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Q99244 (CAC1D_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Voltage-dependent L-type calcium channel subunit alpha-1D
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide isoform 2
Voltage-gated calcium channel subunit alpha Cav1.3
Gene names
Name:CACNA1D
Synonyms:CACH3, CACN4, CACNL1A2, CCHL1A2
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length1610 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).

Subunit structure

Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with RIMBP2. Interacts with CABP1 and CABP4, resulting in a near elimination of calcium-dependent inactivation of the channel By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in brain, heart and skeletal muscle.

Domain

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1D subfamily. [View classification]

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform HCA3A (identifier: Q99244-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform CACH3B (identifier: Q99244-3)

The sequence of this isoform is not available.
Isoform CACH3D (identifier: Q99244-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1261-1303: GYFSDAWNTFDSLIVIGSIIDVALSEADPTESESLPLPTATPG → HYFTDAWNTFDALIVVGSVVDIAITEVN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16101610Voltage-dependent L-type calcium channel subunit alpha-1D
PRO_0000053934

Regions

Topological domain1 – 125125Cytoplasmic Potential
Transmembrane126 – 14419Helical; Name=S1 of repeat I; Potential
Topological domain145 – 16218Extracellular Potential
Transmembrane163 – 18220Helical; Name=S2 of repeat I; Potential
Topological domain183 – 19412Cytoplasmic Potential
Transmembrane195 – 21319Helical; Name=S3 of repeat I; Potential
Topological domain214 – 23421Extracellular Potential
Transmembrane235 – 25319Helical; Name=S4 of repeat I; Potential
Topological domain254 – 27219Cytoplasmic Potential
Transmembrane273 – 29220Helical; Name=S5 of repeat I; Potential
Topological domain293 – 38088Extracellular Potential
Transmembrane381 – 40525Helical; Name=S6 of repeat I; Potential
Topological domain406 – 522117Cytoplasmic Potential
Transmembrane523 – 54220Helical; Name=S1 of repeat II; Potential
Topological domain543 – 55715Extracellular Potential
Transmembrane558 – 57619Helical; Name=S2 of repeat II; Potential
Topological domain577 – 5848Cytoplasmic Potential
Transmembrane585 – 60319Helical; Name=S3 of repeat II; Potential
Topological domain604 – 61310Extracellular Potential
Transmembrane614 – 63219Helical; Name=S4 of repeat II; Potential
Topological domain633 – 65119Cytoplasmic Potential
Transmembrane652 – 67221Helical; Name=S5 of repeat II; Potential
Topological domain673 – 72654Extracellular Potential
Transmembrane727 – 75125Helical; Name=S6 of repeat II; Potential
Topological domain752 – 884133Cytoplasmic Potential
Transmembrane885 – 90319Helical; Name=S1 of repeat III; Potential
Topological domain904 – 91916Extracellular Potential
Transmembrane920 – 93920Helical; Name=S2 of repeat III; Potential
Topological domain940 – 95112Cytoplasmic Potential
Transmembrane952 – 97019Helical; Name=S3 of repeat III; Potential
Topological domain971 – 9766Extracellular Potential
Transmembrane977 – 99620Helical; Name=S4 of repeat III; Potential
Topological domain997 – 101519Cytoplasmic Potential
Transmembrane1016 – 103520Helical; Name=S5 of repeat III; Potential
Topological domain1036 – 112590Extracellular Potential
Transmembrane1126 – 114621Helical; Name=S6 of repeat III; Potential
Topological domain1147 – 120357Cytoplasmic Potential
Transmembrane1204 – 122219Helical; Name=S1 of repeat IV; Potential
Topological domain1223 – 123715Extracellular Potential
Transmembrane1238 – 125720Helical; Name=S2 of repeat IV; Potential
Topological domain1258 – 12647Cytoplasmic Potential
Transmembrane1265 – 128622Helical; Name=S3 of repeat IV; Potential
Topological domain1287 – 131125Extracellular Potential
Transmembrane1312 – 133120Helical; Name=S4 of repeat IV; Potential
Topological domain1332 – 135019Cytoplasmic Potential
Transmembrane1351 – 137020Helical; Name=S5 of repeat IV; Potential
Topological domain1371 – 143767Extracellular Potential
Transmembrane1438 – 146225Helical; Name=S6 of repeat IV; Potential
Topological domain1463 – 1610148Cytoplasmic Potential
Repeat112 – 408297I
Repeat508 – 754247II
Repeat871 – 1153283III
Repeat1190 – 1465276IV
Calcium binding1491 – 150212 Potential
Region428 – 44518Binding to the beta subunit By similarity
Region1073 – 116391Dihydropyridine binding By similarity
Region1418 – 148467Dihydropyridine binding By similarity
Region1430 – 147344Phenylalkylamine binding By similarity
Compositional bias1 – 66Poly-Met
Compositional bias652 – 6587Poly-Leu
Compositional bias826 – 83611Poly-Glu

Sites

Site3631Calcium ion selectivity and permeability By similarity
Site7041Calcium ion selectivity and permeability By similarity
Site10991Calcium ion selectivity and permeability By similarity
Site14041Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue14731Phosphoserine; by PKA Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1261 – 130343GYFSD…TATPG → HYFTDAWNTFDALIVVGSVV DIAITEVN in isoform CACH3D.
VSP_000915

Sequences

Sequence LengthMass (Da)Tools
Isoform HCA3A [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: B3B2E3794D936F79

