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Database: UniProt
Entry: H3AD80_LATCH
LinkDB: H3AD80_LATCH
Original site: H3AD80_LATCH 
ID   H3AD80_LATCH            Unreviewed;      2282 AA.
AC   H3AD80;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   28-MAR-2018, entry version 37.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1G {ECO:0000313|Ensembl:ENSLACP00000007601};
OS   Latimeria chalumnae (West Indian ocean coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007601, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Ensembl:ENSLACP00000007601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000007601};
RX   PubMed=9215903;
RA   Zardoya R., Meyer A.;
RT   "The complete DNA sequence of the mitochondrial genome of a 'living
RT   fossil,' the coelacanth (Latimeria chalumnae).";
RL   Genetics 146:995-1010(1997).
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000007601}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-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. 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; AFYH01103837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01103845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000007601; -.
DR   Ensembl; ENSLACT00000007665; ENSLACP00000007601; ENSLACG00000006736.
DR   eggNOG; KOG2302; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
DR   InParanoid; H3AD80; -.
DR   OMA; FWRLICD; -.
DR   OrthoDB; EOG091G02L1; -.
DR   TreeFam; TF313555; -.
DR   Proteomes; UP000008672; 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:UP000008672};
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:UP000008672};
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   TRANSMEM      7     27       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     99    122       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    224    245       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    251    276       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    660    681       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    751    770       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    827    850       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1167   1185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1238   1257       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1302   1324       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1404   1427       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1501   1522       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1534   1557       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1635   1655       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1667   1687       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1718   1739       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    287       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      629    857       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1165   1437       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1500   1750       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED     1436   1463       {ECO:0000256|SAM:Coils}.
FT   COILED     1740   1763       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2282 AA;  257097 MW;  7B24039219507ADE CRC64;
     IFQAFDDFIF TFFAVEMIVK MIALGIFGKK CYLGDTWNRL DFFIVVAGML EYSLNLQNVS
     LSAVRTVRVL RPLRAINRVP SMRILVTLLL DTLPMLGNVL LLCFFVFFIF GIVGVQLWAG
     LLRNRCFLPE NFTIPTLLEV KKYYHTENDD ENPFICSQPR DNGMRFCRDV PAFREEGLKC
     ILGQDSYNST DNTTCVNWNQ YYTNCSAGDH NPFKGAINFD NIGYAWIAIF QVITLEGWVD
     IMYFVMDAHS FYNFIYFILL IIVGSFFMIN LCLVVIATQF SETKQRESQL MKEQRVRFMS
     NASTLASFSE PGSCYDELLK YLVHVARKAR RQIAQLYNGV VSNMGLKASI VVKSGVDRQT
     HKRQRRKKAS VHHLIHHHHH HHHHYHMGNG SLRAPRASPE ISDVETSSLH NGTNRLMLPS
     PMPHLHPPPN NGSGNTESVH SIYHADCHFE PIRCKSSLTS LGLGVLSPEG LQKNVTSKNY
     PTVHATTPQE MLKEKMLGDN AANSGGSTLT NLNIPPGPYN SMHKLLETQS TGPCKGSCKL
     TSQCGKPENM TCNPESCPYC VRTLNNDSEV TDNETLDSDS EGVYEFTQDA HYSDQRDPQR
     SKPKVKKKNK VLEFWKLVCE TFHKIVDSKY FGRGIMIAIL INTLSMGIEY HEQPEELTNA
     LEISNIVFTS LFALEMLLKV LVYGPFGYIK NPYNIFDGII VVISVWEIVG QQGGGLSVLR
     TFRLMRVLKL VRFMPALQRQ LVVLMKTMDN VATFCMLLML FIFIFSILGM HLFGCKFASE
     RDGDTLPDRK NFDSLLWAIV TVFQILTQED WNKVLYNGMA STSPWAALYF IALMTFGNYV
     LFNLLVAILV EGFQTEEVSK REDVSGQLSC IQLPVDSSVG DASKSDSEAD FFSQSLEDEC
     GSKKDLSNSA LVPLNGHVDL KNSLTPPVIT HTAATPMPIP KSAICDSAHG YESRRGSSVS
     IDPNFYELKS PSSARSSPYA PWSTASSWNS RRSSWNSTGR ASSLKRKNQT GERKSLLSGD
     GKESSEEGEL SEEERSSRAC STNGSIHQHM ESLETKGSFD LPDTLQVPYL YRSPSMHSSH
     MSTSERQDCN GKTSPVAMLH QFYMDEQRNE FEGNDDEANM SKWARIQAWI KTHQPDWCKE
     RETWSLFLFP PQSKFRVTCN KIITHRMFDH IILFIIFLSC ITIAMERPSI EPHSAERIFL
     TLSNYIFTVI FLTEMTVKVV AMGWCFGEQV YLKSSWNILD GLLVMISVID ILVSMVSDSD
     TKILGMLRVL RLLRTLRPLR VISRAPGLKL VVETLMSSLK PIGNIVVICC AFFIIFGILG
     VQLFKGKFFI CQGEDTRNIT NKSDCLQANY KWIRHKYNFD NLGQALMSLF VLASKDGWVD
     IMYDGLDAVG VDQQPIMNYN PWMLLYFISF LLIVAFFVLN MFVGVVVENF HKCRQHQEAE
     EAKRREEKRL RRLEKKRRNI MLDHVISDSS VSVMTEAQCK PYYSDYSPTR FLIHKMCTSH
     YLDLFITVVI GLNVITMAME HYQQSKVLDK ALKICNYIFT IIFVLESVFK LVAFGFRRFF
     KDRWNQLDLA IVLLSIMGIT LEEIEVNASL PINPTIIRIM RVLRIARVLK LLKMAVGMRA
     LLDTVIQALP QVGNLGLLFM LLFFIFAALG VELFGDLKCD EDHPCEGLGR HATFGNFGMA
     FLTLFRVSTG DNWNGIMKDT LRDCGQETTC YNTIVSPIYF ISFVLTAQFV LVNVVIAVLM
     KHLEESNKEA KEEAEMEAEL ELELKNIDST PLNADTLVWA GEDLGDRADS PGMQNDPAYA
     KVDSPLSLDF PVERHLFDTV SLLIQGSLEG ELKLMDNLSG SVCHHYSLSP SDRCTSEKQI
     PLAEMEALSL TSDILSEKSW SLALTDDSFP DDTNTLLLNT LESNIIPYLN QSTEPEKYLL
     SVRKPSVSRT HSLPNDSYMF QSVDEVNSSG ERASSYQKSQ SGSTISVQSQ PAETSNLLQV
     PTDLFRPISP HSKLDSENIP KIPPPRQSPS AQRMLRRQVA IRNDSLDAVY ADSKENVQTH
     TKELPDFSIV AGPIVQPSSL LAPVTPRVLP EHEQSTVYIQ QHSQNQSNLP SCSSLSRNPS
     QELPADPVDQ EVFQINSSTE SNSSCGGSLN LKDLKKCYSV DSQGHLAKPP SWLDDQRRHS
     IEICSSVENS PQHHSTSSLG FNSQVISEVD SFQMARQKKK MSPPCISIDP PDGHELLTRG
     SHGLSSPSTE TCLRRRAPSC DSKDSVDLGD PLLPESTSTS PTAKRDLLTL PNFSFEKAEA
     DH
//
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