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Database: UniProt
Entry: W5KSJ5_ASTMX
LinkDB: W5KSJ5_ASTMX
Original site: W5KSJ5_ASTMX 
ID   W5KSJ5_ASTMX            Unreviewed;      2332 AA.
AC   W5KSJ5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   28-MAR-2018, entry version 26.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Characidae incertae sedis; Astyanax clade;
OC   Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000010557, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Ensembl:ENSAMXP00000010557, ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000010557};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAMXP00000010557}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2014) 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. This channel gives
CC       rise to T-type calcium currents. T-type calcium channels belong to
CC       the "low-voltage activated (LVA)" group and are strongly blocked
CC       by nickel and mibefradil. A particularity of this type of channels
CC       is an opening at quite negative potentials, and a voltage-
CC       dependent inactivation. T-type channels serve pacemaking functions
CC       in both central neurons and cardiac nodal cells and support
CC       calcium signaling in secretory cells and vascular smooth muscle.
CC       They may also be involved in the modulation of firing patterns of
CC       neurons which is important for information processing as well as
CC       in cell growth processes. {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; APWO01115945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APWO01115954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSAMXT00000010557; ENSAMXP00000010557; ENSAMXG00000009755.
DR   GeneTree; ENSGT00830000128242; -.
DR   OMA; FWRLICD; -.
DR   OrthoDB; EOG091G02L1; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0070509; P:calcium ion import; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005445; VDCC_T_a1.
DR   InterPro; IPR030154; VDCC_T_a1G.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF137; PTHR10037:SF137; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
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:UP000018467};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   2332       Voltage-dependent T-type calcium channel
FT                                subunit alpha. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004865479.
FT   TRANSMEM     47     67       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    138    161       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    263    284       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    290    315       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    677    695       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    707    728       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    798    817       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    874    897       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1215   1233       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1253   1274       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1286   1305       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1453   1476       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1550   1567       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1587   1606       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1685   1709       