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Q8AYS8

- KCMA1_CHICK

UniProt

Q8AYS8 - KCMA1_CHICK

Protein

Calcium-activated potassium channel subunit alpha-1

Gene

KCNMA1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by the concentration of cytosolic Mg2+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca2+, caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).1 Publication

    Enzyme regulationi

    Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi398 – 3981MagnesiumBy similarity
    Metal bindingi421 – 4211MagnesiumBy similarity
    Metal bindingi423 – 4231MagnesiumBy similarity
    Metal bindingi913 – 9131Calcium; via carbonyl oxygenBy similarity
    Metal bindingi916 – 9161Calcium; via carbonyl oxygenBy similarity
    Metal bindingi919 – 9191CalciumBy similarity
    Metal bindingi921 – 9211CalciumBy similarity

    GO - Molecular functioni

    1. large conductance calcium-activated potassium channel activity Source: RefGenome
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. voltage-gated potassium channel activity Source: RefGenome

    GO - Biological processi

    1. potassium ion transmembrane transport Source: RefGenome

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Potassium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium-activated potassium channel subunit alpha-1
    Alternative name(s):
    BK channel
    BKCA alpha
    Calcium-activated potassium channel, subfamily M subunit alpha-1
    K(VCA)alpha
    KCa1.1
    Maxi K channel
    Short name:
    MaxiK
    Slo-alpha
    Slo1
    Slowpoke homolog
    Short name:
    Slo homolog
    Short name:
    cSlo
    Gene namesi
    Name:KCNMA1
    Synonyms:KCNMA
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. voltage-gated potassium channel complex Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11371137Calcium-activated potassium channel subunit alpha-1PRO_0000054138Add
    BLAST

    Proteomic databases

    PaxDbiQ8AYS8.
    PRIDEiQ8AYS8.

    Interactioni

    Subunit structurei

    Homotetramer; which constitutes the calcium-activated potassium channel.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P081063EBI-1635766,EBI-1636307
    akt1O575132EBI-1635766,EBI-4306384
    ANXA5P171533EBI-1635766,EBI-1635947
    ATP1B1P082513EBI-1635766,EBI-7206371
    CTTN1Q014062EBI-1635766,EBI-2530463
    GSK3BF1NPL82EBI-1635766,EBI-4306413
    HPCAL1P423243EBI-1635766,EBI-1636399
    HSPA5Q905933EBI-1635766,EBI-1635886
    HSPD1Q5ZL723EBI-1635766,EBI-1635874
    LIN7CQ5F4253EBI-1635766,EBI-1636456
    PDK1F1NLP22EBI-1635766,EBI-4306427
    PHBP841733EBI-1635766,EBI-1636878
    RAP1AF1NSA82EBI-1635766,EBI-4306330
    SNAP25P608783EBI-1635766,EBI-1637031
    SOD1P805663EBI-1635766,EBI-1637015
    STMN1P313953EBI-1635766,EBI-1636998
    VCPQ5ZMU93EBI-1635766,EBI-1637127
    YWHAGQ5F3W63EBI-1635766,EBI-1635853

    Protein-protein interaction databases

    BioGridi675104. 110 interactions.
    IntActiQ8AYS8. 107 interactions.
    MINTiMINT-7260456.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8AYS8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4444ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini66 – 13772CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini159 – 17315ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini195 – 1984CytoplasmicSequence Analysis
    Topological domaini220 – 2234ExtracellularSequence Analysis
    Topological domaini245 – 25915CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini281 – 29414ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini318 – 3269ExtracellularSequence Analysis
    Topological domaini348 – 1137790CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei295 – 31723Pore-forming; Name=P regionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei45 – 6521Helical; Name=Segment S0Sequence AnalysisAdd
    BLAST
    Transmembranei138 – 15821Helical; Name=Segment S1Sequence AnalysisAdd
    BLAST
    Transmembranei174 – 19421Helical; Name=Segment S2Sequence AnalysisAdd
    BLAST
    Transmembranei199 – 21921Helical; Name=Segment S3Sequence AnalysisAdd
    BLAST
    Transmembranei224 – 24421Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
    BLAST
    Transmembranei260 – 28021Helical; Name=Segment S5Sequence AnalysisAdd
    BLAST
    Transmembranei327 – 34721Helical; Name=Segment S6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini374 – 517144RCK N-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni515 – 53521Segment S7Add
    BLAST
    Regioni572 – 59221Segment S8Add
    BLAST
    Regioni636 – 6405Heme-binding motif
    Regioni738 – 75821Segment S9Add
    BLAST
    Regioni933 – 95321Segment S10Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi311 – 3144Selectivity for potassium
    Motifi904 – 92623Calcium bowlAdd
    BLAST