FASTA1,610182,328
        10         20         30         40         50         60 
MMMMMMKKMQ HQRQQQEDHA NEANYARGTR PPISGEGPTS QPNSSKQTVL SWQAAIDAAR 

        70         80         90        100        110        120 
QAKAAQTMST SAPPPVGSLS QRKRQQYAKS KKQGNSSNSR PARALFCLSL NNPIRRACIS 

       130        140        150        160        170        180 
IVEWKPFDIF ILLAIFANCV ALAIYIPFPE DDSNSTNHNL EKVEYAFLII FTVETFLKII 

       190        200        210        220        230        240 
AYGLLLHPNA YVRNGWNLLD FVIVIVGLFS VILEQLTKET EGGNHSSGKS GGFDVKALRA 

       250        260        270        280        290        300 
FRVLRPLRLV SGVPSLQVVL NSIIKAMVPL LHIALLVLFV IIIYAIIGLE LFIGKMHKTC 

       310        320        330        340        350        360 
FFADSDIVAE EDPAPCAFSG NGRQCAVNGT ECRSGWVGPN GGITNFDNFA FAMLTVFQCI 

       370        380        390        400        410        420 
TMEGWTDVLY WMNDAMGFEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD 

       430        440        450        460        470        480 
FQKLRENEQL EEDLKGYLDW ITQAEDIDPE NEEEGGEEGK RNTSMPTSET ESVNTENVSG 

       490        500        510        520        530        540 
EGETQGSCGS LCQAISKSKL SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS 

       550        560        570        580        590        600 
SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE 

       610        620        630        640        650        660 
TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA SLLNSMKSIA SLLLLLFLFI 

       670        680        690        700        710        720 
IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP 

       730        740        750        760        770        780 
SSSGMIVCIY FIILFICGNY ILLNVFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE 

       790        800        810        820        830        840 
SLENKKNNKP EVNQIANSDN KVTIDDYQEE TEDKDPYPPC DVPVGEEEEE EEEEPEVPAG 

       850        860        870        880        890        900 
PRPRRISELN MKEKIVPIPE GSAFFILSKT NPIRVGCHKL INHHIFTNLI LVFIMLSSAA 

       910        920        930        940        950        960 
LAAEDPIRSH SFRNTILGYF DYAFTAIFTV EILLKMTTFG AFLHKGAFCR NYFNLLDMLV 

       970        980        990       1000       1010       1020 
VGVSLVSFGI QSSAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVFVAI RTIGNIMIVT 

      1030       1040       1050       1060       1070       1080 
TLLQFMFACI GVQLFKGKFY RCTDEAKSNP EECRGLFILY KDGDVDSPVV RERIWQNSDF 

      1090       1100       1110       1120       1130       1140 
NFDNVLSAMM ALFTVSTFEG WPALLYKAID SNGENAGPVY NHRVEISIFF IIYIIIVAFF 

      1150       1160       1170       1180       1190       1200 
MMNIFVGFVI VTFQEQGEKE YKNCELDKNQ RQCVEYALKA RPLRRYIPKN PYQYKFWYVV 

      1210       1220       1230       1240       1250       1260 
NSSPFEYMMF VLIMLNTLCL AMQHYEQSKM FNDAMDILNM VFTGVFTVEM VLKVIAFKPK 

      1270       1280       1290       1300       1310       1320 
GYFSDAWNTF DSLIVIGSII DVALSEADPT ESESLPLPTA TPGNSEESNR ISITFFRLFR 

      1330       1340       1350       1360       1370       1380 
VMRLVKLLSR GEGIRTLLWT FIKSFQALPY VALLIAMLFF IYAVIGMQMF GKVAMRDNNQ 

      1390       1400       1410       1420       1430       1440 
INRNNNFQTF PQAVLLLFRC ATGEAWQEIM LACLPGKLCD PDSDYNPGEE YTCGSNFAIV 

      1450       1460       1470       1480       1490       1500 
YFISFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL DEFKRIWSEY DPEAKGRIKH 

      1510       1520       1530       1540       1550       1560 
LDVVTLLRRI QPPLGFGKLC PHRVACKRLV AMNMPLNSDG TVMFNATLFA LVRTALKIKT 

      1570       1580       1590       1600       1610 
EGNLEQANEE LRAVIKKIWK KTSMKLLDQV VPPAGGQCGL CFLSPSRSRS

« Hide

Isoform CACH3B (Sequence not available). ––
Isoform CACH3D [UniParc].

Checksum: BA9DAFC7D6974F0F
Show »

FASTA1,595180,941

References

[1]"Cloning of a novel alpha 1-subunit of the voltage-dependent calcium channel from the beta-cell."
Yaney G.C., Wheeler M.B., Wei X., Perez-Reyes E., Birnbaumer L., Boyd A.E. III, Moss L.G.
Mol. Endocrinol. 6:2143-2152(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HCA3A).
Tissue: Insulinoma.
[2]"Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes."
Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.
J. Biol. Chem. 265:20430-20436(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1146-1441 (ISOFORMS CACH3B AND CACH3D).
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M57969 mRNA. Translation: AAB59702.1.
M57970 mRNA. Translation: AAA62807.1.
PIRA46227.

3D structure databases

ProteinModelPortalQ99244.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG050763.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01636. LVDCCALPHA1D.
ProtoNetSearch...

Entry information

Entry nameCAC1D_MESAU
AccessionPrimary (citable) accession number: Q99244
Secondary accession number(s): Q99245
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: April 3, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents