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Q02294

- CAC1B_RAT

UniProt

Q02294 - CAC1B_RAT

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 binding Source: UniProtKB
    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

    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

    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

    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 – 40340

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9595CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini115 – 13319ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini152 – 16413CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini180 – 1867ExtracellularSequence Analysis
    Topological domaini206 – 22520CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini246 – 33186ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini357 – 483127CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini504 – 51714ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini538 – 5458CytoplasmicSequence Analysis
    Topological domaini565 – 57511ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini594 – 61219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini633 – 68553ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini711 – 1143433CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1168 – 118417ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1205 – 12128CytoplasmicSequence Analysis
    Topological domaini1236 – 125015ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1266 – 128621CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1307 – 139286ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1418 – 147457CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1494 – 150714ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1528 – 15369CytoplasmicSequence Analysis
    Topological domaini1556 – 15638ExtracellularSequence Analysis
    Topological domaini1583 – 160119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1622 – 168362ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1704 – 2336633CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei96 – 11419Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei134 – 15118Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei165 – 17915Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei187 – 20519Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei226 – 24520Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei332 – 35625Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei484 – 50320Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei518 – 53720Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei546 – 56419Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei576 – 59318Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei613 – 63220Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei686 – 71025Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1144 – 116724Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1185 – 120420Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1213 – 123523Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1251 – 126515Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1287 – 130620Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1393 – 141725Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1475 – 149319Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1508 – 152720Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1537 – 155519Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1564 – 158219Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1602 – 162120Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1684 – 170320Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    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.
    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

    MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA     50
    QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM 100
    ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII 150
    ALGFVFHKGS YLRNGWNVMD FVVVLTEILA TAGTDFDLRT LRAVRVLRPL 200
    KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH 250
    KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI 300
    LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL 350
    VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML 400
    AEEDKNAEEK SPLDAVLKRA ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA 450
    RASLKSGKTE SSSYFRRKEK MFRFLIRRMV KAQSFYWVVL CVVALNTLCV 500
    AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR SYFRSSFNCF 550
    DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV 600
    VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF 650
    PAAILTVFQI LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT 700
    LLNVFLAIAV DNLANAQELT KDEEEMEEAA NQKLALQKAK EVAEVSPMSA 750
    ANISIAARQQ NSAKARSVWE QRASQLRLQN LRASCEALYS EMDPEERLRY 800
    ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT EATEGADPPR 850
    RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE 900
    APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT 950
    APVLVPKGER RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE 1000
    VAEKESNVVE GDKETRNHQP KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD 1050
    EQPEDADNQR NVTRMGSQPS DPSTTVHVPV TLTGPPGEAT VVPSANTDLE 1100
    GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF 1150
    EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM 1200
    IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK 1250
    SLRVLRVLRP LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV 1300
    IAVQLFKGKF FYCTDESKEL ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY 1350
    DNVLWALLTL FTVSTGEGWP MVLKHSVDAT YEEQGPSPGF RMELSIFYVV 1400
    YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA CIDFAISAKP 1450
    LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE 1500
    YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT 1550
    DILVTEIANN FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP 1600
    YVCLLIAMLF FIYAIIGMQV FGNIALDDGT SINRHNNFRT FLQALMLLFR 1650
    SATGEAWHEI MLSCLGNRAC DPHANASECG SDFAYFYFVS FIFLCSFLML 1700
    NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYNDMF 1750
    EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR 1800
    TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT 1850
    VGKVYAALMI FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT 1900
    QPAVLRGARV FLRQKSATSL SNGGAIQTQE SGIKESLSWG TQRTQDVLYE 1950
    ARAPLERGHS AEIPVGQPGA LAVDVQMQNM TLRGPDGEPQ PGLESQGRAA 2000
    SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD RPPPSQVSHH 2050
    HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE 2100
    RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT 2150
    AALEPGPHPQ GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY 2200
    KTANSSPVHF AEGQSGLPAF SPGRLSRGLS EHNALLQKEP LSQPLASGSR 2250
    IGSDPYLGQR LDSEASAHNL PEDTLTFEEA VATNSGRSSR TSYVSSLTSQ 2300
    SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC 2336
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M92905 mRNA. Translation: AAA42014.1 .
    PIRi B35901.
    UniGenei Rn.85880.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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: October 1, 2014
    This is version 129 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