    Domaini

    The S0 segment is essential for the modulation by the accessory beta subunits.By similarity
    The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.By similarity
    The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium By similarity.By similarity
    The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ By similarity.By similarity
    The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site. There are however other Ca2+ sensors regions required for activation of the channel By similarity.By similarity
    The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation By similarity.By similarity

    Sequence similaritiesi

    Contains 1 RCK N-terminal domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOVERGENiHBG052222.
    InParanoidiQ8AYS8.
    KOiK04936.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    IPR003148. RCK_N.
    [Graphical view]
    PfamiPF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02254. TrkA_N. 1 hit.
    [Graphical view]
    PRINTSiPR01449. BKCHANNELA.
    PR00169. KCHANNEL.

    Sequences (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q8AYS8-1) [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

    MSNNINANNL NTDSSSSPVN VPKMDALIIP VTMEVPCDSR GQRMWWAFLA     50
    SSMVTFFGGL FIILLWRTLK YLWTVCCHCG VKNKEAQKIN GGGDTQADGA 100
    CKPTDEKEEN VAAEVGWMTS VKDWAGVMIS AQTLTGRVLV VLVFALSIGA 150
    LVIYFIDSSN PIESCQNFYK DFTLQIDMAF NVFFLLYFGL RFIAANDKLW 200
    FWLEVNSVVD FFTVPPVFVS VYLNRSWLGL RFLRALRLIQ FSEILQFLNI 250
    LKTSNSIKLV NLCSIFISTW LTAAGFIHLV ENSGDPWENF QNNQQLTYWE 300
    CVYLLMVTMS TVGYGDVYAK TTLGRLFMVF FILGGLAMFA SYVPEIIELI 350
    GNRKKYGGSY SAVSGRKHIV VCGHITLESV SNFLKDFLHK DRDDVNVEIV 400
    FLHNISPNLE LEALFKRHFT QVEFYQGSVL NPHDLARVKI ESADACLILA 450
    NKYCADPDAE DASNIMRVIS IKNYHPKIRI ITQMLQYHNK AHLLNIPSWN 500
    WKEGDDAICL AELKLGFIAQ SCLAPGLSTM LANLFSMRSF IKIEEDTWQK 550
    YYLEGVANEM YTEYLSSAFV GLSFPAVCEL VFAKLKLLMI AIEYKSEKRE 600
    SSILINPGNH VKIQEGTLGF FIASDAKEVK RAFFYCKACH DDITDPKRIK 650
    KCGCKRLEDE QPSTLSPKKK QRNGGMRNSP NSSPKLMRHD PLLIPGNEQI 700
    DNMDANVKKY DSTGMFHWCP AKDIEKVILT RSEAAMTVLS GHVVVCIFGD 750
    VKSALIGLRN LVMPLRASNF HYHELKHIVF VGSLEYLRRE WETLHNFPKV 800
    SILPGTPLSR ADLRAVNINL CDMCVILSAN QNNIDDASLQ DKECILASLN 850
    IKSMQFDDSI GVLQANSQGF TPPGMDRSSP DNSPVHGLLR QPSITTGANI 900
    PIITELVNDS NVQFLDQDDD DDPDTELYLT QPFACGTAFA VSVLDSLMSA 950
    TYFNDNILTL IRTLVTGGAT PELEALIAEE NALRGGYSTP QTLANRDRCR 1000
    VAQLALYDGP FADLGDGGCY GDLFCKALKT YNMLCFGIYR LRDAHLSTPS 1050
    QCTKRYVITN PPYEFELVPT DLIFCLMQFD HNAGQSRASL SHSSHSSYSS 1100
    SKKSSSVHSI PSTANRPNRT KTRDSREKQK YVQEDRL 1137
    Length:1,137
    Mass (Da):127,647
    Last modified:April 13, 2004 - v2
    Checksum:i40A9735E586F0BD1
    GO
    Isoform 2 (identifier: Q8AYS8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         602-602: S → RSRKR

    Show »
    Length:1,141
    Mass (Da):128,243
    Checksum:i60A2C0EAB0534269
    GO
    Isoform 3 (identifier: Q8AYS8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         657-657: L → PKMSIYKRMKLACCFDCGRSERDCSCMSGSVHSNMDTLERAFPLSSVSVNDCSTSLRAF

    Show »
    Length:1,195
    Mass (Da):134,076
    Checksum:i6AAD8F835A7A8177
    GO
    Isoform 4 (identifier: Q8AYS8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1130-1137: KYVQEDRL → NSTRMNRMGQEKKWFTDEPDNAYPRNIQIKPMSTHMANQINQYKSTSSLIPPIREVEDEC

    Show »
    Length:1,189
    Mass (Da):133,667
    Checksum:iB334AAB3F4714EED
    GO
    Isoform 5 (identifier: Q8AYS8-5) [UniParc]FASTAAdd to Basket

    Also known as: IK

    The sequence of this isoform differs from the canonical sequence as follows:
         906-906: L → LAKPGKLLPLVSISQEKNSGTQILMITEL

    Show »
    Length:1,165
    Mass (Da):130,638
    Checksum:i905BB9D1B2344E58
    GO
    Isoform 6 (identifier: Q8AYS8-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         657-657: L → IYF

    Show »
    Length:1,139
    Mass (Da):127,957
    Checksum:i45822D895211C704
    GO
    Isoform 7 (identifier: Q8AYS8-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MSNNINANNLNTDSSSS → MKPFEVSLPPPPPS

    Show »
    Length:1,134
    Mass (Da):127,387
    Checksum:i40B414AEFE0F1B55
    GO
    Isoform 8 (identifier: Q8AYS8-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-160: N → KSRTADSLI

    Show »
    Length:1,145
    Mass (Da):128,505
    Checksum:iC27FD559A611453C
    GO
    Isoform 9 (identifier: Q8AYS8-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         602-602: S → RSRKRYALFVTFPSNLNPTST

    Show »
    Length:1,157
    Mass (Da):129,997
    Checksum:i6284CAE9979B4A00
    GO
    Isoform 10 (identifier: Q8AYS8-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         687-687: M → MRFSCPFLP

    Show »
    Length:1,145
    Mass (Da):128,595
    Checksum:i61A433CB6C95073E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961Q → R in AAC60378. (PubMed:9178544)Curated
    Sequence conflicti397 – 3971V → I in AAC60378. (PubMed:9178544)Curated
    Sequence conflicti409 – 4091L → P in AAC35370. (PubMed:10362660)Curated
    Sequence conflicti522 – 5221C → S in AAC60378. (PubMed:9178544)Curated
    Sequence conflicti712 – 7121S → W in BAC20639. (PubMed:8755483)Curated
    Sequence conflicti937 – 9371T → P in BAC20639. (PubMed:8755483)Curated
    Sequence conflicti941 – 9411V → D in BAC20639. (PubMed:8755483)Curated
    Sequence conflicti1034 – 10341L → F in AAC35370. (PubMed:10362660)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717MSNNI…DSSSS → MKPFEVSLPPPPPS in isoform 7. 1 PublicationVSP_009983Add
    BLAST
    Alternative sequencei160 – 1601N → KSRTADSLI in isoform 8. 1 PublicationVSP_009984
    Alternative sequencei602 – 6021S → RSRKR in isoform 2. 1 PublicationVSP_009985
    Alternative sequencei602 – 6021S → RSRKRYALFVTFPSNLNPTS T in isoform 9. 1 PublicationVSP_009986
    Alternative sequencei657 – 6571L → PKMSIYKRMKLACCFDCGRS ERDCSCMSGSVHSNMDTLER AFPLSSVSVNDCSTSLRAF in isoform 3. 2 PublicationsVSP_009987
    Alternative sequencei657 – 6571L → IYF in isoform 6. 1 PublicationVSP_009988
    Alternative sequencei687 – 6871M → MRFSCPFLP in isoform 10. 1 PublicationVSP_009989
    Alternative sequencei906 – 9061L → LAKPGKLLPLVSISQEKNSG TQILMITEL in isoform 5. 2 PublicationsVSP_009990
    Alternative sequencei1130 – 11378KYVQEDRL → NSTRMNRMGQEKKWFTDEPD NAYPRNIQIKPMSTHMANQI NQYKSTSSLIPPIREVEDEC in isoform 4. 1 PublicationVSP_009991

