Q01668 (CAC1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2161 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 (via IQ domain) with CABP1 and CABP4 in a calcium independent manner By similarity. Interacts with RIMBP2 By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in pancreatic islets and in brain, where it has been seen in cerebral cortex, hippocampus, basal ganglia, habenula and thalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in skeletal muscle. Ref.4
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.
Polymorphism	A change from seven to eight ATG trinucleotide repeats, resulting in an additional N-terminal methionine, has been found in a patient with non-insulin-dependent diabetes mellitus (NIDDM).
Involvement in disease	Sinoatrial node dysfunction and deafness (SANDD) [MIM:614896]: A disease characterized by congenital severe to profound deafness without vestibular dysfunction, associated with episodic syncope due to intermittent pronounced bradycardia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1D subfamily. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Deafness Disease mutation
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome calcium ion import Inferred from direct assay Ref.1. Source: BHF-UCL energy reserve metabolic process Traceable author statement. Source: Reactome membrane repolarization involved in regulation of SA node cell action potential Inferred from mutant phenotype Ref.6. Source: BHF-UCL positive regulation of calcium ion transport Inferred from direct assay Ref.1. Source: BHF-UCL regulation of atrial cardiac muscle cell membrane repolarization Inferred from sequence or structural similarity. Source: BHF-UCL regulation of heart rate by cardiac conduction Inferred from mutant phenotype Ref.6. Source: BHF-UCL regulation of insulin secretion Traceable author statement. Source: Reactome regulation of potassium ion transmembrane transporter activity Inferred from sequence or structural similarity. Source: BHF-UCL sensory perception of sound Inferred from mutant phenotype Ref.6. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Z disc Inferred from sequence or structural similarity. Source: BHF-UCL voltage-gated calcium channel complex Inferred from direct assay PubMed 11160515. Source: UniProtKB
Molecular_function	ankyrin binding Inferred from sequence or structural similarity PubMed 21859974. Source: BHF-UCL high voltage-gated calcium channel activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated calcium channel activity involved in regulation of SA node cell action potential Inferred from mutant phenotype Ref.6. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform Neuronal-type (identifier: Q01668-1)

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 Beta-cell-type (identifier: Q01668-2)

The sequence of this isoform differs from the canonical sequence as follows:
     373-392: MNDAMGFELPWVYFVSLVIF → VNDAIGWEWPWVYFVSLIIL
     493-493: C → WCWWRRRGAAKAGPSGCRRWG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2161	2161	Voltage-dependent L-type calcium channel subunit alpha-1D		PRO_0000053933
Regions
	Topological domain	1 – 126	126	Cytoplasmic Potential
	Transmembrane	127 – 145	19	Helical; Name=S1 of repeat I; Potential
	Topological domain	146 – 163	18	Extracellular Potential
	Transmembrane	164 – 183	20	Helical; Name=S2 of repeat I; Potential
	Topological domain	184 – 195	12	Cytoplasmic Potential
	Transmembrane	196 – 214	19	Helical; Name=S3 of repeat I; Potential
	Topological domain	215 – 235	21	Extracellular Potential
	Transmembrane	236 – 254	19	Helical; Name=S4 of repeat I; Potential
	Topological domain	255 – 273	19	Cytoplasmic Potential
	Transmembrane	274 – 293	20	Helical; Name=S5 of repeat I; Potential
	Topological domain	294 – 381	88	Extracellular Potential
	Transmembrane	382 – 406	25	Helical; Name=S6 of repeat I; Potential
	Topological domain	407 – 523	117	Cytoplasmic Potential
	Transmembrane	524 – 543	20	Helical; Name=S1 of repeat II; Potential
	Topological domain	544 – 558	15	Extracellular Potential
	Transmembrane	559 – 577	19	Helical; Name=S2 of repeat II; Potential
	Topological domain	578 – 585	8	Cytoplasmic Potential
	Transmembrane	586 – 604	19	Helical; Name=S3 of repeat II; Potential
	Topological domain	605 – 614	10	Extracellular Potential
	Transmembrane	615 – 633	19	Helical; Name=S4 of repeat II; Potential
	Topological domain	634 – 652	19	Cytoplasmic Potential
	Transmembrane	653 – 673	21	Helical; Name=S5 of repeat II; Potential
	Topological domain	674 – 727	54	Extracellular Potential
	Transmembrane	728 – 752	25	Helical; Name=S6 of repeat II; Potential
	Topological domain	753 – 886	134	Cytoplasmic Potential
	Transmembrane	887 – 905	19	Helical; Name=S1 of repeat III; Potential
	Topological domain	906 – 921	16	Extracellular Potential
	Transmembrane	922 – 941	20	Helical; Name=S2 of repeat III; Potential
	Topological domain	942 – 953	12	Cytoplasmic Potential
	Transmembrane	954 – 972	19	Helical; Name=S3 of repeat III; Potential
	Topological domain	973 – 978	6	Extracellular Potential
	Transmembrane	979 – 998	20	Helical; Name=S4 of repeat III; Potential
	Topological domain	999 – 1017	19	Cytoplasmic Potential
	Transmembrane	1018 – 1037	20	Helical; Name=S5 of repeat III; Potential
	Topological domain	1038 – 1127	90	Extracellular Potential
	Transmembrane	1128 – 1148	21	Helical; Name=S6 of repeat III; Potential
	Topological domain	1149 – 1205	57	Cytoplasmic Potential
	Transmembrane	1206 – 1224	19	Helical; Name=S1 of repeat IV; Potential
	Topological domain	1225 – 1239	15	Extracellular Potential
	Transmembrane	1240 – 1259	20	Helical; Name=S2 of repeat IV; Potential
	Topological domain	1260 – 1266	7	Cytoplasmic Potential
	Transmembrane	1267 – 1288	22	Helical; Name=S3 of repeat IV; Potential
	Topological domain	1289 – 1313	25	Extracellular Potential
	Transmembrane	1314 – 1333	20	Helical; Name=S4 of repeat IV; Potential
	Topological domain	1334 – 1352	19	Cytoplasmic Potential
	Transmembrane	1353 – 1372	20	Helical; Name=S5 of repeat IV; Potential
	Topological domain	1373 – 1439	67	Extracellular Potential
	Transmembrane	1440 – 1464	25	Helical; Name=S6 of repeat IV; Potential
	Topological domain	1465 – 2161	697	Cytoplasmic Potential
	Repeat	113 – 409	297	I
	Repeat	509 – 755	247	II
	Repeat	873 – 1155	283	III
	Repeat	1192 – 1467	276	IV
	Calcium binding	1493 – 1504	12	By similarity
	Region	429 – 446	18	Binding to the beta subunit By similarity
	Region	1075 – 1165	91	Dihydropyridine binding By similarity
	Region	1420 – 1486	67	Dihydropyridine binding By similarity
	Region	1432 – 1475	44	Phenylalkylamine binding By similarity
	Compositional bias	1 – 7	7	Poly-Met
	Compositional bias	653 – 659	7	Poly-Leu
	Compositional bias	827 – 838	12	Poly-Glu
Sites
	Site	364	1	Calcium ion selectivity and permeability By similarity
	Site	705	1	Calcium ion selectivity and permeability By similarity
