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Q02294

- CAC1B_RAT

UniProt

Q02294 - CAC1B_RAT

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Protein

Voltage-dependent N-type calcium channel subunit alpha-1B

Gene

Cacna1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei314 – 3141Calcium ion selectivity and permeabilityBy similarity
Sitei664 – 6641Calcium ion selectivity and permeabilityBy similarity
Sitei1367 – 13671Calcium ion selectivity and permeabilityBy similarity
Sitei1655 – 16551Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi452 – 4598ATPSequence Analysis
Calcium bindingi1737 – 174812PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. high voltage-gated calcium channel activity Source: RGD
  4. protein phosphatase 2A binding Source: RGD
  5. voltage-gated calcium channel activity Source: RGD

GO - Biological processi

  1. calcium ion import Source: RGD
  2. calcium ion transport Source: RGD
  3. membrane depolarization during action potential Source: RefGenome
  4. positive regulation of neurotransmitter secretion Source: RGD
  5. response to ethanol Source: RGD
  6. response to organic cyclic compound Source: RGD
  7. response to testosterone Source: RGD
  8. sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent N-type calcium channel subunit alpha-1B
Alternative name(s):
Brain calcium channel III
Short name:
BIII
Calcium channel, L type, alpha-1 polypeptide isoform 5
Voltage-gated calcium channel subunit alpha Cav2.2
Gene namesi
Name:Cacna1b
Synonyms:Cach5, Cacnl1a5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi628852. Cacna1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9595CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei96 – 11419Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Topological domaini115 – 13319ExtracellularSequence AnalysisAdd
BLAST
Transmembranei134 – 15118Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Topological domaini152 – 16413CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei165 – 17915Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Topological domaini180 – 1867ExtracellularSequence Analysis
Transmembranei187 – 20519Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Topological domaini206 – 22520CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei226 – 24520Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Topological domaini246 – 33186ExtracellularSequence AnalysisAdd
BLAST
Transmembranei332 – 35625Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Topological domaini357 – 483127CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei484 – 50320Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Topological domaini504 – 51714ExtracellularSequence AnalysisAdd
BLAST
Transmembranei518 – 53720Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Topological domaini538 – 5458CytoplasmicSequence Analysis
Transmembranei546 – 56419Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Topological domaini565 – 57511ExtracellularSequence AnalysisAdd
BLAST
Transmembranei576 – 59318Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Topological domaini594 – 61219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei613 – 63220Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Topological domaini633 – 68553ExtracellularSequence AnalysisAdd
BLAST
Transmembranei686 – 71025Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Topological domaini711 – 1143433CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1144 – 116724Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1168 – 118417ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1185 – 120420Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1205 – 12128CytoplasmicSequence Analysis
Transmembranei1213 – 123523Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1236 – 125015ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1251 – 126515Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1266 – 128621CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1287 – 130620Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1307 – 139286ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1393 – 141725Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1418 – 147457CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1475 – 149319Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1494 – 150714ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1508 – 152720Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1528 – 15369CytoplasmicSequence Analysis
Transmembranei1537 – 155519Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1556 – 15638ExtracellularSequence Analysis
Transmembranei1564 – 158219Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1583 – 160119CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1602 – 162120Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1622 – 168362ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1684 – 170320Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1704 – 2336633CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon terminus Source: RGD
  2. dendritic shaft Source: RGD
  3. neuronal cell body Source: RGD
  4. neuron projection Source: RGD
  5. plasma membrane Source: RGD
  6. protein complex Source: RGD
  7. voltage-gated calcium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23362336Voltage-dependent N-type calcium channel subunit alpha-1BPRO_0000053924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Modified residuei784 – 7841PhosphoserineBy similarity
Glycosylationi1563 – 15631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
Modified residuei1719 – 17191Phosphoserine; by PKASequence Analysis

Post-translational modificationi

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ02294.
PRIDEiQ02294.

PTM databases

PhosphoSiteiQ02294.

Expressioni

Tissue specificityi

Central nervous system.

Gene expression databases

GenevestigatoriQ02294.

Interactioni

Subunit structurei

Multisubunit complex 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 RIMS1 and RIMBP2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Syt1P217072EBI-540038,EBI-458098

Protein-protein interaction databases

IntActiQ02294. 4 interactions.
MINTiMINT-102470.

Structurei

Secondary structure

1
2336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi364 – 40340Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DEXX-ray2.00B358-468[»]
ProteinModelPortaliQ02294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati82 – 359278IAdd
BLAST
Repeati469 – 713245IIAdd
BLAST
Repeati1135 – 1421287IIIAdd
BLAST
Repeati1458 – 1711254IVAdd
BLAST
Domaini1724 – 175936EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni379 – 39618Binding to the beta subunitAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2049 – 20535Poly-His
Compositional biasi2115 – 21195Poly-Ser

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

Contains 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ02294.
PhylomeDBiQ02294.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: 2 isoforms may be produced.

