CAC1H_RAT
ID CAC1H_RAT Reviewed; 2359 AA.
AC Q9EQ60;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1H;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.2;
GN Name=Cacna1h;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11073957; DOI=10.1074/jbc.m008215200;
RA McRory J.E., Santi C.M., Hamming K.S.C., Mezeyova J., Sutton K.G.,
RA Baillie D.L., Stea A., Snutch T.P.;
RT "Molecular and functional characterization of a family of rat brain T-type
RT calcium channels.";
RL J. Biol. Chem. 276:3999-4011(2001).
RN [2]
RP SEQUENCE REVISION TO 105; 874; 877; 1409 AND 2321.
RA Snutch T.P., McRory J.E., Hamming K.S.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type
CC calcium currents. T-type calcium channels belong to the 'low-voltage
CC activated (LVA)' group. A particularity of this type of channel is an
CC opening at quite negative potentials, and a voltage-dependent
CC inactivation (PubMed:11073957). T-type channels serve pacemaking
CC functions in both central neurons and cardiac nodal cells and support
CC calcium signaling in secretory cells and vascular smooth muscle
CC (Probable). They may also be involved in the modulation of firing
CC patterns of neurons. In the adrenal zona glomerulosa, participates in
CC the signaling pathway leading to aldosterone production in response to
CC either AGT/angiotensin II, or hyperkalemia (By similarity).
CC {ECO:0000250|UniProtKB:O95180, ECO:0000269|PubMed:11073957,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts (via N-terminal cytoplasmic domain) with STAC.
CC {ECO:0000250|UniProtKB:O95180}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11073957};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O95180}.
CC Note=Interaction with STAC increases expression at the cell membrane.
CC {ECO:0000250|UniProtKB:O95180}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11073957}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: In response to raising of intracellular calcium, the T-type
CC channels are activated by CaM-kinase II.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1H subfamily. {ECO:0000305}.
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DR EMBL; AF290213; AAG35187.2; -; mRNA.
DR RefSeq; NP_722521.1; NM_153814.2.
DR AlphaFoldDB; Q9EQ60; -.
DR SMR; Q9EQ60; -.
DR STRING; 10116.ENSRNOP00000042239; -.
DR BindingDB; Q9EQ60; -.
DR ChEMBL; CHEMBL5134; -.
DR DrugCentral; Q9EQ60; -.
DR GuidetoPHARMACOLOGY; 536; -.
DR CarbonylDB; Q9EQ60; -.
DR GlyGen; Q9EQ60; 3 sites.
DR PhosphoSitePlus; Q9EQ60; -.
DR PaxDb; Q9EQ60; -.
DR GeneID; 114862; -.
DR KEGG; rno:114862; -.
DR UCSC; RGD:68943; rat.
DR CTD; 8912; -.
DR RGD; 68943; Cacna1h.
DR eggNOG; KOG2302; Eukaryota.
DR InParanoid; Q9EQ60; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9EQ60; -.
DR PRO; PR:Q9EQ60; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IC:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; ISO:RGD.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0032342; P:aldosterone biosynthetic process; IMP:UniProtKB.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0035865; P:cellular response to potassium ion; ISO:RGD.
DR GO; GO:0034651; P:cortisol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0106134; P:positive regulation of cardiac muscle cell contraction; IMP:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel; Zinc.
FT CHAIN 1..2359
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1H"
FT /id="PRO_0000053956"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..119
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..160
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..184
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..212
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..419
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..824
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..846
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 847..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..871
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..903
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..935
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..987
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1012
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1302..1324
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1325..1342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1343..1363
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1364..1373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1374..1393
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1394..1407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1408..1429