	Site	1101	1	Calcium ion selectivity and permeability By similarity
	Site	1406	1	Calcium ion selectivity and permeability By similarity
Amino acid modifications
	Modified residue	1475	1	Phosphoserine; by PKA Potential
	Glycosylation	155	1	N-linked (GlcNAc...) Potential
	Glycosylation	225	1	N-linked (GlcNAc...) Potential
	Glycosylation	329	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	373 – 392	20	MNDAM…SLVIF → VNDAIGWEWPWVYFVSLIIL in isoform Beta-cell-type.		VSP_000913
	Alternative sequence	493	1	C → WCWWRRRGAAKAGPSGCRRW G in isoform Beta-cell-type.		VSP_000914
	Natural variant	1	1	M → MM in a NIDDM patient. Ref.3		VAR_001497
	Natural variant	403	1	G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. Ref.6		VAR_069170
	Natural variant	2097	1	D → N. Corresponds to variant rs41276455 [ dbSNP | Ensembl ].		VAR_061103
Experimental info
	Sequence conflict	576	1	S → T in BAA07804. Ref.3
	Sequence conflict	637	1	S → C in AAA58402. Ref.1
	Sequence conflict	650	1	I → S in AAA58402. Ref.1
	Sequence conflict	918	1	I → T in BAA07804. Ref.3
	Sequence conflict	960	1	M → I in BAA07804. Ref.3
	Sequence conflict	1289 – 1290	2	Missing in BAA07804. Ref.3
	Sequence conflict	1346	1	S → F in AAA58402. Ref.1
	Sequence conflict	1433	1	Y → H in AAA58402. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Neuronal-type [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 31B0ADFCDB30B575	FASTA	2,161	245,141
	10 20 30 40 50 60 MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA 70 80 90 100 110 120 RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI 130 140 150 160 170 180 SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI 190 200 210 220 230 240 IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR 250 260 270 280 290 300 AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT 310 320 330 340 350 360 CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC 370 380 390 400 410 420 ITMEGWTDVL YWMNDAMGFE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG 430 440 450 460 470 480 DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS 490 500 510 520 530 540 GEGENRGCCG SLCQAISKSK LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI 550 560 570 580 590 600 SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT 610 620 630 640 650 660 ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI ASLLLLLFLF 670 680 690 700 710 720 IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG 730 740 750 760 770 780 PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEAE EKERKKIARK 790 800 810 820 830 840 ESLENKKNNK PEVNQIANSD NKVTIDDYRE EDEDKDPYPP CDVPVGEEEE EEEEDEPEVP 850 860 870 880 890 900 AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS 910 920 930 940 950 960 AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT FGAFLHKGAF CRNYFNLLDM 970 980 990 1000 1010 1020 LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI 1030 1040 1050 1060 1070 1080 VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI LYKDGDVDSP VVRERIWQNS 1090 1100 1110 1120 1130 1140 DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENIGP IYNHRVEISI FFIIYIIIVA 1150 1160 1170 1180 1190 1200 FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY 1210 1220 1230 1240 1250 1260 VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK 1270 1280 1290 1300 1310 1320 PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PTESENVPVP TATPGNSEES NRISITFFRL 1330 1340 1350 1360 1370 1380 FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML FFIYAVIGMQ MFGKVAMRDN 1390 1400 1410 1420 1430 1440 NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL CDPESDYNPG EEYTCGSNFA 1450 1460 1470 1480 1490 1500 IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWS EYDPEAKGRI 1510 1520 1530 1540 1550 1560 KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS DGTVMFNATL FALVRTALKI 1570 1580 1590 1600 1610 1620 KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE VTVGKFYATF LIQDYFRKFK 1630 1640 1650 1660 1670 1680 KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC DLQDDEPEET KREEEDDVFK 1690 1700 1710 1720 1730 1740 RNGALLGNHV NHVNSDRRDS LQQTNTTHRP LHVQRPSIPP ASDTEKPLFP PAGNSVCHNH 1750 1760 1770 1780 1790 1800 HNHNSIGKQV PTSTNANLNN ANMSKAAHGK RPSIGNLEHV SENGHHSSHK HDREPQRRSS 1810 1820 1830 1840 1850 1860 VKRTRYYETY IRSDSGDEQL PTICREDPEI HGYFRDPHCL GEQEYFSSEE CYEDDSSPTW 1870 1880 1890 1900 1910 1920 SRQNYGYYSR YPGRNIDSER PRGYHHPQGF LEDDDSPVCY DSRRSPRRRL LPPTPASHRR 1930 1940 1950 1960 1970 1980 SSFNFECLRR QSSQEEVPSS PIFPHRTALP LHLMQQQIMA VAGLDSSKAQ KYSPSHSTRS 1990 2000 2010 2020 2030 2040 WATPPATPPY RDWTPCYTPL IQVEQSEALD QVNGSLPSLH RSSWYTDEPD ISYRTFTPAS 2050 2060 2070 2080 2090 2100 LTVPSSFRNK NSDKQRSADS LVEAVLISEG LGRYARDPKF VSATKHEIAD ACDLTIDEME 2110 2120 2130 2140 2150 2160 SAASTLLNGN VRPRANGDVG PLSHRQDYEL QDFGPGYSDE EPDPGRDEED LADEMICITT L
	Isoform Beta-cell-type [UniParc]. Checksum: 93C3A848E89B5A76	FASTA	2,181	247,566
	10 20 30 40 50 60 MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA 70 80 90 100 110 120 RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI 130 140 150 160 170 180 SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI 190 200 210 220 230 240 IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR 250 260 270 280 290 300 AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT 310 320 330 340 350 360 CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC 370 380 390 400 410 420 ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG 430 440 450 460 470 480 DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS 490 500 510 520 530 540 GEGENRGCCG SLWCWWRRRG AAKAGPSGCR RWGQAISKSK LSRRWRRWNR FNRRRCRAAV 550 560 570 580 590 600 KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ 610 620 630 640 650 660 AYFVSLFNRF DCFVVCGGIT ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV 670 680 690 700 710 720 ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ 730 740 750 760 770 780 ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES 790 800 810 820 830 840 LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD NKVTIDDYRE EDEDKDPYPP 850 860 870 880 890 900 CDVPVGEEEE EEEEDEPEVP AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH 910 920 930 940 950 960 KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT 970 980 990 1000 1010 1020 FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG 1030 1040 1050 1060 1070 1080 LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI 1090 1100 1110 1120 1130 1140 LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENIGP 1150 1160 1170 1180 1190 1200 IYNHRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL 1210 1220 1230 1240 1250 1260 KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL 1270 1280 1290 1300 1310 1320 NMVFTGVFTV EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PTESENVPVP 1330 1340 1350 1360 1370 1380 TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML 1390 1400 1410 1420 1430 1440 FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL 1450 1460 1470 1480 1490 1500 CDPESDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH 1510 1520 1530 1540 1550 1560 HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS 1570 1580 1590 1600 1610 1620 DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE 1630 1640 1650 1660 1670 1680 VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC 1690 1700 1710 1720 1730 1740 DLQDDEPEET KREEEDDVFK RNGALLGNHV NHVNSDRRDS LQQTNTTHRP LHVQRPSIPP 1750 1760 1770 1780 1790 1800 ASDTEKPLFP PAGNSVCHNH HNHNSIGKQV PTSTNANLNN ANMSKAAHGK RPSIGNLEHV 1810 1820 1830 1840 1850 1860 SENGHHSSHK HDREPQRRSS VKRTRYYETY IRSDSGDEQL PTICREDPEI HGYFRDPHCL 1870 1880 1890 1900 1910 1920 GEQEYFSSEE CYEDDSSPTW SRQNYGYYSR YPGRNIDSER PRGYHHPQGF LEDDDSPVCY 1930 1940 1950 1960 1970 1980 DSRRSPRRRL LPPTPASHRR SSFNFECLRR QSSQEEVPSS PIFPHRTALP LHLMQQQIMA 1990 2000 2010 2020 2030 2040 VAGLDSSKAQ KYSPSHSTRS WATPPATPPY RDWTPCYTPL IQVEQSEALD QVNGSLPSLH 2050 2060 2070 2080 2090 2100 RSSWYTDEPD ISYRTFTPAS LTVPSSFRNK NSDKQRSADS LVEAVLISEG LGRYARDPKF 2110 2120 2130 2140 2150 2160 VSATKHEIAD ACDLTIDEME SAASTLLNGN VRPRANGDVG PLSHRQDYEL QDFGPGYSDE 2170 2180 EPDPGRDEED LADEMICITT L

