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Database: UniProt
Entry: A0A091CTZ0_FUKDA
LinkDB: A0A091CTZ0_FUKDA
Original site: A0A091CTZ0_FUKDA 
ID   A0A091CTZ0_FUKDA        Unreviewed;      2216 AA.
AC   A0A091CTZ0;
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 N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=H920_17079 {ECO:0000313|EMBL:KFO21438.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Bathyergidae; Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21438.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO21438.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO21438.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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; KN124375; KFO21438.1; -; Genomic_DNA.
DR   Proteomes; UP000028990; 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:SF161; PTHR10037:SF161; 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; 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:UP000028990};
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:UP000028990};
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    193    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    303    325       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    454    474       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    480    497       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    579    601       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    657    679       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1033   1051       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1071   1091       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1103   1121       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1164   1186       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1276   1301       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1357   1375       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1387   1410       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1422   1446       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1467   1496       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1565   1588       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1604   1639       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      682    708       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2216 AA;  248355 MW;  EDC3F181855193CD CRC64;
     MILATIIANC IVLALEQHLP DGDKTPMSER LDDTEPYFIG IFCFEAGIKI IALGFVFHKG
     SYLRNGWNVM DFVVVLTGCV PTELTAEGCW MLLLGGCQGH GSDRVDRFLF PDIASSKQMD
     SGCGYQDPGL GAVRTLTGLR DLVKQLWILA TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ
     VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH KACFPNSTDA DPVGDFPCGK
     DAPARLCEGD TECREYWPGP NFGITNFDNI LFAILTVFQC ITMEGWTDIL YNTNDAAGNT
     WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE
     WIFKAEEVML AEEDENAEEK SPLDVLKRAA TKKSRSDLIH AEEGDDRFTD LCAVGSPFTR
     TSLKSGKTES SSYFRRKEKM FRFFIRRMVK AQSFYWVVLC VVALNTLCVA MVHYNQPQRL
     TTALYFAEFV FLGLFLTEMS LKMYGLGPRS YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT
     SFGISVLRAL RLLRIFKVTK YWNSLRNLVV SLLNSMKSII SLLFLLFLFI VVFALLGMQL
     FGGQFNFKDE TPTTNFDTFP AAILTVFQIL TGEDWNAVMY HGIESQGGVS RGMFSSFYFI
     VLTLFGNYTL LNVFLAIAVD NLANAQELTK DEEEMEEAAN QKLALQKAKE VAEVSPISAA
     NISIAAFVKQ TRGTVSRSSS VSSVNSPRQQ NSARARSVWE QRASQLRLQN LRASCEALYS
     EMDPEERLRY ATSRHLRPDM KTHLDRPLVV EPSRDGPRGP TSGKARPEAT ESTEALDPPR
     RHHRHRDRDK APTTLPSARL KEAESGEEPG RRHRARHKAP PMQEAVEKEG EAPEGDKEVR
     NHQPKDPHSD LEAGGVMGMD PVLTLPSTCL QKVEEQPEDA DNQRNVTRMG SQPSDPSTTE
     HAPVTLTGPA GETTAVPSGN VDLESQAEGK KEVEADDVLR SGPRPIVPYS SMFCLSPTNL
     LRRFCHYIVT MRYFEMVILV VIALSSIALA AEDPVQTDSS RNNALKYMDY IFTGVFTFEM
     VIKMIDLGLL LHPGAYFRDL WNILDFVVVS GALVAFAFSG SKGKDISTIK SLRVLRVLRP
     LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV IAVQLFKGKF FYCTDESKEL
     ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL FTVSTGEGWP MVLKHSVDAT
     YEEQGPSPGF RMELSIFYVV YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA
     CIDFAISAKP LTRYMPQNRQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
     YELMLKCLNI VFTSMFSMEC VLKIIAFGVL NYFRDAWNVF DFVTVLGSIT DILVTEIANN
     FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
     FGNIALDDDT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLSNRAC DPNANASECG
     SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
     CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
     TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
     FDFYKQNKTT RDQIHQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSSTSL
     SNGGAIQTQE SGIKESVSWG TQRTQEALYE ARAPLERGHS AEIPVGQRGT LAVDVQMQSM
     ALRDPDGEPQ PGLESQGRAA SMPRLAAETQ PVPDASPMKR SISTLAQRPH GAHLCNAALD
     RLPPSQVPHH HHHRCHRRRD KKQRSLEKGP GLSADTDGAP NSTPGPGLPP GEGPAGCRHE
     RKQGRGRSQE RRQPSSSSSE KQRFYSCDRF GGREPPQPKS SISSHPTSPT AGPEPAPPPQ
     GGGTVHGSPL LSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPVHF AGAQSGLPAF
     SPGRLSRGLS EHNALLQRDP LSQPLAPSSR IGSDPYLGQR LDSEASAHTL PEDTLTFEEA
     MATNSGRSSR TSYVSSLTSQ SHPLRRVPNG YHCTLGLSAG GRARHSYHHP DQDHWC
//
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