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P54282

- CAC1A_RAT

UniProt

P54282 - CAC1A_RAT

Protein

Voltage-dependent P/Q-type calcium channel subunit alpha-1A

Gene

Cacna1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei320 – 3201Calcium ion selectivity and permeabilityBy similarity
    Sitei670 – 6701Calcium ion selectivity and permeabilityBy similarity
    Sitei1411 – 14111Calcium ion selectivity and permeabilityBy similarity
    Sitei1600 – 16001Binds to omega-Aga-IVABy similarity
    Sitei1707 – 17071Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1791 – 180212By similarityAdd
    BLAST

    GO - Molecular functioni

    1. calmodulin binding Source: UniProtKB
    2. high voltage-gated calcium channel activity Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. voltage-gated calcium channel activity Source: UniProtKB

    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 cytosolic calcium ion concentration Source: UniProtKB
    5. sensory perception of pain Source: RGD
    6. synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    TCDBi1.A.1.11.8. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Voltage-dependent P/Q-type calcium channel subunit alpha-1A
    Alternative name(s):
    Brain calcium channel I
    Short name:
    BI
    Calcium channel, L type, alpha-1 polypeptide, isoform 4
    Rat brain class A
    Short name:
    RBA-I
    Voltage-gated calcium channel subunit alpha Cav2.1
    Gene namesi
    Name:Cacna1a
    Synonyms:Cach4, Cacn3, Cacnl1a4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2244. Cacna1a.

    Subcellular locationi

    GO - Cellular componenti

    1. perikaryon Source: RGD
    2. plasma membrane Source: RGD
    3. protein complex Source: RGD
    4. voltage-gated calcium channel complex Source: RGD

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22122212Voltage-dependent P/Q-type calcium channel subunit alpha-1APRO_0000053919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Modified residuei792 – 7921PhosphoserineBy similarity
    Glycosylationi1607 – 16071N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1773 – 17731Phosphoserine; by PKASequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP54282.
    PRIDEiP54282.

    PTM databases

    PhosphoSiteiP54282.

    Expressioni

    Tissue specificityi

    Brain specific. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. Also found in heart, in kidney distal convoluted tubule (DCT), and in pituitary.

    Gene expression databases

    GenevestigatoriP54282.

    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. Interact (via C-terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rims1Q9JIR44EBI-3507416,EBI-3507436

    Protein-protein interaction databases

    DIPiDIP-29638N.
    IntActiP54282. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP54282.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 100100CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini120 – 13819ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini157 – 16812CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini185 – 1928ExtracellularSequence Analysis
    Topological domaini212 – 23019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini251 – 33787ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini363 – 489127CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini510 – 52314ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini544 – 5518CytoplasmicSequence Analysis
    Topological domaini571 – 58010ExtracellularSequence Analysis
    Topological domaini600 – 61819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini639 – 69153ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini717 – 1190474CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1215 – 123117ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1252 – 12587CytoplasmicSequence Analysis
    Topological domaini1283 – 129311ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1312 – 133019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1351 – 143787ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1463 – 151856CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1538 – 155114ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1574 – 15807CytoplasmicSequence Analysis
    Topological domaini1601 – 16077ExtracellularSequence Analysis
    Topological domaini1627 – 164519CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1666 – 173772ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1764 – 2212449CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei101 – 11919Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei139 – 15618Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei169 – 18416Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei193 – 21119Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei231 – 25020Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei338 – 36225Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei490 – 50920Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei524 – 54320Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei552 – 57019Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei581 – 59919Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei619 – 63820Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei692 – 71625Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1191 – 121424Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1232 – 125120Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1259 – 128224Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1294 – 131118Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1331 – 135020Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1438 – 146225Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1519 – 153719Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1552 – 157322Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1581 – 160020Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1608 – 162619Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1646 – 166520Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1738 – 176326Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati87 – 365279IAdd
    BLAST
    Repeati475 – 719245IIAdd
    BLAST
    Repeati1182 – 1465284IIIAdd
    BLAST
    Repeati1502 – 1765264IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni385 – 40218Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 208Poly-Gly
    Compositional biasi729 – 7346Poly-Glu
    Compositional biasi1155 – 11584Poly-Glu
    Compositional biasi2162 – 217110Poly-His

    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

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231530.
    HOVERGENiHBG050763.
    KOiK04344.
    PhylomeDBiP54282.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005448. VDCC_P/Q_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view]
    PANTHERiPTHR10037:SF59. PTHR10037:SF59. 1 hit.
    PfamiPF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view]
    PRINTSiPR00167. CACHANNEL.
    PR01632. PQVDCCALPHA1.
    SMARTiSM01062. Ca_chan_IQ. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P54282-1) [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

    MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY     50
    KQSMAQRART MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP 100
    PFEYMILATI IANCIVLALE QHLPDDDKTP MSERLDDTEP YFIGIFCFEA 150
    GIKIVALGFA FHKGSYLRNG WNVMDFVVVL TGILATVGTE FDLRTLRAVR 200
    VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL IFAIIGLEFY 250
    MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI 300
    TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS 350
    FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK 400
    AEEVILAEDE TDVEQRHPFD GALRRATLKK SKTDLLNPEE AEDQLADIAS 450
    VGSPFARASI KSAKLENSTF FHKKERRMRF YIRRMVKTQA FYWTVLSLVA 500
    LNTLWLAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM YGLGTRPYFH 550
    SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA 600
    SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP 650
    TNFDTFPAAI MTVFQILTGE DWNEVMYDEI KSQGGVQGGM VFSIYFIVLT 700
    LFGNYTLLNV FLAIAVDNLA NAQELTKDEQ EEEEAANQKL ALQKAKEVAE 750
    VSPLSAANMS IAVKEQQKNQ KPAKSVWEQR TSEMRKQNLL ASREALYGDA 800
    AERWPTTYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR APEALRQTAR 850
    PRESARDPDA RRAWPSSPER APGREGPYGR ESEPQQREHA PPREHVPWDA 900
    DPERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA 950
    TRPARAADGE GDDGERKRRH RHGPPAHDDR ERRHRRRKES QGSGVPMSGP 1000
    NLSTTRPIQQ DLGRQDLPLA EDLDNMKNNK LATGEPASPH DSLGHSGLPP 1050
    SPAKIGNSTN PGPALATNPQ NAASRRTPNN PGNPSNPGPP KTPENSLIVT 1100
    NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN ANPDPLPKKE 1150
    EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC 1200
    ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL 1250
    GLVLHQGAYF RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR 1300
    VLRPLKTIKR LPKLKAVFDC VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF 1350
    KGKFFHCTDE SKEFERDCRG KYLLYEKNEV KARDREWKKY DFHYDNVLWA 1400
    LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI FYVVYFVVFP 1450
    FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP 1500
    QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR 1550
    VFNIVFTSLF SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE 1600
    FGNNFINLSF LRLFRAARLI KLLRQGYTIR ILLWTFVQSF KALPYVCLLI 1650
    AMLFFIYAII GMQVFGNIGI DGEDEDSDED EFQITEHNNF RTFFQALMLL 1700
    FRSATGEAWH NIMLSCLSGK PCDKNSGIQK PECGNEFAYF YFVSFIFLCS 1750
    FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY 1800
    KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA 1850
    LIRTALDIKI AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST 1900
    DLTVGKIYAA MMIMEYYRQS KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE 1950
    GGPSQNALPS TQLDPGGGLM AQESSMKESP SWVTQRAQEM FQKTGTWSPE 2000
    RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT RAASMPRLPA 2050
    ENQRRRGRPR GNNLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN 2100
    QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD 2150
    RGRPKDRKHR PHHHHHHHHH HPPAPDRERY AQERPDTGRA RAREQRWSRS 2200
    PSEGREHATH RQ 2212
    Length:2,212
    Mass (Da):251,527
    Last modified:October 1, 1996 - v1
    Checksum:iDFBD7A0F553AFA52
    GO
    Isoform 2 (identifier: P54282-2) [UniParc]FASTAAdd to Basket

    Also known as: RKC8

    The sequence of this isoform differs from the canonical sequence as follows:
         1602-1602: G → GNP

    Show »
    Length:2,214
    Mass (Da):251,739
    Checksum:iD2ED9869D22AF77F
    GO
    Isoform 3 (identifier: P54282-3)

    Also known as: RBA-65

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 4 (identifier: P54282-4)

    Sequence is not available
    Length:
    Mass (Da):

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1602 – 16021G → GNP in isoform 2. 1 PublicationVSP_000881

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64373 mRNA. Translation: AAA40806.1.
    M99222 mRNA. Translation: AAA40896.1.
    PIRiA41098.
    RefSeqiNP_037050.2. NM_012918.3.
    UniGeneiRn.87769.

    Genome annotation databases

    GeneIDi25398.
    KEGGirno:25398.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64373 mRNA. Translation: AAA40806.1 .
    M99222 mRNA. Translation: AAA40896.1 .
    PIRi A41098.
    RefSeqi NP_037050.2. NM_012918.3.
    UniGenei Rn.87769.

    3D structure databases

    ProteinModelPortali P54282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29638N.
    IntActi P54282. 2 interactions.

    Chemistry

    BindingDBi P54282.
    GuidetoPHARMACOLOGYi 532.

    Protein family/group databases

    TCDBi 1.A.1.11.8. the voltage-gated ion channel (vic) superfamily.

    PTM databases

    PhosphoSitei P54282.

    Proteomic databases

    PaxDbi P54282.
    PRIDEi P54282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25398.
    KEGGi rno:25398.

    Organism-specific databases

    CTDi 773.
    RGDi 2244. Cacna1a.

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231530.
    HOVERGENi HBG050763.
    KOi K04344.
    PhylomeDBi P54282.

    Miscellaneous databases

    NextBioi 13949997.
    PROi P54282.

    Gene expression databases

    Genevestigatori P54282.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005448. VDCC_P/Q_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view ]
    PANTHERi PTHR10037:SF59. PTHR10037:SF59. 1 hit.
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01632. PQVDCCALPHA1.
    SMARTi SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of a calcium channel that is highly expressed in the rat cerebellum."
      Starr T.V.B., Prystay W., Snutch T.P.
      Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "Molecular characterization and nephron distribution of a family of transcripts encoding the pore-forming subunit of Ca2+ channels in the kidney."
      Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.
      Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2).
      Tissue: Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3).
    4. "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
      Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
      Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABP1.

    Entry informationi

    Entry nameiCAC1A_RAT
    AccessioniPrimary (citable) accession number: P54282
    Secondary accession number(s): Q01541
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3