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Database: UniProt
Entry: G3GUU3_CRIGR
LinkDB: G3GUU3_CRIGR
Original site: G3GUU3_CRIGR 
ID   G3GUU3_CRIGR            Unreviewed;      1969 AA.
AC   G3GUU3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 31.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=I79_001467 {ECO:0000313|EMBL:EGW00704.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW00704.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
RA   Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
RA   Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
RA   Quake S.R., Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
RT   line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in an
CC       opposit effects on the channel function.
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; JH000032; EGW00704.1; -; Genomic_DNA.
DR   InParanoid; G3GUU3; -.
DR   Proteomes; UP000001075; 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   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 6.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 6.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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:UP000001075};
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:UP000001075};
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     24     45       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     76       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    190    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    404    423       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    476    497       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    673    692       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    704    724       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    730    751       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    763    789       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    809    839       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    893    914       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    934    961       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1013   1033       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1045   1064       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1168   1191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1259   1283       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1417   1451       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      542    573       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1969 AA;  223182 MW;  58C8E38AD589F2FA CRC64;
     MPVTRQCPQH LGLLTFTPWE KVEYAFLIIF TVETFLKIIA YGLLLHPNAY VRNGWNLLDF
     VIVIVGLFSV ILEQLTKETE GGNHSSGKSG GFDVKALRAF RVLRPLRLVS GVPNIVAEED
     PAPCAFSGNG RQCTANGTEC RSGWVGPNGG ITNFDNFAFA MLTVFQCITM EGWTDVLYWM
     NDAMGFELPW VYFVSLVIFG SFFVLNLVLG VLSGEFSKER EKAKARGDFQ KLREKQQLEE
     DLKGYLDWIT QAEDIDPENE EEGGEEGKRN TSMPTSETES VNTENIMRHM APIRSLCVYQ
     CSLESAHIAN KVLLALFTCE MLVKMYSLGL QAYFVSLFNR FDCFVVCGGI TETILVELEL
     MSPLGVSVFR CVRLLRIFKV TRHWTSLSNL VASLLNSMKS IASLLLLLFL FIIIFSLLGM
     QLFGGKFNFD ETQTKRSTFD NFPQALLTVF QILTGEDWNA VMYDGIMAYG GPSSSGMIVC
     IYFIILFICG NCILWNYQDY VVPITALLSL NFPVVAMMVE AIGIFKLDIL LNVFLAIAVD
     NLADAESLNT AQKEEAEEKE RKKIARKESL ENKKNNKPEV NQIANSDNKV TIDDYQEETE
     DKDPYPPCDV PVGEEEEEEE DEPEVPAGPR PRRISELNMK EKIAPIPEGS AFFILSKTNP
     IRVGCHKLIN HHIFTNLILV FIMLSSAALA AEDPIRSHSF RNTILGYFDY AFTAIFTVEI
     LLKVLGYADY VFTGTFAFEI ILKMTTFGAF LHKGAFCRNY FNLLDMLVVG VSLVSFGIQS
     SAISVVKILR VLRVLRPLRA INRAKGLKHV VQCVFVAIRT IGNIMIVTTL LQFMFACIGV
     QLFKGKFYRC TDEAKSNPEE CRGLFILYKD GDVDSPVVRE RIWQNSDFNF DNVLSAMMAL
     FTVSTFEGWP ALLYKAIDSN GENVGPVYNY RVEISIFFII YIIIVAFFMM NIFVGFVIVT
     FQEQGEKEYK NCELDKNQRQ CVEYALKARP LRRYIPKNPY QYKFWYVVNS SPFEYMMFVL
     IMLNTLCLAM QHYEQSKMFN DAMDILNMVF TGVFTVEMVL KVIAFKPKGY FSDAWNTFDS
     LIVIGSIIDV ALSEADHYFT DAWNTFDALI VVGSVVDIAI TEVNNSEESN RISITFFRLF
     RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIAMLF FIYAVIGMQM FGKVAMRDNN
     QINRNNNFQT FPQAVLLLFR CATGEAWQEI MLACLPGKLC DPDSDYNPGE EYTCGSNFAI
     VYFISFYMLC AFLIINLFVA VIMDNFDYLT RDWSILGPHH LDEFKRIWSE YDPEAKGRIK
     HLDVVTLLRR IQPPLGFGKL CPHRVACKRL VAMNMPLNSD GTVMFNATLF ALVRTALKIK
     TEGNLEQANE ELRAVIKKIW KKTSMKLLDQ VVPPAGDDEV TVGKFYATFL IQDYFRKFKK
     RKEQGLVGKY PTKNTTIALQ AGLRTLHDIG PEIRRAISCD LQDDEPEDSK ADEEDVFKRN
     GALLGNHVNH VNSDRRDSLQ QTNTTHRPLH VQRPSIPPAS DTEKPLFPPA GNSVCHNHHN
     HNSIGKQVPT STNANLNNAN MSKAAHGKRP SIGSLEHVSE NGHYSYKHDR ELQRRSGIKR
     SESGDEQLPT ICREDPETHG YFRDPHCLGE QEYFSSEECC EDDSSPTWSR QNYSYYNRYP
     GSSMDFERPR GYHHPQGFLE DDDSPIGYDS QRSPRRRLLP PTPPSHRRSS FNFECLRRQS
     SQEDILPSPA LPHRAALPLH LMQQQIMAVA GLDSSKAQKY SPSHSTRSWA TPPATPPYRD
     WTPCYTPLIQ VDRSESLDQV NGSLPSLHRS SWYTDEPDIS YRTFTPASLT VPSSFRNKNS
     DKQRSADSLV EAVLISEGLG RYARDPKFVS ATKHEIADAC DLTIDEMESA ASTLLNGSVC
     PRANGDMGPI SHRQDYELQD FGPGYSDEEP DPGREEEDLA DEMICITTL
//
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