References

[1]	"Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype." Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G., Ellis S.B., Harpold M.M. Neuron 8:71-84(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NEURONAL-TYPE). Tissue: Neuroblastoma.
[2]	"Cloning of the alpha 1 subunit of a voltage-dependent calcium channel expressed in pancreatic beta cells." Seino S., Chen L., Seino M., Blondel O., Takeda J., Johnson J.H., Bell G.I. Proc. Natl. Acad. Sci. U.S.A. 89:584-588(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-CELL-TYPE). Tissue: Pancreatic islet.
[3]	"The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes." Yamada Y., Masuda K., Li Q., Ihara Y., Kubota A., Miura T., Nakamura K., Fujii Y., Seino S., Seino Y. Genomics 27:312-319(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BETA-CELL-TYPE), VARIANT MET-1 INS.
[4]	"Molecular diversity of neuronal-type calcium channels identified in small cell lung carcinoma." Oguro-Okano M., Griesmann G.E., Wieben E.D., Slaymaker S.J., Snutch T.P., Lennon V.A. Mayo Clin. Proc. 67:1150-1159(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 747-1039, TISSUE SPECIFICITY. Tissue: Lung carcinoma.
[5]	"Loss of recognition by cross-reactive T cells and its relation to a C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide." Loll B., Ruckert C., Hee C.S., Saenger W., Uchanska-Ziegler B., Ziegler A. Protein Sci. 0:0-0(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 502-510 IN COMPLEX WITH HLA.
[6]	"Loss of Ca(v)1.3 (CACNA1D) function in a human channelopathy with bradycardia and congenital deafness." Baig S.M., Koschak A., Lieb A., Gebhart M., Dafinger C., Nurnberg G., Ali A., Ahmad I., Sinnegger-Brauns M.J., Brandt N., Engel J., Mangoni M.E., Farooq M., Khan H.U., Nurnberg P., Striessnig J., Bolz H.J. Nat. Neurosci. 14:77-84(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SANDD GLY-403 INS, CHARACTERIZATION OF VARIANT SANDD GLY-403 INS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M76558 mRNA. Translation: AAA58402.1.
M83566 mRNA. Translation: AAA35629.1.
D43747 Genomic DNA. Translation: BAA07804.1.

IPI

IPI00009008.
IPI00216354.

PIR

JH0564.

RefSeq

NP_000711.1. NM_000720.3.
NP_001122311.1. NM_001128839.2.
NP_001122312.1. NM_001128840.2.

UniGene

Hs.476358.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LV3	X-ray	1.94	C	502-510	[»]

ProteinModelPortal

Q01668.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48998N.

STRING

9606.ENSP00000288139.

PTM databases

PhosphoSite

Q01668.

Polymorphism databases

DMDM

116241275.

Proteomic databases

PaxDb

Q01668.

PRIDE

Q01668.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288139; ENSP00000288139; ENSG00000157388.
ENST00000350061; ENSP00000288133; ENSG00000157388.

GeneID

776.

KEGG

hsa:776.

UCSC

uc003dgu.4. human.
uc003dgv.4. human.

Organism-specific databases

CTD

776.

GeneCards

GC03P053504.

HGNC

HGNC:1391. CACNA1D.

HPA

HPA020215.

MIM

114206. gene.
614896. phenotype.

neXtProt

NX_Q01668.

PharmGKB

PA84.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1226.

HOGENOM

HOG000231529.

HOVERGEN

HBG050763.

KO

K04851.

OMA

TCFFADS.

OrthoDB

EOG47D9F6.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q01668.

Bgee

Q01668.

CleanEx

HS_CACNA1D.

Genevestigator

Q01668.

GermOnline

ENSG00000157388. Homo sapiens.

Family and domain databases

InterPro

IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]

Pfam

PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]

PRINTS

PR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01636. LVDCCALPHA1D.

SMART

SM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q01668.

ChEMBL

CHEMBL4138.

DrugBank

DB00661. Verapamil.

GenomeRNAi

776.

NextBio

3136.

SOURCE

Search...

Entry information

Entry name

CAC1D_HUMAN

Accession

Primary (citable) accession number: Q01668
Secondary accession number(s): Q13916, Q13931, Q9UDC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.