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Protein

Voltage-dependent L-type calcium channel subunit alpha-1D

Gene

Cacna1d

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei364Calcium ion selectivity and permeabilityBy similarity1
Sitei763Calcium ion selectivity and permeabilityBy similarity1
Sitei1160Calcium ion selectivity and permeabilityBy similarity1
Sitei1450Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1537 – 1548Sequence analysisAdd BLAST12

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • high voltage-gated calcium channel activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • PDZ domain binding Source: RGD
  • voltage-gated calcium channel activity Source: BHF-UCL
  • voltage-gated calcium channel activity involved in cardiac muscle cell action potential Source: BHF-UCL

GO - Biological processi

  • aging Source: RGD
  • calcium ion import Source: RGD
  • calcium ion transport Source: BHF-UCL
  • calcium-mediated signaling Source: RGD
  • divalent metal ion transport Source: RGD
  • heart development Source: RGD
  • membrane depolarization during action potential Source: GO_Central
  • membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
  • memory Source: RGD
  • positive regulation of CREB transcription factor activity Source: RGD
  • regulation of calcium ion transport Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.

Protein family/group databases

TCDBi1.A.1.11.1. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1D
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 2
Rat brain class D
Short name:
RBD
Voltage-gated calcium channel subunit alpha Cav1.3
Gene namesi
Name:Cacna1d
Synonyms:Cach3, Cacn4, Cacnl1a2, Cchl1a2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70973. Cacna1d.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 126CytoplasmicSequence analysisAdd BLAST126
Transmembranei127 – 145Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini146 – 163ExtracellularSequence analysisAdd BLAST18
Transmembranei164 – 183Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini184 – 195CytoplasmicSequence analysisAdd BLAST12
Transmembranei196 – 214Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini215 – 235ExtracellularSequence analysisAdd BLAST21
Transmembranei236 – 254Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini255 – 273CytoplasmicSequence analysisAdd BLAST19
Transmembranei274 – 293Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini294 – 381ExtracellularSequence analysisAdd BLAST88
Transmembranei382 – 406Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini407 – 582CytoplasmicSequence analysisAdd BLAST176
Transmembranei583 – 602Helical; Name=S1 of repeat IISequence analysisAdd BLAST20
Topological domaini603 – 617ExtracellularSequence analysisAdd BLAST15
Transmembranei618 – 636Helical; Name=S2 of repeat IISequence analysisAdd BLAST19
Topological domaini637 – 644CytoplasmicSequence analysis8
Transmembranei645 – 663Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini664 – 673ExtracellularSequence analysis10
Transmembranei674 – 692Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini693 – 711CytoplasmicSequence analysisAdd BLAST19
Transmembranei712 – 732Helical; Name=S5 of repeat IISequence analysisAdd BLAST21
Topological domaini733 – 786ExtracellularSequence analysisAdd BLAST54
Transmembranei787 – 811Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini812 – 945CytoplasmicSequence analysisAdd BLAST134
Transmembranei946 – 964Helical; Name=S1 of repeat IIISequence analysisAdd BLAST19
Topological domaini965 – 980ExtracellularSequence analysisAdd BLAST16
Transmembranei981 – 1000Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1001 – 1012CytoplasmicSequence analysisAdd BLAST12
Transmembranei1013 – 1031Helical; Name=S3 of repeat IIISequence analysisAdd BLAST19
Topological domaini1032 – 1037ExtracellularSequence analysis6
Transmembranei1038 – 1057Helical; Name=S4 of repeat IIISequence analysisAdd BLAST20
Topological domaini1058 – 1076CytoplasmicSequence analysisAdd BLAST19
Transmembranei1077 – 1096Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1097 – 1186ExtracellularSequence analysisAdd BLAST90
Transmembranei1187 – 1207Helical; Name=S6 of repeat IIISequence analysisAdd BLAST21
Topological domaini1208 – 1264CytoplasmicSequence analysisAdd BLAST57
Transmembranei1265 – 1283Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1284 – 1298ExtracellularSequence analysisAdd BLAST15
Transmembranei1299 – 1318Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1319 – 1325CytoplasmicSequence analysis7
Transmembranei1326 – 1347Helical; Name=S3 of repeat IVSequence analysisAdd BLAST22
Topological domaini1348 – 1357ExtracellularSequence analysis10
Transmembranei1358 – 1377Helical; Name=S4 of repeat IVSequence analysisAdd BLAST20
Topological domaini1378 – 1396CytoplasmicSequence analysisAdd BLAST19
Transmembranei1397 – 1416Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1417 – 1483ExtracellularSequence analysisAdd BLAST67
Transmembranei1484 – 1508Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1509 – 2203CytoplasmicSequence analysisAdd BLAST695

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • dendrite Source: RGD
  • dendrite membrane Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • sarcolemma Source: RGD
  • voltage-gated calcium channel complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1656 – 1657IQ → AA: Loss of calcium-dependent inactivation related to the C-terminal lobe of calmodulin. 1 Publication2

Chemistry databases

ChEMBLiCHEMBL4132.
GuidetoPHARMACOLOGYi530.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539361 – 2203Voltage-dependent L-type calcium channel subunit alpha-1DAdd BLAST2203

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Glycosylationi329N-linked (GlcNAc...)Sequence analysis1
Modified residuei469PhosphoserineBy similarity1
Modified residuei473PhosphoserineBy similarity1
Modified residuei1519Phosphoserine; by PKASequence analysis1
Modified residuei1743PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP27732.
PRIDEiP27732.

PTM databases

iPTMnetiP27732.
PhosphoSitePlusiP27732.

Expressioni

Tissue specificityi

Expressed in brain, pancreatic islets and B-lymphocytes.1 Publication

Interactioni

Subunit structurei

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 CABP1 and CABP4, resulting in a near elimination of calcium-dependent inactivation of the channel. Interacts with RIMBP2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Gabbr2O888716EBI-8072674,EBI-7090239

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • PDZ domain binding Source: RGD

Protein-protein interaction databases

DIPiDIP-60740N.
IntActiP27732. 2 interactors.
MINTiMINT-7965882.
STRINGi10116.ENSRNOP00000051407.

Chemistry databases

BindingDBiP27732.

Structurei

3D structure databases

ProteinModelPortaliP27732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati112 – 408IAdd BLAST297
Repeati528 – 774IIAdd BLAST247
Repeati892 – 1174IIIAdd BLAST283
Repeati1211 – 1486IVAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni429 – 446Binding to the beta subunitBy similarityAdd BLAST18
Regioni1134 – 1224Dihydropyridine bindingBy similarityAdd BLAST91
Regioni1464 – 1530Dihydropyridine bindingBy similarityAdd BLAST67
Regioni1476 – 1519Phenylalkylamine bindingBy similarityAdd BLAST44

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 7Poly-Met7
Compositional biasi712 – 718Poly-Leu7
Compositional biasi886 – 897Poly-GluAdd BLAST12

Domaini

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 similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiP27732.
KOiK04851.
PhylomeDBiP27732.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF139. PTHR10037:SF139. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16885. CAC1F_C. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01636. LVDCCALPHA1D.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (13)i

Sequence statusi: Complete.

This entry describes 13 isoformsi produced by alternative splicing. AlignAdd to basket

Note: The region sequenced in isoforms ROB3 and RKC5 is identical to CACN4.
Isoform 1 (identifier: P27732-1) [UniParc]FASTAAdd to basket
Also known as: CACN4A

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.

« Hide

        10         20         30         40         50
MMMMMMMKKM QHQRQQQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV
60 70 80 90 100
LSWQAAIDAA RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS
110 120 130 140 150
RPARALFCLS LNNPIRRACI SIVDWKPFDI FILLAIFANC VALAIYIPFP
160 170 180 190 200
EDDSNSTNHN LEKVEYAFLI IFTVETFLKI IASGLLLHPN ASVRNGWNLL
210 220 230 240 250
DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR AFRVLRPLRL
260 270 280 290 300
VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
310 320 330 340 350
CFFADSDIVA EEDPAPCAFS GNGRQCAANG TECRSGWVGP NGGITNFDNF
360 370 380 390 400
AFAMLTVFQC ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL
410 420 430 440 450
VLGVLSGEFS KEREKAKARG DFQKLREKQQ LEEDLKGYLD WITQAEDIDP
460 470 480 490 500
ENEEEGGEEG KRNTSMPTSE TESVNTENVS GEGETQGCCG SLWCWWKRRG
510 520 530 540 550
AAKTGPSGCR RWGQAISKSK LRSHGAREAL CVCRCSLESL VKLWTSRFSA
560 570 580 590 600
HLQAAYVRPY SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS
610 620 630 640 650
SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD
660 670 680 690 700
CFVVCGGITE TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA
710 720 730 740 750
SLLNSMKSIA SLLLLLFLFI IIFSLLGMQL FGGKFNFDET QTKRSTFDNF
760 770 780 790 800
PQALLTVFQI LTGEDWNAVM YDGIMAYGGP SSSGMIVCIY FIILFICGNY
810 820 830 840 850
ILLKLFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE SLENKKNNKP
860 870 880 890 900
EVNQIANSDN KVTIDDYQEE AEDKDPYPPC DVPVGEEEEE EEEDEPEVPA
910 920 930 940 950
GPRPRRISEL NMKEKIAPIP EGSAFFILSK TNPIRVGCHK LINHHIFTNL
960 970 980 990 1000
ILVFIMLSSA ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF
1010 1020 1030 1040 1050
GAFLHKGAFC RNYFNLLDML VVGVSLVSFG IQSSAISVVK ILRVLRVLRP
1060 1070 1080 1090 1100
LRAINRAKGL KHVVQCVFVA IRTIGNIMIV TTLLQFMFAC IGVQLFKGKF
1110 1120 1130 1140 1150
YRCTDEAKSN PEECRGLFIL YKDGDVDSPV VRERIWQNSD FNFDNVLSAM
1160 1170 1180 1190 1200
MALFTVSTFE GWPALLYKAI DSNGENVGPV YNYRVEISIF FIIYIIIVAF
1210 1220 1230 1240 1250
FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK
1260 1270 1280 1290 1300
NPYQYKFWYV VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN
1310 1320 1330 1340 1350
MVFTGVFTVE MVLKVIAFKP KGYFSDAWNT FDSLIVIGSI IDVALSEADN
1360 1370 1380 1390 1400
SEESNRISIT FFRLFRVMRL VKLLSRGEGI RTLLWTFIKS FQALPYVALL
1410 1420 1430 1440 1450
IAMLFFIYAV IGMQMFGKVA MRDNNQINRN NNFQTFPQAV LLLFRCATGE
1460 1470 1480 1490 1500
AWQEIMLACL PGKLCDPDSD YNPGEEYTCG SNFAIVYFIS FYMLCAFLII
1510 1520 1530 1540 1550
NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV
1560 1570 1580 1590 1600
TLLRRIQPPL GFGKLCPHRV ACKRLVAMNM PLNSDGTVMF NATLFALVRT
1610 1620 1630 1640 1650
ALKIKTEGNL EQANEELRAV IKKIWKKTSM KLLDQVVPPA GDDEVTVGKF
1660 1670 1680 1690 1700
YATFLIQDYF RKFKKRKEQG LVGKYPAKNT TIALQAGLRT LHDIGPEIRR
1710 1720 1730 1740 1750
AISCDLQDDE PEDSKPEEED VFKRNGALLG NYVNHVNSDR RESLQQTNTT
1760 1770 1780 1790 1800
HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG KQVPTSTNAN
1810 1820 1830 1840 1850
LNNANMSKAA HGKRPSIGDL EHVSENGHYS YKHDRELQRR SSIKRTRYYE
1860 1870 1880 1890 1900
TYIRSESGDE QLPTIFREDP EIHGYFRDPR CFGEQEYFSS EECCEDDSSP
1910 1920 1930 1940 1950
TWSRQNYSYY NRYPGSSMDF ERPRGYHHPQ GFLEDDDSPI GYDSRRSPRR
1960 1970 1980 1990 2000
RLLPPTPPSH RRSSFNFECL RRQNSQDDVL PSPALPHRAA LPLHLMQQQI
2010 2020 2030 2040 2050
MAVAGLDSSK AQKYSPSHST RSWATPPATP PYRDWTPCYT PLIQVDRSES
2060 2070 2080 2090 2100
MDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
2110 2120 2130 2140 2150
DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN
2160 2170 2180 2190 2200
GSVCPRANGD MGPISHRQDY ELQDFGPGYS DEEPDPGREE EDLADEMICI

