UniProtKB - P27884 (CAC1A_RABIT)
Voltage-dependent P/Q-type calcium channel subunit alpha-1A
CACNA1A
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 318 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Sitei | 668 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Sitei | 1469 | Calcium ion selectivity and permeabilityBy similarity | 1 | |
Sitei | 1658 | Binds to omega-Aga-IVA | 1 | |
Sitei | 1765 | Calcium ion selectivity and permeabilityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Calcium bindingi | 1849 – 1860 | By similarityAdd BLAST | 12 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- protein C-terminus binding Source: UniProtKB
- voltage-gated calcium channel activity Source: UniProtKB
GO - Biological processi
- calcium ion transmembrane transport Source: GOC
- positive regulation of cytosolic calcium ion concentration Source: UniProtKB
- regulation of ion transmembrane transport Source: UniProtKB-KW
Keywordsi
Molecular function | Calcium channel, Ion channel, Voltage-gated channel |
Biological process | Calcium transport, Ion transport, Transport |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Voltage-dependent P/Q-type calcium channel subunit alpha-1AAlternative name(s): Brain calcium channel I Short name: BI Calcium channel, L type, alpha-1 polypeptide isoform 4 Voltage-gated calcium channel subunit alpha Cav2.1 |
Gene namesi | Name:CACNA1A Synonyms:CACH4, CACN3, CACNL1A4 |
Organismi | Oryctolagus cuniculus (Rabbit) |
Taxonomic identifieri | 9986 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Multi-pass membrane protein Sequence analysis
Plasma Membrane
- plasma membrane Source: UniProtKB
- voltage-gated calcium channel complex Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 98 | CytoplasmicSequence analysisAdd BLAST | 98 | |
Transmembranei | 99 – 117 | Helical; Name=S1 of repeat ISequence analysisAdd BLAST | 19 | |
Topological domaini | 118 – 135 | ExtracellularSequence analysisAdd BLAST | 18 | |
Transmembranei | 136 – 155 | Helical; Name=S2 of repeat ISequence analysisAdd BLAST | 20 | |
Topological domaini | 156 – 167 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 168 – 185 | Helical; Name=S3 of repeat ISequence analysisAdd BLAST | 18 | |
Topological domaini | 186 – 190 | ExtracellularSequence analysis | 5 | |
Transmembranei | 191 – 209 | Helical; Name=S4 of repeat ISequence analysisAdd BLAST | 19 | |
Topological domaini | 210 – 228 | CytoplasmicSequence analysisAdd BLAST | 19 | |
Transmembranei | 229 – 248 | Helical; Name=S5 of repeat ISequence analysisAdd BLAST | 20 | |
Topological domaini | 249 – 335 | ExtracellularSequence analysisAdd BLAST | 87 | |
Transmembranei | 336 – 360 | Helical; Name=S6 of repeat ISequence analysisAdd BLAST | 25 | |
Topological domaini | 361 – 487 | CytoplasmicSequence analysisAdd BLAST | 127 | |
Transmembranei | 488 – 506 | Helical; Name=S1 of repeat IISequence analysisAdd BLAST | 19 | |
Topological domaini | 507 – 521 | ExtracellularSequence analysisAdd BLAST | 15 | |
Transmembranei | 522 – 541 | Helical; Name=S2 of repeat IISequence analysisAdd BLAST | 20 | |
Topological domaini | 542 – 549 | CytoplasmicSequence analysis | 8 | |
Transmembranei | 550 – 568 | Helical; Name=S3 of repeat IISequence analysisAdd BLAST | 19 | |
Topological domaini | 569 – 578 | ExtracellularSequence analysis | 10 | |
Transmembranei | 579 – 597 | Helical; Name=S4 of repeat IISequence analysisAdd BLAST | 19 | |
Topological domaini | 598 – 616 | CytoplasmicSequence analysisAdd BLAST | 19 | |
Transmembranei | 617 – 636 | Helical; Name=S5 of repeat IISequence analysisAdd BLAST | 20 | |
Topological domaini | 637 – 689 | ExtracellularSequence analysisAdd BLAST | 53 | |
Transmembranei | 690 – 714 | Helical; Name=S6 of repeat IISequence analysisAdd BLAST | 25 | |
Topological domaini | 715 – 1253 | CytoplasmicSequence analysisAdd BLAST | 539 | |
Transmembranei | 1254 – 1272 | Helical; Name=S1 of repeat IIISequence analysisAdd BLAST | 19 | |