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1721   1739       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1769   1790       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        4    326       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      676    903       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1213   1486       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1550   1801       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED     1485   1512       {ECO:0000256|SAM:Coils}.
FT   COILED     1791   1814       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2332 AA;  261531 MW;  E03BE4BDDBD240A5 CRC64;
     MVCNPWFERA SMLVILLNCV TLGMFHPCED SDCDSERCKI LEDFDDFIFA FFAIEMVIKM
     VALGIFGKKC YLGDTWNRLD FFIVLAGMLE YSLNLQNVSF SAVRTVRVLR PLRAINRVPS
     MRILVTLLLD TLPMLGNVLL LCFFVFFIFG IVGVQLWAGL LRNRCFLPEN FSLPQTLDLH
     TYYHTENDDE SPFICSQPRE NGMRQCSSIP MLLEETVQCH LDMGAYNTTD NTTCVNWNQY
     YTNCSAGEVN PFKGAINFDN IGYAWIAIFQ VITLEGWVDI MYFVMDAHSF YNFIYFILLI
     IVGSFFMINL CLVVIATQFS ETKQRESQLM KEQRVRFMSN ASTLASFSEP GSCYDELLKY
     LVYIVRKGTR QLGHLVRAAA RRAGLRVRAS PVLEPPNTKR QRQKQRQGSI HHLVHHHHHH
     HHHHYHLGNG SIRSDRTREL EMYNRAGAGS GRLTLPSITP LPDPSSNPCP AALSPGSAES
     IHSVYHTACH LEPLHCNPSP GPSALQAYKR NSVPFAAPAH KNYPTLQPCL PLEHLRQRSL
     EPGGASCTTS ALTSLNIPPN PTNTSQCLLD PQGPAALFLL CLVHSICYNA RTILAFDPET
     CPYCTKAAAN DSEGTEANET ADSDSEGVYE FTQDAHYRDN RDPNKKRKFK LGARAAKVVH
     FWRLVCDTFR KIVDSKYFGR GIMIAILINT LSMGIEYHEQ PEELTNALEI SNIVFTSLFA
     LEMLLKLLVY GPFGYIKNPY NIFDGIIVVI SVWEIVGQQG GGLSVLRTFR LMRVLKLVRF
     MPALQRQLVV LMKTMDNVAT FCMLLMLFIF IFSILGMHLF GCKFGSERDG DTLPDRKNFD
     SLLWAIVTVF QILTQEDWNK VLYNGMASTS PVAALYFIAL MTFGNYVLFN LLVAILVEGF
     QTEEITKRED LHGQLSCIQL PIDSGGDASK SDSEADFYAR SIDDDQNVKI CVTVICLGSQ
     NYYKKSIAQS ILFIFIIFNL KIETTTKYSI GPISEYSYEP TSPALSCCYL QSSARSSPHA
     PWSSGSSWNS RRSSWNSLGR APSLKRQKHQ SGERRSLLSG DGQSSSDEDG GRVGGGASEG
     DDASLSRTDS FGQRPRHRRM ESLETRSSFD LPPDALQVPY LHRSASIHST RPPNLLSNGK
     SSPTGATTQL SLDDHHSEDD NPDEEGNLSR RARLYRWFER KQPEWCRQRG TWSLYLFPPE
     SKFRVTCNKI ITHKMFDHVV LVIIFLNCIT IAMERPRIES RSAERIFLTL SNYIFTAIFV
     TEMTIKVVAL GWCFGEKCYL KSSWNILDGM LVMISVIDIL VSLISNSGTK ILGMLRVLRL
     LRTLRPLRYM SPCVGWEKEI NTLISCLGNK RGVCVCVCFT FYNLYSVLRV KLFKGKFFVC
     QGEDIRNITN KSDCLLAKYK WVRHKYNFDN LGQALMSLFV LASKDGWVDI MYDGLDAVGV
     DQQPIMNYNP WMLLYFISFL LIVAFFVLNM FVGVVVENFH KCRRHQEAEE AKRREEKRLK
     RMEKKRRNIM MTGVSWPSPE GGVTVEAQSK PYYSDYSPTR RLIHKMCTSH YLDLFITIVI
     GLNVITMSME HYQQPRVLDE ALKICNYIFT VIFVLESVFK LVAFGFRRFF KDRWNQLDLA
     IVLLSIMGIT LEEIEVNASL PINPTIIRIM RVLRIARVLK LLKMAVGMRA LLDTVIQALP
     QVGNLGLLFM LLFFIFAALG VELFGDLICD ELHPCEGLGR YATFKNFGMA FLLLFRVSTG
     DNWNGIMKDT LRDCAQETGT CYNTVVSPIY FVSFVLTAQF VLVNVVIAVL MKHLEESNKE
     AKEEADMEAE LELEAVVIGD IVGPRGSPWI SRGSQDRGYP TDSPPADIRR DSAAHIKTDP
     PLRRPMFDSV SLVIQGSLEG ELSLMDNLSD SICHYYALPP LPSKHSTDKQ IPLAEMEALS
     LASEKSWSLA LTDDSVPDDF NPPLLTSLEC NINTDPHEPL EEHLLCVKKT TVGRTHSLPN
     DSYMFLPLQD TVNTSTTLTT SVQQAQSGSS GSVNFHTEDP SQHLTVPTEL FRPISPHSLS
     DSESIPRIPP PRRHTFSRTL RRQVAVSADS QEALNVEGGE SEGSASAELS APPANCPAPL
     QRQQHRPSLL LVPATPGASP KASRSSVHTQ HNPYDQYSVS SRCPRSPPPP PLPSHLSRSA
     KPSGYGGGGL PTDSRGPCLR QLKKHHSADA QGHRVPLLPR PSSWLDDPRR HSIEVCSSVE
     SSPQRSSASS GFVSRAGSLQ TSQPSPHARK KKMSPPCISV DPPEALSLGT VAPPPLPSRD
     TCLRRRAPSS DSKDSFDLGG SGGGDGLPQE GVPNPKLLTL PSFSFEKSSS EH
//
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