TTL
Length:2,203
Mass (Da):250,136
Last modified:July 15, 1999 - v2
Checksum:i8E746A8D988050C6
GO
Isoform 2 (identifier: P27732-2) [UniParc]FASTAAdd to basket
Also known as: CACN4B

The sequence of this isoform differs from the canonical sequence as follows:
     1642-1668: DDEVTVGKFYATFLIQDYFRKFKKRKE → GNSRSGKSKAWWGNTLRRTPRSPYRRD
     1669-2203: Missing.

Show »
Length:1,668
Mass (Da):189,438
Checksum:iC0B994698B1EEA77
GO
Isoform 3 (identifier: P27732-3) [UniParc]FASTAAdd to basket
Also known as: CACH3A, RB48, RBD-55

The sequence of this isoform differs from the canonical sequence as follows:
     1349-1349: D → DPSDSENIPLPTATPG

Show »
Length:2,218
Mass (Da):251,614
Checksum:iF76CD9838B0DD9BB
GO
Isoform 4 (identifier: P27732-4) [UniParc]FASTAAdd to basket
Also known as: Delta-IV-S3, RKC6

The sequence of this isoform differs from the canonical sequence as follows:
     1322-1349: Missing.

Show »
Length:2,175
Mass (Da):247,135
Checksum:i3BB7746587D5E475
GO
Isoform 5 (identifier: P27732-5) [UniParc]FASTAAdd to basket
Also known as: Delta-IV-S4

The sequence of this isoform differs from the canonical sequence as follows:
     1354-1368: Missing.

Show »
Length:2,188
Mass (Da):248,267
Checksum:i7036D5421C98E89D
GO
Isoform 6 (identifier: P27732-6) [UniParc]FASTAAdd to basket
Also known as: RB9

The sequence of this isoform differs from the canonical sequence as follows:
     1322-1348: GYFSDAWNTFDSLIVIGSIIDVALSEA → HYFTDAWNTFDALIVVGSVVDIAITEVN
     1349-1349: D → DPSDSENIPLPTATPG

Show »
Length:2,219
Mass (Da):251,820
Checksum:i1720A717CCD314D0
GO
Isoform 7 (identifier: P27732-7) [UniParc]FASTAAdd to basket
Also known as: RB11

The sequence of this isoform differs from the canonical sequence as follows:
     493-512: Missing.

Show »
Length:2,183
Mass (Da):247,705
Checksum:iACA674F99711ECC7
GO
Isoform 8 (identifier: P27732-8) [UniParc]FASTAAdd to basket
Also known as: RB34

The sequence of this isoform differs from the canonical sequence as follows:
     481-492: Missing.

Show »
Length:2,191
Mass (Da):249,014
Checksum:iF928E1B53FAD29FF
GO
Isoform 9 (identifier: P27732-9) [UniParc]FASTAAdd to basket
Also known as: RH1

The sequence of this isoform differs from the canonical sequence as follows:
     1322-1392: Missing.

Show »
Length:2,132
Mass (Da):241,962
Checksum:iB0E7A0FBBB1B582A
GO
Isoform 10 (identifier: P27732-10) [UniParc]FASTAAdd to basket
Also known as: RH2

The sequence of this isoform differs from the canonical sequence as follows:
     1322-1349: Missing.
     1354-1368: Missing.

Show »
Length:2,160
Mass (Da):245,266
Checksum:i8CD4F488BCAB9E28
GO
Isoform 11 (identifier: P27732-13)
Also known as: RKC5
Sequence is not available
Length:
Mass (Da):
Isoform 12 (identifier: P27732-14)
Also known as: ROB3
Sequence is not available
Length:
Mass (Da):
Isoform 13 (identifier: P27732-12) [UniParc]FASTAAdd to basket
Also known as: Truncated

The sequence of this isoform differs from the canonical sequence as follows:
     1686-1691: AGLRTL → MLERML
     1692-2203: Missing.