Isoform 1 (identifier: Q02294-1) [UniParc]FASTAAdd to Basket

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
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA
60 70 80 90 100
QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM
110 120 130 140 150
ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII
160 170 180 190 200
ALGFVFHKGS YLRNGWNVMD FVVVLTEILA TAGTDFDLRT LRAVRVLRPL
210 220 230 240 250
KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH
260 270 280 290 300
KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI
310 320 330 340 350
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL
360 370 380 390 400
VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML
410 420 430 440 450
AEEDKNAEEK SPLDAVLKRA ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA
460 470 480 490 500
RASLKSGKTE SSSYFRRKEK MFRFLIRRMV KAQSFYWVVL CVVALNTLCV
510 520 530 540 550
AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR SYFRSSFNCF
560 570 580 590 600
DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
610 620 630 640 650
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF
660 670 680 690 700
PAAILTVFQI LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT
710 720 730 740 750
LLNVFLAIAV DNLANAQELT KDEEEMEEAA NQKLALQKAK EVAEVSPMSA
760 770 780 790 800
ANISIAARQQ NSAKARSVWE QRASQLRLQN LRASCEALYS EMDPEERLRY
810 820 830 840 850
ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT EATEGADPPR
860 870 880 890 900
RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE
910 920 930 940 950
APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT
960 970 980 990 1000
APVLVPKGER RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE
1010 1020 1030 1040 1050
VAEKESNVVE GDKETRNHQP KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD
1060 1070 1080 1090 1100
EQPEDADNQR NVTRMGSQPS DPSTTVHVPV TLTGPPGEAT VVPSANTDLE
1110 1120 1130 1140 1150
GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF
1160 1170 1180 1190 1200
EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM
1210 1220 1230 1240 1250
IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK
1260 1270 1280 1290 1300
SLRVLRVLRP LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV
1310 1320 1330 1340 1350
IAVQLFKGKF FYCTDESKEL ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY
1360 1370 1380 1390 1400
DNVLWALLTL FTVSTGEGWP MVLKHSVDAT YEEQGPSPGF RMELSIFYVV
1410 1420 1430 1440 1450
YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA CIDFAISAKP
1460 1470 1480 1490 1500
LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
1510 1520 1530 1540 1550
YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT
1560 1570 1580 1590 1600
DILVTEIANN FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP
1610 1620 1630 1640 1650
YVCLLIAMLF FIYAIIGMQV FGNIALDDGT SINRHNNFRT FLQALMLLFR
1660 1670 1680 1690 1700
SATGEAWHEI MLSCLGNRAC DPHANASECG SDFAYFYFVS FIFLCSFLML
1710 1720 1730 1740 1750
NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYNDMF
1760 1770 1780 1790 1800
EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
1810 1820 1830 1840 1850
TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT
1860 1870 1880 1890 1900
VGKVYAALMI FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT
1910 1920 1930 1940 1950
QPAVLRGARV FLRQKSATSL SNGGAIQTQE SGIKESLSWG TQRTQDVLYE
1960 1970 1980 1990 2000
ARAPLERGHS AEIPVGQPGA LAVDVQMQNM TLRGPDGEPQ PGLESQGRAA
2010 2020 2030 2040 2050
SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD RPPPSQVSHH
2060 2070 2080 2090 2100
HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE
2110 2120 2130 2140 2150
RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT
2160 2170 2180 2190 2200
AALEPGPHPQ GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY
2210 2220 2230 2240 2250
KTANSSPVHF AEGQSGLPAF SPGRLSRGLS EHNALLQKEP LSQPLASGSR
2260 2270 2280 2290 2300
IGSDPYLGQR LDSEASAHNL PEDTLTFEEA VATNSGRSSR TSYVSSLTSQ
2310 2320 2330
SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC
Length:2,336
Mass (Da):262,256
Last modified:October 1, 1996 - v1
Checksum:i8D50AF67834FD1BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1538 – 15381N → D no nucleotide entry (PubMed:1692134)Curated
Sequence conflicti1579 – 15791C → L no nucleotide entry (PubMed:1692134)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92905 mRNA. Translation: AAA42014.1.
PIRiB35901.
UniGeneiRn.85880.

Genome annotation databases

UCSCiRGD:628852. rat. [Q02294-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92905 mRNA. Translation: AAA42014.1 .
PIRi B35901.
UniGenei Rn.85880.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DEX X-ray 2.00 B 358-468 [» ]
ProteinModelPortali Q02294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q02294. 4 interactions.
MINTi MINT-102470.

Chemistry

BindingDBi Q02294.
ChEMBLi CHEMBL5107.
GuidetoPHARMACOLOGYi 533.

PTM databases

PhosphoSitei Q02294.

Proteomic databases

PaxDbi Q02294.
PRIDEi Q02294.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:628852. rat. [Q02294-1 ]

Organism-specific databases

RGDi 628852. Cacna1b.

Phylogenomic databases

eggNOGi COG1226.
HOGENOMi HOG000231530.
HOVERGENi HBG050763.
InParanoidi Q02294.
PhylomeDBi Q02294.

Miscellaneous databases

PROi Q02294.

Gene expression databases

Genevestigatori Q02294.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view ]
Pfami PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view ]
PRINTSi PR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
PROSITEi PS50222. EF_HAND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of the alpha-1 subunit of an omega-conotoxin-sensitive calcium channel."
    Dubel S.J., Starr T.V.B., Hell J.W., Ahlijanian M.K., Enyeart J.J., Catterall W.A., Snutch T.P.
    Proc. Natl. Acad. Sci. U.S.A. 89:5058-5062(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1516-1679 (CLONE RBB-10).
  3. "Differential phosphorylation of two size forms of the N-type calcium channel alpha 1 subunit which have different COOH termini."
    Hell J.W., Appleyard S.M., Yokoyama C.T., Warner C., Catterall W.A.
    J. Biol. Chem. 269:7390-7396(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  4. "Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit."
    Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.
    Nature 368:67-70(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BETA-SUBUNIT BINDING DOMAIN.

Entry informationi

Entry nameiCAC1B_RAT
AccessioniPrimary (citable) accession number: Q02294
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3