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23821 mRNA. Translation: AAC60378.1.
    U23823 mRNA. Translation: AAC60125.1.
    U73189 mRNA. Translation: AAB17873.1.
    AF087663 mRNA. Translation: AAC35370.1.
    AB072618 mRNA. Translation: BAC20639.1.
    RefSeqiNP_989555.1. NM_204224.1.
    UniGeneiGga.3260.

    Genome annotation databases

    GeneIDi374065.
    KEGGigga:374065.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23821 mRNA. Translation: AAC60378.1 .
    U23823 mRNA. Translation: AAC60125.1 .
    U73189 mRNA. Translation: AAB17873.1 .
    AF087663 mRNA. Translation: AAC35370.1 .
    AB072618 mRNA. Translation: BAC20639.1 .
    RefSeqi NP_989555.1. NM_204224.1.
    UniGenei Gga.3260.

    3D structure databases

    ProteinModelPortali Q8AYS8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 675104. 110 interactions.
    IntActi Q8AYS8. 107 interactions.
    MINTi MINT-7260456.

    Proteomic databases

    PaxDbi Q8AYS8.
    PRIDEi Q8AYS8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 374065.
    KEGGi gga:374065.

    Organism-specific databases

    CTDi 3778.

    Phylogenomic databases

    eggNOGi COG1226.
    HOVERGENi HBG052222.
    InParanoidi Q8AYS8.
    KOi K04936.

    Miscellaneous databases

    NextBioi 20813586.
    PROi Q8AYS8.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    IPR003148. RCK_N.
    [Graphical view ]
    Pfami PF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02254. TrkA_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01449. BKCHANNELA.
    PR00169. KCHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "CSlo encodes calcium-activated potassium channels in the chick's cochlea."
      Jiang G.J., Zidanic M., Michaels R.L., Michael T.H., Griguer C., Fuchs P.A.
      Proc. R. Soc. B 264:731-737(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE OF 398-1137 (ISOFORM 4).
      Strain: Leghorn.
      Tissue: Cochlear duct.
    2. "Distribution of Ca2+-activated K+ channel isoforms along the tonotopic gradient of the chicken's cochlea."
      Rosenblatt K.P., Sun Z.-P., Heller S., Hudspeth A.J.
      Neuron 19:1061-1075(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9 AND 10).
      Strain: White leghorn.
      Tissue: Brain.
    3. "Molecular biology and electrophysiology of calcium-activated potassium channels from lens epithelium."
      Rae J.L., Shepard A.R.
      Curr. Eye Res. 17:264-275(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: White leghorn.
      Tissue: Lens epithelium.
    4. "Characterization of a newly found stretch-activated KCa,ATP channel in cultured chick ventricular myocytes."
      Kawakubo T., Naruse K., Matsubara T., Hotta N., Sokabe M.
      Am. J. Physiol. 276:H1827-H1838(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-1137 (ISOFORM 3).
    5. "Posttranslational regulation of Ca(2+)-activated K+ currents by a target-derived factor in developing parasympathetic neurons."
      Subramony P., Raucher S., Dryer L., Dryer S.E.
      Neuron 17:115-124(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 710-973 (ISOFORM 5).
    6. "A molecular mechanism for electrical tuning of cochlear hair cells."
      Ramanathan K., Michael T.H., Jiang G.-J., Hiel H., Fuchs P.A.
      Science 283:215-217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiKCMA1_CHICK
    AccessioniPrimary (citable) accession number: Q8AYS8
    Secondary accession number(s): O12942
    , O13110, O93569, Q98951, Q9PS76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The protein was initially thought to contain two functionally distinct parts: The core channel (from the N-terminus to the S9 segment) that mediates the channel activity, and the cytoplasmic tail (from the S9 segment to the C-terminus) that mediates the calcium sensing. The situation is however more complex, since the core channel contains binding sites for Ca2+ and Mg2+.

    Caution

    It is uncertain whether Met-1 is the initiator or if the sequence starts further upstream.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3