Show »
Length:1,691
Mass (Da):192,179
Checksum:iBF6F15F872E7F40B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti124D → N in AAA42015 (PubMed:1648940).Curated1
Sequence conflicti183S → Y in AAA42015 (PubMed:1648940).Curated1
Sequence conflicti192S → Y in AAA42015 (PubMed:1648940).Curated1
Sequence conflicti513G → C (PubMed:1648940).Curated1
Sequence conflicti522 – 560Missing (PubMed:1648940).CuratedAdd BLAST39
Sequence conflicti1452W → R in AAA89156 (PubMed:7479909).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000916481 – 492Missing in isoform 8. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_000917493 – 512Missing in isoform 7. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_0009181322 – 1392Missing in isoform 9. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_0009191322 – 1349Missing in isoform 4 and isoform 10. 2 PublicationsAdd BLAST28
Alternative sequenceiVSP_0009201322 – 1348GYFSD…ALSEA → HYFTDAWNTFDALIVVGSVV DIAITEVN in isoform 6. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_0009211349D → DPSDSENIPLPTATPG in isoform 6 and isoform 3. 2 Publications1
Alternative sequenceiVSP_0009221354 – 1368Missing in isoform 10 and isoform 5. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_0009231642 – 1668DDEVT…KKRKE → GNSRSGKSKAWWGNTLRRTP RSPYRRD in isoform 2. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_0009241669 – 2203Missing in isoform 2. 1 PublicationAdd BLAST535
Alternative sequenceiVSP_0009251686 – 1691AGLRTL → MLERML in isoform 13. 1 Publication6
Alternative sequenceiVSP_0009261692 – 2203Missing in isoform 13. 1 PublicationAdd BLAST512

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38101 mRNA. Translation: BAA07282.1.
D38102 mRNA. Translation: BAA07283.1.
M57682 mRNA. Translation: AAA42015.1.
U14005 Genomic DNA. Translation: AAB60515.1.
M99221 mRNA. Translation: AAA40895.1.
U31772 mRNA. Translation: AAA89156.1.
U49126 mRNA. Translation: AAB61634.1.
U49127 mRNA. Translation: AAB61635.1.
U49128 mRNA. Translation: AAB61636.1.
PIRiJH0422.
T42742.
RefSeqiNP_058994.1. NM_017298.1. [P27732-1]
UniGeneiRn.89671.

Genome annotation databases

GeneIDi29716.
KEGGirno:29716.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38101 mRNA. Translation: BAA07282.1.
D38102 mRNA. Translation: BAA07283.1.
M57682 mRNA. Translation: AAA42015.1.
U14005 Genomic DNA. Translation: AAB60515.1.
M99221 mRNA. Translation: AAA40895.1.
U31772 mRNA. Translation: AAA89156.1.
U49126 mRNA. Translation: AAB61634.1.
U49127 mRNA. Translation: AAB61635.1.
U49128 mRNA. Translation: AAB61636.1.
PIRiJH0422.
T42742.
RefSeqiNP_058994.1. NM_017298.1. [P27732-1]
UniGeneiRn.89671.

3D structure databases

ProteinModelPortaliP27732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60740N.
IntActiP27732. 2 interactors.
MINTiMINT-7965882.
STRINGi10116.ENSRNOP00000051407.

Chemistry databases

BindingDBiP27732.
ChEMBLiCHEMBL4132.
GuidetoPHARMACOLOGYi530.

Protein family/group databases

TCDBi1.A.1.11.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiP27732.
PhosphoSitePlusiP27732.

Proteomic databases

PaxDbiP27732.
PRIDEiP27732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29716.
KEGGirno:29716.

Organism-specific databases

CTDi776.
RGDi70973. Cacna1d.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiP27732.
KOiK04851.
PhylomeDBiP27732.

Enzyme and pathway databases

ReactomeiR-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.

Miscellaneous databases

PROiP27732.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF139. PTHR10037:SF139. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16885. CAC1F_C. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01636. LVDCCALPHA1D.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1D_RAT
AccessioniPrimary (citable) accession number: P27732
Secondary accession number(s): O09022
, O09023, O09024, Q01542, Q62691, Q62815, Q63491, Q63492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.