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1430..1439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1440..1463
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1464..1540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1541..1566
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1567..1621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1622..1642
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1643..1656
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1657..1678
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1679..1685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1686..1704
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1705..1718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1719..1742
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1743..1756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1757..1777
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1778..1840
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1841..1868
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1869..2359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 87..422
FT /note="I"
FT REPEAT 776..1015
FT /note="II"
FT REPEAT 1292..1569
FT /note="III"
FT REPEAT 1607..1868
FT /note="IV"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1974..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2016..2258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2335..2359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..535
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2016..2030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2167..2190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 378
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 971
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1515
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1813
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2359 AA; 261113 MW; 6E708FA1D8E3765E CRC64;
MTEGTLAADE VRVPLGASPP APAAPVRASP ASPGAPGREE QGGSGSGVLA PESPGTECGA
DLGADEEQPV PYPALAATVF FCLGQTTRPR SWCLRLVCNP WFEHISMLVI MLNCVTLGMF
RPCEDVECRS ERCSILEAFD DFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVM
AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV
FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ
KCSHIPSRRE LRVQCTLGWE AYGQPQAEDG GAGRNACINW NQYYNVCRSG EFNPHNGAIN
FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIMGSFFM INLCLVVIAT
QFSETKQREN QLMREQRARY LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA
RWQSRWRKKV DPSSTVHGQG PGRRPRRAGR RTASVHHLVY HHHHHHHHHY HFSHGGPRRP
SPEPGAGDNR LVRACAPPSP PSPGHGPPDS ESVHSIYHAD CHVEGPQERA RVAHSIATAA
SLKLASGLGT MNYPTILPSG TVNSKGGTSS RPKGLRGAGA PGAAVHSPLS LGSPRPYEKI
QDVVGEQGLG RASSHLSGLS VPCPLPSPQA GTLTCELKSC PYCASALEDP EFEFSGSESG
DSDAHGVYEF TQDVRHGDCR DPVQQPHEVG TPGHSNERRR TPLRKASQPG GIGHLWASFS
GKLRRIVDSK YFNRGIMAAI LVNTLSMGVE YHEQPEELTN ALEISNIVFT SMFALEMLLK
LLACGPLGYI RNPYNIFDGI VVVISVWEIV GQANGGLSVL RTFRLLRVLK LVRFLPALRR
QLVVLMRTMD NVATFCMLLM LFIFIFSILG MHLFGCKFSL KTDSGDTVPD RKNFDSLLWA
IVTVFQILTQ EDWNVVLYNG MASTSSWAAL YFVALMTFGN YVLFNLLVAI LVEGFQAEGD
ATRSDTDEDK TSTQLEGDFD KLRDLRATEM KMYSLAVTPN GHLEGRGSLP PPLITHTAAT
PMPTPKSSPN LDVAHALLDS RRSSSGSVDP QLGDQKSLAS LRSSPCTPWG PNSAGSSRRS
SWNSLGRAPS LKRRNQCGER ESLLSGEGKG STDDEAEDSR PSTGTHPGAS PGPRATPLRR
AESLDHRSTL DLCPPRPAAL LPTKFHDCNG QMVALPSEFF LRIDSHKEDA AEFDDDIEDS
CCFRLHKVLE PYAPQWCRSR ESWALYLFPP QNRLRVSCQK VIAHKMFDHV VLVFIFLNCI
TIALERPDID PGSTERAFLS VSNYIFTAIF VVEMMVKVVA LGLLWGEHAY LQSSWNVLDG
LLVLVSLVDI IVAMASAGGA KILGVLRVLR LLRTLRPLRV ISRAPGLKLV VETLISSLRP
IGNIVLICCA FFIIFGILGV QLFKGKFYYC EGTDTRNITT KAECHAAHYR WVRRKYNFDN
LGQALMSLFV LSSKDGWVNI MYDGLDAVGI DQQPVQNHNP WMLLYFISFL LIVSFFVLNM
FVGVVVENFH KCRQHQEAEE ARRREEKRLR RLERRRRKAQ RRPYYADYSH TRRSIHSLCT
SHYLDLFITF IICLNVITMS MEHYNQPKSL DEALKYCNYV FTIVFVFEAA LKLVAFGFRR
FFKDRWNQLD LAIVLLSIMG IALEEIEMNA ALPINPTIIR IMRVLRIARV LKLLKMATGM
RALLDTVVQA LPQVGNLGLL FMLLFFIYAA LGVELFGRLE CSEDNPCEGL SRHATFTNFG
MAFLTLFRVS TGDNWNGIMK DTLRECTRED KHCLSYLPAL SPVYFVTFML VAQFVLVNVV
VAVLMKHLEE SNKEAREDAE MDAEIELEMA QGSTAQPPPT AQESQGTQPD TPNLLVVRKV
SVSRMLSLPN DSYMFRPVAP AAAPHSHPLQ EVEMETYTGP VTSAHSPPLE PRASFQVPSA
ASSPARVSDP LCALSPRGTP RSLSLSRILC RQEAMHSESL EGKVDDVGGD SIPDYTEPAE
NMSTSQASTG APRSPPCSPR PASVRTRKHT FGQRCISSRP PTLGGDEAEA ADPADEEVSH
ITSSAHPWPA TEPHSPEASP TASPVKGTMG SGRDPRRFCS VDAQSFLDKP GRPDAQRWSS
VELDNGESHL ESGEVRGRAS ELEPALGSRR KKKMSPPCIS IEPPTKDEGS SRPPAAEGGN
TTLRRRTPSC EAALHRDCPE PTEGPGTGGD PVAKGERWGQ ASCRAEHLTV PNFAFEPLDM
GGPGGDCFLD SDQSVTPEPR VSSLGAIVPL ILETELSMPS GDCPEKEQGL YLTVPQTPLK
KPGSTPATPA PDDSGDEPV
