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词条 Cation channel superfamily
释义

  1. Human channels with 6 TM helices

     Cation   Transient receptor potential    Canonical    Melastatin    Vanilloid    Mucolipin    Ankyrin    TRPP   Calcium   Voltage-dependent    Sperm    Ryanodine receptor   Potassium   Voltage-gated potassium    Delayed rectifier    A-type potassium    Outward-rectifying    Inwardly-rectifying    Slowly activating    Modifier/silencer    Calcium-activated    BK    SK    IK    Other subfamilies    Inward-rectifier potassium   Sodium  Cyclic nucleotide-gated  Proton  Related proteins 

  2. Human channels with 2 TM helices in each subunit

     Potassium  Tandem pore domain potassium channel 

  3. Non-human channels

      Two-pore    Pore-only potassium   Ligand-gated potassium    Voltage-gated potassium    Prokaryotic KCa   Voltage and cyclic nucleotide gated potassium    Sodium    Non-selective   Prokaryotic inward-rectifier potassium    Engineered  

  4. References

  5. External links

{{Short description|family of ion channel proteins}}{{see also|Voltage-gated ion channel}}{{Pfam_box
| Symbol = Ion_trans
| Name = Ion channel (eukaryotic)
| image =2r9r_opm.png
| width =250
| caption =Potassium channel Kv1.2 (with beta2 auxiliary subunits), structure in a membrane-like environment. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
| Pfam= PF00520
| InterPro= IPR005821
| SMART=
| Prosite =
| SCOP = 1bl8
| TCDB = 1.A.1
| OPM family= 8
| OPM protein= 2a79
| PDB={{PDB3|1qg9}}A:157-176 {{PDB3|2a79}}B:225-409 {{PDB3|1ho7}}A:378-397{{PDB3|1ho2}}A:378-397 {{PDB3|1ujl}}A:570-611
}}{{Pfam_box
| Symbol = Ion_trans_2
| Name = Ion channel (bacterial)
| image =1r3j.png
| width =250
| caption =Potassium channel KcsA. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
| Pfam= PF07885
| InterPro= IPR013099
| SMART=
| Prosite =
| SCOP = 1bl8
| TCDB =
| OPM family=
| OPM protein= 1r3j
| PDB={{PDB3|1lnq}}E:25-100 {{PDB3|2a0l}}B:169-250 {{PDB3|1orq}}C:169-250{{PDB3|1k4c}}C:34-116 {{PDB3|1r3i}}C:34-116 {{PDB3|2boc}}C:34-116{{PDB3|1j95}}C:34-116 {{PDB3|1r3l}}C:34-116 {{PDB3|1jvm}}B:34-116{{PDB3|1bl8}}C:34-116 {{PDB3|2a9h}}D:34-116 {{PDB3|1k4d}}C:34-116{{PDB3|1r3j}}C:34-116 {{PDB3|1r3k}}C:34-116 {{PDB3|2bob}}C:34-116{{PDB3|1p7b}}B:77-151
}}

The transmembrane cation channel superfamily was defined in InterPro and Pfam as the family of tetrameric ion channels. These include the sodium, potassium,[1] calcium, ryanodine receptor, HCN, CNG, CatSper, and TRP channels. This large group of ion channels apparently includes families {{TCDB|1.A.1}}, {{TCDB|1.A.2}}, {{TCDB|1.A.3}}, and {{TCDB|1.A.4}} of the TCDB transporter classification.

They are described as minimally having two transmembrane helices flanking a loop which determines the ion selectivity of the channel pore. Many eukaryotic channels have four additional transmembrane helices (TM) ({{Pfam|PF00520}}), related to or vestigial of voltage gating. The proteins with only two transmembrane helices ({{Pfam|PF07885}}) are most commonly found in bacteria. This also includes the 2-TM inward-rectifier potassium channels ({{Pfam|PF01007}}) found primarily in eukaryotes. There are commonly additional regulatory domains which serve to regulate ion conduction and channel gating. The pores may also be homotetramers or heterotetramers; where heterotetramers may be encoded as distinct genes or as multiple pore domains within a single polypeptide. The HVCN1 and Putative tyrosine-protein phosphatase proteins do not contain an expected ion conduction pore domain, but rather have homology only to the voltage sensor domain of voltage gated ion channels.

