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Database: UniProt
Entry: A0A2I3H9V4_NOMLE
LinkDB: A0A2I3H9V4_NOMLE
Original site: A0A2I3H9V4_NOMLE 
ID   A0A2I3H9V4_NOMLE        Unreviewed;      2137 AA.
AC   A0A2I3H9V4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1G {ECO:0000313|Ensembl:ENSNLEP00000040256.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000040256.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000040256.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000040256.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. This channel gives rise to T-type calcium
CC       currents. T-type calcium channels belong to the "low-voltage activated
CC       (LVA)" group and are strongly blocked by nickel and mibefradil. A
CC       particularity of this type of channels is an opening at quite negative
CC       potentials, and a voltage-dependent inactivation. T-type channels serve
CC       pacemaking functions in both central neurons and cardiac nodal cells
CC       and support calcium signaling in secretory cells and vascular smooth
CC       muscle. They may also be involved in the modulation of firing patterns
CC       of neurons which is important for information processing as well as in
CC       cell growth processes. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR   EMBL; ADFV01070083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01070092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSNLET00000046590.1; ENSNLEP00000040256.1; ENSNLEG00000007757.3.
DR   GeneTree; ENSGT00940000159664; -.
DR   Proteomes; UP000001073; Chromosome 14.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005445; VDCC_T_a1.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF137; VOLTAGE-DEPENDENT T-TYPE CALCIUM CHANNEL SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW   Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602077-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022568, ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        813..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        889..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1225..1243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1263..1287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1358..1380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1460..1483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1558..1579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1591..1614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1668..1686
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1706..1723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1769..1791
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..380
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          769..918
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1223..1493
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1557..1801
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1818..1877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1955..2009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2040..2137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1492..1519
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        470..484
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1024
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1066
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         871
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1432
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ   SEQUENCE   2137 AA;  236259 MW;  ABA9BC3296AF3866 CRC64;
     MDEEEDGAGA EESGQPRRFM RLNDLSRAGG RPGPGSAEKD PGSADSEVEG LPYPALAPVV
     FLYLSQDSRP RRWCLRTVCN PYPSGTWFER ISMLVILLNC VTLGMFRPCE DIACDSQRCR
     ILQAFDDFIF AFFAVEMVVK MVALGIFGKK CYLGDTWNRL DFFIVIAGTV RVLRPLRAIN
     RVPSMRILVT LLLDTLPMLG NVLLLCFFVF FIFGIVGVQL WAGLPLSVDL ERYYQTENED
     ESPFICSQPR ENGMRSCRSV PTLRGEGGGG PPCGLDYEAY NSSSNTTCVN WNQYYTNCSA
     GEHNPFKGAI NFDNIGYAWI AIFQVITLEG WVDIMYFVMD AHSFYNFIYF ILLIIVGSFF
     MINLCLVVIA TQFSETKQRE SQLMREQRVR FLSNASTLAS FSEPGSCYEE LLKYLVYILR
     KAARRLAQVS RAAGVRAGLL SSPAPLGGQE TQPSSSCSRS HRRLSVHHLV HHHHHHHHHY
     HLGNGTLRAP RASPEIQDRD ANGSRRLMLP PPSTPALSGG PPGGAESVHS FYHADCHLEP
     VRCQAPPPRS PSEASGRTVG SGKVYPTVHT SPPPETLKEK ALVEVAASSG PPTLTSLNIP
     PGPYSSMHKL LETQSTGTCQ SSCKISSPCL KADSGACGPD SCPYCARAGA GEVELADREM
     PDSDSEAVYE FTQDAQHRDL RDPHSRRQRS LGPDAEPSSV LAFWRLICDT FRKIVDSKYF
     GRGIMIAILV NTLSMGIEYH EQVGVWAEAG LLVKVQGAQA ACPLCSVWEI VGQQGGGLSV
     LRTFRLMRVL KLVRFLPALQ RQLVVLMKTM DNVATFCMLL MLFIFIFSIL GMHLFGCKFA
     SERDGDTLPD RKNFDSLLWA IVTVFQILTQ EDWNKVLYNG MASTSSWAAL YFIALMTFGN
     YVLFNLLVAI LVEGFQAEEI SKREDASGQL SCIQLPVDSQ GGDANKSESE PDFFSPSLDG
     DGDRKKCLAL VSLGEHPELR KSLLPPLIIH TAATPMSLPK STSTGLGEAL GPASRRTSSS
     GSAEPGAAHE MKSPPSARSS PHSPWSAASS WTSRRSSRNS LGRAPSLKRR SPSGERRSLL
     SGEGQESQDE EESSEEERAS PAGSDRHHRG SLEREAKSSF DLPDTLQVPG LHRTASGRGS
     ASEHQDCNGK SASGRLARAL RPDDPPLDGD DADDEGNLSK GERVRAWIRA RLPACCLERD
     SWSAYIFPPQ SRFRLLCHRI ITHKMFDHVV LVIIFLNCIT IAMERPKIDP HSAERIFLTL
     SNYIFTAVFL AEMTVKVMGA GVGLAGILRS SWNVLDGLLV LISVIDILVS MVSDSGTKIL
     GMLRVLRLLR TLRPLRVISR AQGLKLVVET LMSSLKPIGN IVVICCAFFI IFGILGVQLF
     KGKFFVCQGE DTRNITNKSD CAEASYRWVR HKYNFDNLGQ ALMSLFVLAS KDGWVDIMYD
     GLDAVGVDQQ PIMNHNPWML LYFISFLLIV AFFVLNMFVG VVVENFHKCR QHQEEEEARR
     REEKRLRRLE KKRRNLMLDD VIASGSSASA ASEAQCKPYY SDYSRFRLLV HHLCTSHYLD
     LFITGVIGLN VVTMAMEHYQ QPQILDEALK ICNYIFTVIF VLESVFKLVA FGFRRFFQDR
     WNQLDLAIVL LSIMGITLEE IEVNASLPIN PTIIRIMRVL RIARVLKLLK MAVGMRALLD
     TVMQALPQVH RFYFFSSFPG GEPGTSLHVV FFIFAALGVE LFGDLVSWGR GVSTGDNWNW
     HYEGKGLGLD TLRDCDQEST CYNTVISPIY FVSFVLTAQF VLVNVVIAVL MKHLEESNKE
     AKEEAELEAE LELEMKTLSP QPHSPLGSPF LWPGVEGPDS PDSPKPGAPH PAAHARSASH
     FSLQHPTMQP HPTELPGPDL LTVRKSGVSR THSLPNDSYM CRHGSTAEGP LGHRGWGLPK
     AQSGSVLSVH SQPADTSYIL QLPKDAPHLL QPHSTPTWGT IPKLPPPGRS PLAQRPLRRQ
     AAIRTDSLDV QGLGSREDLL AEEPPSPRDL KKCYSVEAQS CQRRATSWLD EQRRHSIAVS
     CLDSGSQPHL GTDPSNLGGH RPKKKLSPPS ISIDPPESQG PRPLPSPGVC LRRRAPSSDS
     KEPLASGPPD SMAASPSPKK DVLSLSGLSS DPADLDP
//
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