Topological domaini | 1273 – 1288 | ExtracellularSequence analysisAdd BLAST | 16 | |
Transmembranei | 1289 – 1308 | Helical; Name=S2 of repeat IIISequence analysisAdd BLAST | 20 | |
Topological domaini | 1309 – 1320 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 1321 – 1339 | Helical; Name=S3 of repeat IIISequence analysisAdd BLAST | 19 | |
Topological domaini | 1340 – 1350 | ExtracellularSequence analysisAdd BLAST | 11 | |
Transmembranei | 1351 – 1369 | Helical; Name=S4 of repeat IIISequence analysisAdd BLAST | 19 | |
Topological domaini | 1370 – 1388 | CytoplasmicSequence analysisAdd BLAST | 19 | |
Transmembranei | 1389 – 1408 | Helical; Name=S5 of repeat IIISequence analysisAdd BLAST | 20 | |
Topological domaini | 1409 – 1495 | ExtracellularSequence analysisAdd BLAST | 87 | |
Transmembranei | 1496 – 1520 | Helical; Name=S6 of repeat IIISequence analysisAdd BLAST | 25 | |
Topological domaini | 1521 – 1575 | CytoplasmicSequence analysisAdd BLAST | 55 | |
Transmembranei | 1576 – 1604 | Helical; Name=S1 of repeat IVSequence analysisAdd BLAST | 29 | |
Topological domaini | 1605 – 1609 | ExtracellularSequence analysis | 5 | |
Transmembranei | 1610 – 1629 | Helical; Name=S2 of repeat IVSequence analysisAdd BLAST | 20 | |
Topological domaini | 1630 – 1637 | CytoplasmicSequence analysis | 8 | |
Transmembranei | 1638 – 1656 | Helical; Name=S3 of repeat IVSequence analysisAdd BLAST | 19 | |
Topological domaini | 1657 – 1665 | ExtracellularSequence analysis | 9 | |
Transmembranei | 1666 – 1684 | Helical; Name=S4 of repeat IVSequence analysisAdd BLAST | 19 | |
Topological domaini | 1685 – 1703 | CytoplasmicSequence analysisAdd BLAST | 19 | |
Transmembranei | 1704 – 1723 | Helical; Name=S5 of repeat IVSequence analysisAdd BLAST | 20 | |
Topological domaini | 1724 – 1795 | ExtracellularSequence analysisAdd BLAST | 72 | |
Transmembranei | 1796 – 1820 | Helical; Name=S6 of repeat IVSequence analysisAdd BLAST | 25 | |
Topological domaini | 1821 – 2424 | CytoplasmicSequence analysisAdd BLAST | 604 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 188 | E → K: No change in inhibition by omega-Aga-IVA. 1 Publication | 1 | |
Mutagenesisi | 386 | E → S: Reduced beta-subunit interaction. 1 Publication | 1 | |
Mutagenesisi | 389 | L → H: Reduced beta-subunit interaction. 1 Publication | 1 | |
Mutagenesisi | 392 | Y → S: Reduced beta-subunit interaction. 1 Publication | 1 | |
Mutagenesisi | 400 | E → A: No effect on beta-subunit interaction. 1 Publication | 1 | |
Mutagenesisi | 1658 | E → K: Loss of inhibition by omega-Aga-IVA. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053918 | 1 – 2424 | Voltage-dependent P/Q-type calcium channel subunit alpha-1AAdd BLAST | 2424 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 283 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 409 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 448 | PhosphoserineBy similarity | 1 | |
Modified residuei | 451 | PhosphoserineBy similarity | 1 | |
Modified residuei | 750 | PhosphoserineBy similarity | 1 | |
Modified residuei | 753 | PhosphoserineBy similarity | 1 | |
Modified residuei | 790 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1091 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1104 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 1665 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1993 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 2054 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2072 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2084 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2086 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2127 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2148 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PRIDEi | P27884 |
Expressioni
Tissue specificityi
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 (By similarity).
Interacts with the spider omega-agatoxin-IVA (AC P30288).
