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Database: UniProt
Entry: H0W390_CAVPO
LinkDB: H0W390_CAVPO
Original site: H0W390_CAVPO 
ID   H0W390_CAVPO            Unreviewed;      1844 AA.
AC   H0W390;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   22-NOV-2017, entry version 42.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1S {ECO:0000313|Ensembl:ENSCPOP00000017435};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000017435};
RN   [1] {ECO:0000313|Ensembl:ENSCPOP00000017435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000017435};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000017435}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000017435};
RG   Ensembl;
RL   Submitted (JAN-2012) 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-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}.
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:ENSCPOP00000017435}.
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DR   EMBL; AAKN02017958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003474895.1; XM_003474847.3.
DR   STRING; 10141.ENSCPOP00000017435; -.
DR   Ensembl; ENSCPOT00000026293; ENSCPOP00000017435; ENSCPOG00000024686.
DR   GeneID; 100734741; -.
DR   CTD; 779; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; H0W390; -.
DR   OMA; ACSYGKL; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000005447; 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; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
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   Complete proteome {ECO:0000313|Proteomes:UP000005447};
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:UP000005447};
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}.
SQ   SEQUENCE   1844 AA;  208988 MW;  DE289E7ABE5F0863 CRC64;
     MEPSSPQDES LKKKQPKKPV PEILPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT
     IFANCVALAI YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFIIV FLGVFTVILE QVNIIQSNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE
     KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
     VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
     EDLRGYMSWI TQGEVMDVED LREGKLSLDE TGSDTESLYE IEGLNKIIQF IRHWRQWNRV
     FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDVANRV LLTLFTIEML
     MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE LLLVQSGAMT PLGISVLRCI RLLRIFKITK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWNSVM YNGIMAYGGP TYPGMLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PEKSEEEKST IAKKLEQKPK GEGIPTTAKL
     KVDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRAESTRNQ ILGYFDIAFT
     SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFFSCNDL
     SKMTEEECKG SYYVYKDGDP TQIELRPRQW LHNDFHFDNV LSAMMSLFTV STFEGWPQLL
     YKAIDANEED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
     NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
     EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
     IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIAMVDGTQI NRNNNFQTFP QAVLLLFRCA
     TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LIINLFVAVI
     MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
     HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
     TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTVQIQAGLR
     TIEEEAAPEI HRTISGDLTA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP
     VMANQRPLQF TEIEMEELES PVFLEDFPHD SRTNPLARAN ANNANANVAR GNSNHSNSQA
     FSSVHYEREF PEETPAARGG GPSSPSSDNK SLVEKLRGQQ AQRVMRRGQT LPAPCQVTGQ
     RPGGKFHEGL WQGKGPSSMA GSLHEETHRS RSSQEGAARC QAPATTLLIQ EALVRGGLGS
     LAADANFVMA TGQALADACQ MEPEEVEVAA TELLKERQSP AGTA
//
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