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Database: UniProt
Entry: L5JVS7_PTEAL
LinkDB: L5JVS7_PTEAL
Original site: L5JVS7_PTEAL 
ID   L5JVS7_PTEAL            Unreviewed;      1686 AA.
AC   L5JVS7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 22.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=PAL_GLEAN10001453 {ECO:0000313|EMBL:ELK03415.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera;
OC   Pteropodidae; Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03415.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y.,
RA   Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y.,
RA   Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G.,
RA   Wang L.F., Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 339:456-460(2013).
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; KB031088; ELK03415.1; -; Genomic_DNA.
DR   InParanoid; L5JVS7; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF234; PTHR10037:SF234; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
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:UP000010552};
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:UP000010552};
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     71     88       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    108    127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    139    155       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    212    235       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    275    296       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    308    330       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    493    512       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    555    578       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    642    660       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    680    700       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    712    738       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    758    784       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    872    899       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    950    971       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    983   1002       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1148   1171       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1271   1305       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED     1328   1358       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ELK03415.1}.
SQ   SEQUENCE   1686 AA;  189938 MW;  AB17E941DB1AC114 CRC64;
     KRRTQHSKHK TVAAASAQRS PRALFCLTLA NPLRRSCISI VEWKHPGRPR ADLRGCSAWV
     LDYVYLRPFD ILILLTIFAN CVALGVYIPF PEDDSNTANH NLEQVEYVFL VIFTVETVLK
     IVAYGLVLHP SAYIRNGWNL LDFIIVVVGL FSVLLEQGPG RPGDAPHTGG KPGGFDVKAL
     RAFRVLRPLR LVSGVPSLHI VLNSIMKALV PLLHIALLVL FVIIIYAIIG LELFLGRMHK
     TCYFLGSGRV CTLNQTECRG RWAGPNGGIT NFDNFFFAML TVFQCVTMEG WTDVLYWMQD
     AMGYELPWVY FVSLVIFGSF FVLNLVLGVL SGEFSKEREK AKARGDFQKL REKQQLEEDL
     RGYLDWIMQA EELDIEDPSA DDNFCSVAEE GRAGHQYANK VLLCLFTVEM LLKLYGLGPS
     AYVSSFFNRF DCFVVCGGIL ETTLVEVGAM QPLGISVLRC VRLLRIFKVT RHWASLSNLV
     ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDQ THTKRSTFDT FPQALLTVFQ
     ILTGEDWNVV MYDGIMAYGG PFFPGMLVCI YFIILFICGN CMEEEEEEEE EEEEGGAGRV
     ELLQEVVPKE KVVPIPEGSA FFCLSQTNSL RKACHTLIHH HVFTNLILVF IILSSVSLAA
     EDPIRAHSFR NHILGYFDYA FTSIFTVEIL LKMTVFGAFL HQGSFCRSWF NLLDLLVVSV
     SLISFGIHSS AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVFVAIRTI GNIMIVTTLL
     QFMFACIGVQ LFKPVCNIHR GSFLVYPDGD VSRPLVRERL WVNSDFNFDN VLSAMMALFT
     VSTFEGWPAL LYKAIDAHAE DEGPIYNYHV EISVFFIVYI IIIAFFMMNI FVGFVIITFR
     AQGEQEYQNC ELDKNQRQCV EYALKAQPLR RYIPKNPHQY RVWATVNSAA FEYLMFLLIL
     LNTVALAMQH YEQTAPFNYA MDILNMVFTG LFTIEMVLKI IAFKPKHYFA DAWNTFDALI
     VVGSVVDIAV TEVNSSEDSS RISITFFRLF RVMRLVKLLS KGEGIRTLLW TFIKSFQMFG
     KVALQDGTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ATLPGNRCDP ESDFGPGEEF
     TCGSNFAIAY FISFFMLCAF LIINLFVAVI MDNFDYLTRD WSILGPHHLD EFKRIWSEYD
     PGAKGRIKHL DVVALLRRIQ PPLGFGKLCP HRVACKRLVA MNMPLNSDGT VTFNATLFAL
     VRTSLKIKTE EEEVTVGKFY ATFLIQDYFR KFRRRKEKGL LGTEAPPSTS SALQAGLRSL
     QDLGPEIRQA LTCDTDQEEE EEKEEEEERQ EGEEEEDKDP ETYKAPIGFQ PPSRRRSSVI
     SLSLPAGDKL PDSLSLGPSD DDGGAPNSRQ FSVPQAGSHT HRRSSGALIF TIPEERSSQP
     KGTEEEEKQD EEEEVPSQFS DLNMLSYLDE QAGTPLHPIL LPPHRPQRYV GGHRVPHRRL
     LPPTPAGRKP SFTIQCLRRQ SSCEDLPIPG TYHRGRNSGL SRTQGSWATP PQRGRLLYAP
     LLLVEEGTAG EGYLGKSSGP LRTFTCLHVP GTHSDPSHVK RGSADSLVEA VLISEGLGLF
     ARDPHFVALA KQEIADACRL TLDEMDSAAS DLLAQGTSSF YSDEESIRSR FDEEDLRDEM
     ACIHGL
//
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