By similarityBinary interactionsi
Hide detailsP27884
With | #Exp. | IntAct |
---|---|---|
CALM3 [P0DP25] from Homo sapiens. | 3 | EBI-15685548,EBI-397435 |
GEM [P55040] from Homo sapiens. | 2 | EBI-15685548,EBI-744104 |
GO - Molecular functioni
- protein C-terminus binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 1172286, 4 interactors |
DIPi | DIP-29591N |
IntActi | P27884, 3 interactors |
STRINGi | 9986.ENSOCUP00000010319 |
Structurei
Secondary structure
3D structure databases
BMRBi | P27884 |
SMRi | P27884 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27884 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 85 – 363 | IAdd BLAST | 279 | |
Repeati | 473 – 717 | IIAdd BLAST | 245 | |
Repeati | 1240 – 1523 | IIIAdd BLAST | 284 | |
Repeati | 1560 – 1823 | IVAdd BLAST | 264 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 383 – 400 | Binding to the beta subunitAdd BLAST | 18 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 13 – 18 | Poly-Gly | 6 | |
Compositional biasi | 727 – 732 | Poly-Glu | 6 | |
Compositional biasi | 1004 – 1010 | Poly-Gly | 7 | |
Compositional biasi | 1012 – 1017 | Poly-Arg | 6 | |
Compositional biasi | 2219 – 2227 | Poly-His | 9 | |
Compositional biasi | 2242 – 2246 | Poly-Arg | 5 | |
Compositional biasi | 2288 – 2297 | Poly-Arg | 10 | |
Compositional biasi | 2298 – 2301 | Poly-Gly | 4 | |
Compositional biasi | 2372 – 2377 | Poly-Pro | 6 | |
Compositional biasi | 2411 – 2416 | Poly-Gly | 6 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | P27884 |
OrthoDBi | 172471at2759 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005448, CACNA1A IPR031649, GPHH_dom IPR005821, Ion_trans_dom IPR014873, VDCC_a1su_IQ IPR002077, VDCCAlpha1 IPR027359, Volt_channel_dom_sf |
Pfami | View protein in Pfam PF08763, Ca_chan_IQ, 1 hit PF16905, GPHH, 1 hit PF00520, Ion_trans, 4 hits |
PRINTSi | PR00167, CACHANNEL PR01632, PQVDCCALPHA1 |
SMARTi | View protein in SMART SM01062, Ca_chan_IQ, 1 hit |
s (5)i Sequence
Sequence statusi: Complete.
This entry describes 5 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
MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ
60 70 80 90 100
SMAQRARTMA LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF
110 120 130 140 150
EYMILATIIA NCIVLALEQH LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI
160 170 180 190 200
KIIALGFAFH KGSYLRNGWN VMDFVVVLTG ILATVGTEFD LRTLRAVRVL
210 220 230 240 250
RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF AIIGLEFYMG
260 270 280 290 300
KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ
310 320 330 340 350
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF
360 370 380 390 400
MLNLVLGVLS GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE
410 420 430 440 450
EVILAEDETD VEQRHPFDGA LRRATIKKSK TDLLHPEEAE DQLADIASVG
460 470 480 490 500
SPFARASIKS AKLENSSFFH KKERRMRFYI RRMVKTQAFY WTVLSLVALN
510 520 530 540 550
TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG LGTRPYFHSS
560 570 580 590 600
FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
610 620 630 640 650
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN
660 670 680 690 700
FDTFPAAIMT VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF
710 720 730 740 750
GNYTLLNVFL AIAVDNLANA QELTKDEQEE EEAVNQKLAL QKAKEVAEVS
760 770 780 790 800
PLSAANMSIA MKEQQKNQKP AKSVWEQRTS EMRKQNLLAS REALYSEMDP
810 820 830 840 850
EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR VAEPTVDQRL
860 870 880 890 900
GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY
910 920 930 940 950
GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG
960 970 980 990 1000
SPRTGTADGE PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE
1010 1020 1030 1040 1050
GPDGGGGGGG ERRRRHRHGP PPAYDPDARR DDRERRHRRR KDTQGSGVPV
1060 1070 1080 1090 1100
SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK NSRLATAEPV SPHENLSHAG
1110 1120 1130 1140 1150
LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN PSNPGPPKTP
1160 1170 1180 1190 1200
ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN
1210 1220 1230 1240 1250
PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL
1260 1270 1280 1290 1300
NLRYFEMCIL MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE
1310 1320 1330 1340 1350
MVIKMIDLGL VLHQGAYFRD LWNILDFIVV SGALVAFAFT GNSKGKDINT
1360 1370 1380 1390 1400
IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVFNIL IVYMLFMFIF
1410 1420 1430 1440 1450
AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA RDREWKKYEF
1460 1470 1480 1490 1500
HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY
1510 1520 1530 1540 1550
VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA
1560 1570 1580 1590 1600
KPLTRHMPQN KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS
1610 1620 1630 1640 1650
VAYDNALKVF NIVFTSLFSL ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS
1660 1670 1680 1690 1700
ITDILVTEFG NNFINLSFLR LFRAARLIKL LRQGYTIRIL LWTFVQSFKA
1710 1720 1730 1740 1750
LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF QITEHNNFRT
1760 1770 1780 1790 1800
FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF
1810 1820 1830 1840 1850
VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP
1860 1870 1880 1890 1900
AAWGRMLYRD MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV
1910 1920 1930 1940 1950
HFNSTLMALI RTALDIKIAK GGADKQQMDA ELRKEMMAIW PNLSQKTLDL
1960 1970 1980 1990 2000
LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA KKLQAMREEQ NRTPLMFQRM
2010 2020 2030 2040 2050
EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT QRAQEMFQKT
2060 2070 2080 2090 2100
GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS
2110 2120 2130 2140 2150
MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE
2160 2170 2180 2190 2200
RVPPEENQRH HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP
2210 2220 2230 2240 2250
SREREQERGR PKDRKHRPHH HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA
2260 2270 2280 2290 2300
RVRPARAPAL AHARARARAP ARLLPELRLR RARRPRPRQR RRPRRRRGGG
2310 2320 2330 2340 2350
GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL PGPRTGQAPR
2360 2370 2380 2390 2400
ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR
2410 2420
RGGRRWTASA GKGGGGPRAS APSP
The sequence of this isoform differs from the canonical sequence as follows:
2230-2273: RGPGRVSPGV...RARARAPARL → PAAADKERYG...EGREHTTHRQ
2274-2424: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1857-1884: LYRDMYAMLRHMPPPLGLGKNCPARVAY → HYKDMYSLLRVISPPLGLGKKCPHRVAC
The sequence of this isoform differs from the canonical sequence as follows:
772-1120: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
772-1051: Missing.
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 419 | Missing in isoform CBP315. | 1 | |
Natural varianti | 877 | A → T in isoform CBS. | 1 | |
Natural varianti | 1104 | S → N in isoform CBS. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000877 | 772 – 1120 | Missing in isoform CBP103. CuratedAdd BLAST | 349 | |
Alternative sequenceiVSP_000876 | 772 – 1051 | Missing in isoform CBP107. CuratedAdd BLAST | 280 | |
Alternative sequenceiVSP_000878 | 1857 – 1884 | LYRDM…ARVAY → HYKDMYSLLRVISPPLGLGK KCPHRVAC in isoform CBP101. CuratedAdd BLAST | 28 | |
Alternative sequenceiVSP_000879 | 2230 – 2273 | RGPGR…APARL → PAAADKERYGPQDRPDHGHG RARARDQRWSRSPSEGREHT THRQ in isoform BI-1. CuratedAdd BLAST | 44 | |
Alternative sequenceiVSP_000880 | 2274 – 2424 | Missing in isoform BI-1. CuratedAdd BLAST | 151 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57477 mRNA Translation: CAA40715.1 X57689 mRNA Translation: CAA40872.1 X57476 mRNA Translation: CAA40714.1 X57688 mRNA Translation: CAA40871.1 |
PIRi | I46477 I46480 |
RefSeqi | NP_001095163.1, NM_001101693.1 [P27884-2] |
Genome annotation databases
GeneIDi | 100009265 |
KEGGi | ocu:100009265 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57477 mRNA Translation: CAA40715.1 X57689 mRNA Translation: CAA40872.1 X57476 mRNA Translation: CAA40714.1 X57688 mRNA Translation: CAA40871.1 |
PIRi | I46477 I46480 |
RefSeqi | NP_001095163.1, NM_001101693.1 [P27884-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3DVM | X-ray | 2.60 | B | 1963-1982 | [»] | |
BMRBi | P27884 | |||||
SMRi | P27884 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 1172286, 4 interactors |
DIPi | DIP-29591N |
IntActi | P27884, 3 interactors |
STRINGi | 9986.ENSOCUP00000010319 |
Proteomic databases
PRIDEi | P27884 |
Genome annotation databases
GeneIDi | 100009265 |
KEGGi | ocu:100009265 |
Organism-specific databases
CTDi | 773 |
Phylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | P27884 |
OrthoDBi | 172471at2759 |
Miscellaneous databases
EvolutionaryTracei | P27884 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005448, CACNA1A IPR031649, GPHH_dom IPR005821, Ion_trans_dom IPR014873, VDCC_a1su_IQ IPR002077, VDCCAlpha1 IPR027359, Volt_channel_dom_sf |
Pfami | View protein in Pfam PF08763, Ca_chan_IQ, 1 hit PF16905, GPHH, 1 hit PF00520, Ion_trans, 4 hits |
PRINTSi | PR00167, CACHANNEL PR01632, PQVDCCALPHA1 |
SMARTi | View protein in SMART SM01062, Ca_chan_IQ, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CAC1A_RABIT | |
Accessioni | P27884Primary (citable) accession number: P27884 Secondary accession number(s): P27883 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | July 1, 1993 | |
Last modified: | December 2, 2020 | |
This is version 149 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families