UniProtKB - O35505 (CAC1C_CAVPO)
Voltage-dependent L-type calcium channel subunit alpha-1C
CACNA1C
Functioni
Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:10101289).
Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity).
Plays an important role in excitation-contraction coupling in the heart (By similarity).
Required for normal heart development and normal regulation of heart rhythm (By similarity).
Required for normal contraction of smooth muscle cells in blood vessels and in the intestine (By similarity).
Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity).
Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity).
By similarity1 PublicationActivity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 392 | CalciumBy similarity | 1 | |
Sitei | 392 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Metal bindingi | 735 | CalciumBy similarity | 1 | |
Sitei | 735 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Metal bindingi | 1144 | CalciumBy similarity | 1 | |
Sitei | 1144 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Sitei | 1445 | Calcium ion selectivity and permeabilityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Calcium bindingi | 1534 – 1545 | CuratedAdd BLAST | 12 |
GO - Molecular functioni
- calmodulin binding Source: UniProtKB-KW
- high voltage-gated calcium channel activity Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- voltage-gated calcium channel activity Source: UniProtKB
GO - Biological processi
- calcium ion transmembrane transport Source: UniProtKB
- calcium ion transmembrane transport via high voltage-gated calcium channel Source: UniProtKB
- calcium ion transport into cytosol Source: UniProtKB
- cardiac conduction Source: UniProtKB
- positive regulation of adenylate cyclase activity Source: UniProtKB
- regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: UniProtKB
Keywordsi
Molecular function | Calcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel |
Biological process | Calcium transport, Ion transport, Transport |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Voltage-dependent L-type calcium channel subunit alpha-1CAlternative name(s): Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle Voltage-gated calcium channel subunit alpha Cav1.2 |
Gene namesi | Name:CACNA1C Synonyms:CACH2, CACN2, CACNL1A1, CCHL1A1 |
Organismi | Cavia porcellus (Guinea pig) |
Taxonomic identifieri | 10141 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricomorpha › Caviidae › Cavia |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Multi-pass membrane protein By similarity
- sarcolemma By similarity; Multi-pass membrane protein By similarity
- postsynaptic density membrane By similarity
- T-tubule By similarity
Other locations
- Perikaryon By similarity
- dendrite By similarity
Note: Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane.By similarity
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB
- L-type voltage-gated calcium channel complex Source: UniProtKB
- postsynaptic density membrane Source: UniProtKB-SubCell
- sarcolemma Source: UniProtKB
- T-tubule Source: UniProtKB
Other locations
- dendrite Source: UniProtKB-SubCell
- perikaryon Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 153 | CytoplasmicCuratedAdd BLAST | 153 | |
Transmembranei | 154 – 172 | Helical; Name=S1 of repeat IBy similarityAdd BLAST | 19 | |
Topological domaini | 173 – 187 | ExtracellularCuratedAdd BLAST | 15 | |
Transmembranei | 188 – 208 | Helical; Name=S2 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 209 – 217 | CytoplasmicCurated | 9 | |
Transmembranei | 218 – 238 | Helical; Name=S3 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 239 – 261 | ExtracellularCuratedAdd BLAST | 23 | |
Transmembranei | 262 – 280 | Helical; Name=S4 of repeat IBy similarityAdd BLAST | 19 | |
Topological domaini | 281 – 297 | CytoplasmicCuratedAdd BLAST | 17 | |
Transmembranei | 298 – 319 | Helical; Name=S5 of repeat IBy similarityAdd BLAST | 22 | |
Topological domaini | 320 – 379 | ExtracellularCuratedAdd BLAST | 60 | |
Intramembranei | 380 – 401 | Pore-formingBy similarityAdd BLAST | 22 | |
Topological domaini | 402 – 409 | ExtracellularCurated | 8 | |
Transmembranei | 410 – 430 | Helical; Name=S6 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 431 – 553 | CytoplasmicCuratedAdd BLAST | 123 | |
