ID A0A0F8BCZ1_LARCR Unreviewed; 1427 AA.
AC A0A0F8BCZ1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN ORFNames=EH28_05264 {ECO:0000313|EMBL:KKF31724.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF31724.1};
RN [1] {ECO:0000313|EMBL:KKF31724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSNF {ECO:0000313|EMBL:KKF31724.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KKF31724.1};
RX PubMed=25835551;
RA Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL PLoS Genet. 11:E1005118-E1005118(2015).
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; KQ041009; KKF31724.1; -; Genomic_DNA.
DR RefSeq; XP_019110578.1; XM_019255033.1.
DR eggNOG; KOG2302; Eukaryota.
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; -; 3.
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:SF209; 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; 3.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01629; TVDCCALPHA1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 3.
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};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
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 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 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1069..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1107..1128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1140..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1202..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1303..1327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..331
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 519..747
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1067..1337
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 388..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1427 AA; 161423 MW; B45A13D1FAFE7329 CRC64;
MVILLNCVTL GMYQPCENID CSSDRCQILQ AFDAFIYIFF ALEMVIKMVA RGIFGQRCYL
GDTWNRLDFF IVMAGMVEYS LDLQNVNFTA IRTVRVLRPL RAINRVPSMR ILVNLLLDTL
PMLGNVLLLC FFVFFIFGII GVQLWAGLLR NRCYPEENFT RDTGIRLPRP YYMADEDDER
PFICSLPVDN GIMSCSDVPA RREGGRMCCL DKDDALYRQS LGLSPEPLAN GTDRVAGLCV
NWNRYYTRCH TGYSNPHKGA INFDNIAYAW IVIFQVITLE GWVEIMYYVM DAHSFYNFIY
FILLIIVGSF FMINLCLVVI ATQFSETKQR EHQLMQKQRA ECSSNSTMAS EPGDCYEELF
QLVCHVLRKA RRKTVALFNT LRGKPRGFRG VGRGRGGGEG RERKANGRGG RERRAMRRHG
APCPHHNKPD HASPMALTTA SATDGCPQCA AALSLTDGVG PVHSTNDEAE EGAVEETDRE
GEHCSSKEKD KKGQKNQKKS CKDVWHDIRM KLWGIVESKY FNRGIMIAIL INTISMGIEH
HEQPEELTNV LEICNIVFTS MFSLEMILKI TAFGSFSYLR NPYNVFDGII VIISVCEIVG
QSDGGLSVLR TFRLLRVLKL VRFMPALRRQ LVVLMKTMDN VATFCMLLML FIFIFSILGM
HIFGCKFSLR TETGDTVPDR KNFDSLLWAI VTVFQILTQE DWNVVLYNGM AATSPIAALY
FVALMTFGNY VLFNLLVAIL VEGFQAEGDA NRSYSDDDRS SSNFDESEKH DSIKLSDPRI
CTLTPNGHLE LGALSGSRGS YSSERRSFTI ESRKSSVMSL GKSSLERRSL SLRHGRSPNY
HNWGRPFPPQ SAWSRRSSSN SLGRRSYGFG GAPIVGGSLR VHSTRSPHSY PYAAEQESLL
SHSSHSHHPL HPHHPPPPPS FFSRHFAVRR DRRALSLELP ELHRAGGQPP GLPPVHLDSG
RRSGSGAGGS ITGGSGAGSG LGVDHRDCNG KTPGPHTQLM AEVFPHVSAR KDRADLDEET
DYSLCFRIQK MMEVYKPDWC ESREEWSVYL FSPQNKFRLL CQSIIAHKLF DYVVLAFIFL
NCITVALERP KILQGSLERV FLTISNYIFT AIFVAEMTVK VVSMGLYLGE KAYLRSSWNI
LDGFLVFVSL IDIVVSMAGG AKILGVLRVL RLLRTLRPLR VISRAPGLKL VVETLITSLK
PIGNIVLICC AFFIIFGILG VQLFKGKFYY CVGFDVKNIT NKSECLAANY RWVHHKYNFD
NLGQALMSLF VLASKDGWVN IMYHGLDAVG IDKQPMINNN PWMLLYFISF LLIVSFFVLN
MFVGVVVENF HKCRQHQEVE EARRREEKRQ RRMEKKRRKA QKLPYYASYG PARLAIHTLC
TSHYLDLVIT FIICINVITM SLEHYNQPQV TTLLAGDGRA VWVWVLE
//
