEFYMGRF HKACFPNSTE PVGDFPCGKE APARLCEGDT
     ECREYWPGPN FGITNFDNIL FAILTVFQCI TMEGWTDILY STNDAAGNTW NWLYFIPLII
     IGSFFMLNLV LGVLSGEFAK ERERVENRRA FLKLRRQQQI ERELNGYLEW IFKAEEVMLA
     EEDKNAEEKS PLDAVLKRAA TKKSRNDLIH AEEGADRLAD LCALGSPFAR ASLKSGKTDS
     SSYFRRKEKM FRFFIRRLVK AQSFYWAVLC VVALNTLCVA VVHHNQPQRL TTALYFAEFV
     FLGLFLTEMS LKMYGLGPRS YFRSSFNCFD CGVIVGSIFE VVWAAIKPGT SFGISVLRAL
     RLLRIFKVTK YWNSLRNLVV SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE
     TPTTNFDTFP AAILTVFQIL TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL
     LNVFLAIAVD NLANAQELTK DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN
     SAKARSVWEQ RASQLRLQNL RASCEALYSE MDPEERLHYA TSRHLRPDMK THLDRPLEVE
     PGRDGPRAST GPKARSEGVE ATEGGDPPRR HHRHRDKDRA LSTAPPAGDQ DGADAPKAES
     GGQVAREERA RPRRSCSKED AGPRGEAAGP REVRGERGRG LGSEGPRRHH RHGSPEEAAE
     REPRRHRGHR HADQGKEGTT LGAKGERRAR HRGGLRAGPR ETENGEEPAR RHRVRHKVQS
     PPEGTEKEAA GTAGGGKDKE PRNHHPMEPN CDLEASVMTA PAHTLHSTCL QKVEEQPEDA
     DNQRNVTRTG SPPSDPSTVV HIPVTLTAPP GETEVIPSGN VDPESQAEGR KEVEADEGMG
     SGPRPIVPYS SMFCLRPTNL LRRCCLYIVT MRYFEMVILV VIALSSIALA AEDPVWTDSP
     RNNVLKYMDY IFTGVFTFEM VIKMVDLGLL LHPGAYFRDL WNVLDFIVVS GALVAFAFSG
     SKGKDISTIK SLRVLRVLRP LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV
     IAVQLFKGKF FYCTDESKEL ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL
     FTVSTGEGWP MVLKHSVDAT YEEQGPSPGY RMELSIFYVV YFVVFPFFFV NIFVALIIIT
     FQEQGDKVMS ECSLEKNERA CIDFAISAKP LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM
     AMIALNTAVL MMKFYDAPYE YELMLKGLNV VFTSMFSMEC VLKIIAFGVL NYFRDAWNVF
     DFVTVLGSIT DILVTEIANN FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP
     YVCLLIAMLF FIYAIIGMQV FGNIALDDDT SINRHNNFRT FLQALMLLFR SATGEAWHEI
     MLSCLSHRAC DRLANASECG SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI
     LGPHHLDEFI RVWAEYDPAA CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM
     PISNEDMTVH FTSTLMALIR TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL
     VPPHRPGEMT VGKVYAALMI FDFYKQSKTS RDQARQAPGG LSQMGPVSLF HPLKATLEQT
     QPAVLRGARV FLRQKSSTSL SNGGAVQTQQ SGIKESVSWG TQRTQDTPCE ARPPLERGHS
     AEIPVGQSRT LAVDVQTALK DPDGEPQPGL ESQGRAASMP RLAAETQHAP DASPMKRSIS
     TLAQRPHGVH LCSATLDRPA PSQATHHHHH RCHRRRDKKQ RSLEKGPSLS ADTDGAPNST
     AGPGLPPGDG PTGCRRERRR ERGRSQERRQ PSSSSSEKQR FYSCDRWGGR EPLPPRPSLS
     SHPTSPTAGQ GPGPHTQVSI TYKTAHSSPV HYGGAQTSLP AFSPGRLSRG LSEHNALLQR
     DTLSQPLAPG SRIGSDPNLG QRLDSEAADH PLPEDTLTFE EAVATNSGRS STATTVLWDS
     ARAAGHGTAT TTPTKTTGAS CAVIATPARS GTSHG
//
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