Transmembranei | 554 – 572 | Helical; Name=S1 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 573 – 583 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 584 – 604 | Helical; Name=S2 of repeat IIBy similarityAdd BLAST | 21 | |
Topological domaini | 605 – 615 | CytoplasmicCuratedAdd BLAST | 11 | |
Transmembranei | 616 – 635 | Helical; Name=S3 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 636 – 644 | ExtracellularCurated | 9 | |
Transmembranei | 645 – 663 | Helical; Name=S4 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 664 – 682 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 683 – 702 | Helical; Name=S5 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 703 – 722 | ExtracellularCuratedAdd BLAST | 20 | |
Intramembranei | 723 – 744 | Pore-formingBy similarityAdd BLAST | 22 | |
Topological domaini | 745 – 754 | ExtracellularCurated | 10 | |
Transmembranei | 755 – 774 | Helical; Name=S6 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 775 – 929 | CytoplasmicCuratedAdd BLAST | 155 | |
Transmembranei | 930 – 948 | Helical; Name=S1 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 949 – 960 | ExtracellularCuratedAdd BLAST | 12 | |
Transmembranei | 961 – 980 | Helical; Name=S2 of repeat IIIBy similarityAdd BLAST | 20 | |
Topological domaini | 981 – 996 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 997 – 1015 | Helical; Name=S3 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1016 – 1022 | ExtracellularCurated | 7 | |
Transmembranei | 1023 – 1041 | Helical; Name=S4 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1042 – 1060 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 1061 – 1080 | Helical; Name=S5 of repeat IIIBy similarityAdd BLAST | 20 | |
Topological domaini | 1081 – 1130 | ExtracellularCuratedAdd BLAST | 50 | |
Intramembranei | 1131 – 1151 | Pore-formingBy similarityAdd BLAST | 21 | |
Topological domaini | 1152 – 1168 | ExtracellularCuratedAdd BLAST | 17 | |
Transmembranei | 1169 – 1190 | Helical; Name=S6 of repeat IIIBy similarityAdd BLAST | 22 | |
Topological domaini | 1191 – 1248 | CytoplasmicCuratedAdd BLAST | 58 | |
Transmembranei | 1249 – 1270 | Helical; Name=S1 of repeat IVBy similarityAdd BLAST | 22 | |
Topological domaini | 1271 – 1278 | ExtracellularCurated | 8 | |
Transmembranei | 1279 – 1300 | Helical; Name=S2 of repeat IVBy similarityAdd BLAST | 22 | |
Topological domaini | 1301 – 1310 | CytoplasmicCurated | 10 | |
Transmembranei | 1311 – 1330 | Helical; Name=S3 of repeat IVBy similarityAdd BLAST | 20 | |
Topological domaini | 1331 – 1353 | ExtracellularCuratedAdd BLAST | 23 | |
Transmembranei | 1354 – 1372 | Helical; Name=S4 of repeat IVBy similarityAdd BLAST | 19 | |
Topological domaini | 1373 – 1390 | CytoplasmicCuratedAdd BLAST | 18 | |
Transmembranei | 1391 – 1411 | Helical; Name=S5 of repeat IVBy similarityAdd BLAST | 21 | |
Topological domaini | 1412 – 1433 | ExtracellularCuratedAdd BLAST | 22 | |
Intramembranei | 1434 – 1452 | Pore-formingBy similarityAdd BLAST | 19 | |
Topological domaini | 1453 – 1480 | ExtracellularCuratedAdd BLAST | 28 | |
Transmembranei | 1481 – 1505 | Helical; Name=S6 of repeat IVBy similarityAdd BLAST | 25 | |
Topological domaini | 1506 – 2169 | CytoplasmicCuratedAdd BLAST | 664 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, SynapsePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053927 | 1 – 2169 | Voltage-dependent L-type calcium channel subunit alpha-1CAdd BLAST | 2169 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 182 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 345 ↔ 361 | By similarity | ||
Glycosylationi | 357 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 498 | PhosphoserineBy similarity | 1 | |
Modified residuei | 505 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 837 | PhosphoserineBy similarity | 1 | |
Modified residuei | 844 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1087 ↔ 1098 | By similarity | ||
Glycosylationi | 1417 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1460 ↔ 1476 | By similarity | ||
Glycosylationi | 1468 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1699 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1720 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1927 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinExpressioni
Tissue specificityi
Developmental stagei
Interactioni
Subunit structurei
Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit. CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity).
Interacts with CACNB1 (By similarity).
Interacts with CACNB2.
Identified in a complex with CACNA2D4 and CACNB3.
Interacts with CACNB3.
Interacts with CACNA2D1.
Interacts with CACNA2D4 (By similarity).
Interacts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity).
Interacts with CALM1.
Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca2+-dependent channel inactivation. The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding (By similarity). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation.
Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner.
Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (By similarity).
Interacts with STAC2 and STAC3; this inhibits channel inactivation (By similarity).
By similarityBinary interactionsi
O35505
With | #Exp. | IntAct |
---|---|---|
CALM3 [P0DP24] from Homo sapiens. | 2 | EBI-9084208,EBI-397435 |
CAST [P20810] from Homo sapiens. | 2 | EBI-9084208,EBI-1268770 |
GO - Molecular functioni
- calmodulin binding Source: UniProtKB-KW
Protein-protein interaction databases
IntActi | O35505, 2 interactors |
MINTi | O35505 |
Chemistry databases
BindingDBi | O35505 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 140 – 437 | ICuratedAdd BLAST | 298 | |
Repeati | 539 – 785 | IICuratedAdd BLAST | 247 | |
Repeati | 916 – 1198 | IIICuratedAdd BLAST | 283 | |
Repeati | 1235 – 1508 | IVCuratedAdd BLAST | 274 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 76 – 97 | Calmodulin-bindingBy similarityAdd BLAST | 22 | |
Regioni | 98 – 127 | DisorderedSequence analysisAdd BLAST | 30 | |
Regioni | 457 – 474 | AID/alpha-interaction domain; mediates interaction with the beta subunitBy similarityAdd BLAST | 18 | |
Regioni | 478 – 510 | DisorderedSequence analysisAdd BLAST | 33 | |
Regioni | 793 – 890 | DisorderedSequence analysisAdd BLAST | 98 | |
Regioni | 858 – 905 | Interaction with STAC2By similarityAdd BLAST | 48 | |
Regioni | 1118 – 1207 | Dihydropyridine bindingBy similarityAdd BLAST | 90 | |
Regioni | 1459 – 1527 | Dihydropyridine bindingBy similarityAdd BLAST | 69 | |
Regioni | 1473 – 1515 | Phenylalkylamine bindingBy similarityAdd BLAST | 43 | |
Regioni | 1640 – 1667 | Important for interaction with STAC1, STAC2 and STAC3By similarityAdd BLAST | 28 | |
Regioni | 1646 – 1666 | Calmodulin-binding IQ regionBy similarityAdd BLAST | 21 | |
Regioni | 1680 – 1699 | Important for localization in at the junctional membraneBy similarityAdd BLAST | 20 | |
Regioni | 1761 – 1793 | DisorderedSequence analysisAdd BLAST | 33 | |
Regioni | 1894 – 1920 | DisorderedSequence analysisAdd BLAST | 27 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 390 – 393 | Selectivity filter of repeat IBy similarity | 4 | |
Motifi | 733 – 736 | Selectivity filter of repeat IIBy similarity | 4 | |
Motifi | 1142 – 1145 | Selectivity filter of repeat IIIBy similarity | 4 | |
Motifi | 1443 – 1446 | Selectivity filter of repeat IVBy similarity | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 793 – 838 | Basic and acidic residuesSequence analysisAdd BLAST | 46 | |
Compositional biasi | 1894 – 1912 | Basic and acidic residuesSequence analysisAdd BLAST | 19 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | O35505 |
OMAi | KQPQWLT |
OrthoDBi | 172471at2759 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR031688, CAC1F_C IPR031649, GPHH_dom IPR005821, Ion_trans_dom IPR014873, VDCC_a1su_IQ IPR005451, VDCC_L_a1csu IPR005446, VDCC_L_a1su IPR002077, VDCCAlpha1 IPR027359, Volt_channel_dom_sf |
Pfami | View protein in Pfam PF08763, Ca_chan_IQ, 1 hit PF16885, CAC1F_C, 2 hits PF16905, GPHH, 1 hit PF00520, Ion_trans, 4 hits |
PRINTSi | PR00167, CACHANNEL PR01630, LVDCCALPHA1 PR01635, LVDCCALPHA1C |
SMARTi | View protein in SMART SM01062, Ca_chan_IQ, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MVPLVQPTTP AYRPLPSHLS ADTEVRGRGT LVHEAQLNCF YISPGGSNYG
60 70 80 90 100
SPRPAHANIN ANAAAGLAPE HIPTPGAALS WQAAIDAGRQ AKLMGSAGNT
110 120 130 140 150
TISTVSSTQR KRQQYGKPKK QSGTTATRPP RALLCLTLKN PIRRACISIV
160 170 180 190 200
EWKPFEIIIL LTIFANCVAL AIYIPFPEDD SNATNSNLER VEYLFLIIFT
210 220 230 240 250
VEAFLKVIAY GLLFHPNAYL RNGWNLLDFI IVVVGLFSAI LEQATKADGA
260 270 280 290 300
NALGGKGAGF DVKALRAFRV LRPLRLVSGV PSLQVVLNSI IKAMVPLLHT
310 320 330 340 350
ALLVLFVIII YAIIGLELFM GKMHKTCYNQ EGITDVPAEE DPSPCALESG
360 370 380 390 400
HGRQCQNGTV CKPGWDGPKH GITNFDNFAF AMLTVFQCIT MEGWTDVLYW
410 420 430 440 450
MQDAMGYELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF
460 470 480 490 500
QKLREKQQLE EDLKGYLDWI TQAEDIDPEN EDEGVDEEKP RNMSMPTSET
510 520 530 540 550
ESVNTENVAG GDIEGENCGA RLAHRISKSK FSRYWRRWNR FCRRKCRAAV
560 570 580 590 600
KSNVFYWLVI FLVFLNTLTI ASEHYNQPHW LTEVQDTANK ALLALFTAEM
610 620 630 640 650
LLKMYSLGLQ AYFVSLFNRL DCFIVCGGIL ETILVETKIM SPLGISVLRC
660 670 680 690 700
VRLLRIFKIT RYWNSLSNLV ASLLNSVRSI ASLLLLLFLF IIIFSLLGMQ
710 720 730 740 750
LFGGKFNFDE MRTRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG
760 770 780 790 800
PSFPGMLVCI YFIILFICGN YILLNVFLAI AVDNLADAES LTSAQKEEEE
810 820 830 840 850
EKERKKLART ASPEKKQEVV EKPAVEETKE EKIELKSITA DGESPPTTKI
860 870 880 890 900
NMDDLQPNEN EDKSPYPNPD AAGEEDEEEP EMPVGPRPRP LSELHLKEKA
910 920 930 940 950
VPMPEASAFF IFSPNNRFRL QCHRIVNDTI FTNLILFFIL LSSISLAAED
960 970 980 990 1000
PVQHTSFRNH ILFYFDIVFT TIFTIEIALK MTAYGAFLHK GSFCRNYFNI
1010 1020 1030 1040 1050
LDLLVVSVSL ISFGIQSSAI NVVKILRVLR VLRPLRAINR AKGLKHVVQC
1060 1070 1080 1090 1100
VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAECKG
1110 1120 1130 1140 1150
NYITYKDGEV DQPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL
1160 1170 1180 1190 1200
YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
1210 1220 1230 1240 1250
QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNQHQYK VWYVVNSTYF
1260 1270 1280 1290 1300
EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI
1310 1320 1330 1340 1350
AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVNPAEHTQC SPSMNAEENS
1360 1370 1380 1390 1400
RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF
1410 1420 1430 1440 1450
FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI
1460 1470 1480 1490 1500
MLACMPGKKC APESDPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
1510 1520 1530 1540 1550
VAVVMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL
1560 1570 1580 1590 1600
RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTAMFNAT LFALVRTALR
1610 1620 1630 1640 1650
IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT
1660 1670 1680 1690 1700
FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG
1710 1720 1730 1740 1750
DLTAEEELDK AMKEAVSAAS EDDIFGRAGG LFGNHVSYYQ SDSRSTFPQT
1760 1770 1780 1790 1800
FTTQRPLHIN KAGNNQGDTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
1810 1820 1830 1840 1850
NTALGRFPHP AGYPSTVSTV EGHRPPSSPA TWAQEATRKL GAMRCHSRES
1860 1870 1880 1890 1900
QIAVVCQEEP SQDKTYDVEL NKDAEYCSEP SLLSTEMLSY KDDENRQLTP
1910 1920 1930 1940 1950
PEEDKGDTRP SPKKGFLRSA SLGRRASFHL ECLKRQKNHG GDISQKTVLP
1960 1970 1980 1990 2000
LHLVHHQALA VAGLSPLLQR SHSPTAIPRP CATPPATPGS RGWPPKPIPT
2010 2020 2030 2040 2050
LRLEGAESCE KLNSSFPSIH CSSWSEEPSP CGGGSSAARR ARPVSLMVPS
2060 2070 2080 2090 2100
QAGAPGRQFH GSASSLAEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
2110 2120 2130 2140 2150
IGEMENAADN ILSGGAPQSP NGTLLPFVNC RDPGQDRAGG DEDEGCACAL
2160
GRGWSEEELA DSRVHVRSL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 1460 | C → R in AAB62890 (PubMed:11058528).Curated | 1 | |
Sequence conflicti | 1465 | D → E in AAB62890 (PubMed:11058528).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_060907 | 1234 – 1352 | KNQHQ…ENSRI → I in isoform 2. CuratedAdd BLAST | 119 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB016287 mRNA Translation: BAA34185.2 AF005938 mRNA Translation: AAB62890.1 |
RefSeqi | NP_001166394.1, NM_001172923.1 [O35505-1] |
Genome annotation databases
GeneIDi | 100135490 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB016287 mRNA Translation: BAA34185.2 AF005938 mRNA Translation: AAB62890.1 |
RefSeqi | NP_001166394.1, NM_001172923.1 [O35505-1] |
3D structure databases
SMRi | O35505 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | O35505, 2 interactors |
MINTi | O35505 |
Chemistry databases
BindingDBi | O35505 |
ChEMBLi | CHEMBL2366456 |
DrugCentrali | O35505 |
Genome annotation databases
GeneIDi | 100135490 |
Organism-specific databases
CTDi | 775 |
Phylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | O35505 |
OMAi | KQPQWLT |
OrthoDBi | 172471at2759 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR031688, CAC1F_C IPR031649, GPHH_dom IPR005821, Ion_trans_dom IPR014873, VDCC_a1su_IQ IPR005451, VDCC_L_a1csu IPR005446, VDCC_L_a1su IPR002077, VDCCAlpha1 IPR027359, Volt_channel_dom_sf |
Pfami | View protein in Pfam PF08763, Ca_chan_IQ, 1 hit PF16885, CAC1F_C, 2 hits PF16905, GPHH, 1 hit PF00520, Ion_trans, 4 hits |
PRINTSi | PR00167, CACHANNEL PR01630, LVDCCALPHA1 PR01635, LVDCCALPHA1C |
SMARTi | View protein in SMART SM01062, Ca_chan_IQ, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CAC1C_CAVPO | |
Accessioni | O35505Primary (citable) accession number: O35505 Secondary accession number(s): Q9Z305 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | February 10, 2021 | |
Last modified: | February 23, 2022 | |
This is version 111 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families