Human channels with 6 TM helices

Cation

Transient receptor potential

{{main|Transient receptor potential channel}}
Canonical
{{Main|TRPC|l1=Canonical TRP channels}}
  • TRPC1; TRPC3; TRPC4; TRPC5; TRPC6; TRPC7
Melastatin
{{Main|TRPM|l1=Melastatin TRP channels}}
  • TRPM1; TRPM2; TRPM3; TRPM4; TRPM5; TRPM6; TRPM7; TRPM8
Vanilloid
{{Main|TRPV|l1=Vanilloid TRP channels}}
  • TRPV1; TRPV2; TRPV3; TRPV4; TRPV5; TRPV6
Mucolipin
{{Main|TRPML|l1=Mucolipin TRP channels}}
  • MCOLN1; MCOLN2; MCOLN3;
Ankyrin
{{Main|TRPA (channel)|l1=Ankyrin TRP channels}}
  • TRPA1
TRPP
{{Main|TRPP|l1=Transient Receptor Potential Polycystic}}
  • PKD1L3;

Calcium

Voltage-dependent

{{Main|Voltage-dependent calcium channels}}
  • CACNA1A; CACNA1B; CACNA1C; CACNA1D; CACNA1E; CACNA1F; CACNA1G; CACNA1H; CACNA1I; CACNA1S

Sperm

{{Main|Cation channels of sperm}}
  • CATSPER1; CATSPER2; CATSPER3; CATSPER4

Ryanodine receptor

{{Main|Ryanodine receptor}}
  • RYR1; RYR2; RYR3

Potassium

Voltage-gated potassium

{{Main|Voltage-gated potassium channels}}
Delayed rectifier
  • Kvα1.x - Shaker-related: Kv1.1 (KCNA1), Kv1.2 (KCNA2), Kv1.3 (KCNA3), Kv1.5 (KCNA5), Kv1.6 (KCNA6), Kv1.7 (KCNA7), Kv1.8 (KCNA10)
  • Kvα2.x - Shab-related: Kv2.1 (KCNB1), Kv2.2 (KCNB2)
  • Kvα3.x - Shaw-related: Kv3.1 (KCNC1), Kv3.2 (KCNC2)
  • Kvα7.x: Kv7.1 (KCNQ1) - KvLQT1, Kv7.2 (KCNQ2), Kv7.3 (KCNQ3), Kv7.4 (KCNQ4), Kv7.5 (KCNQ5)
  • Kvα10.x: Kv10.1 (KCNH1)
A-type potassium
  • Kvα1.x - Shaker-related: Kv1.4 (KCNA4)
  • Kvα3.x - Shaw-related: Kv3.3 (KCNC3), Kv3.4 (KCNC4)
  • Kvα4.x - Shal-related: Kv4.1 (KCND1), Kv4.2 (KCND2), Kv4.3 (KCND3)
Outward-rectifying
  • Kvα10.x: Kv10.2 (KCNH5)
Inwardly-rectifying
  • Kvα11.x - ether-a-go-go potassium channels: Kv11.1 (KCNH2) - hERG, Kv11.2 (KCNH6), Kv11.3 (KCNH7)
Slowly activating
  • Kvα12.x: Kv12.1 (KCNH8), Kv12.2 (KCNH3), Kv12.3 (KCNH4)
Modifier/silencer
  • Kvα5.x: Kv5.1 (KCNF1)
  • Kvα6.x: Kv6.1 (KCNG1), Kv6.2 (KCNG2), Kv6.3 (KCNG3), Kv6.4 (KCNG4)
  • Kvα8.x: Kv8.1 (KCNV1), Kv8.2 (KCNV2)
  • Kvα9.x: Kv9.1 (KCNS1), Kv9.2 (KCNS2), Kv9.3 (KCNS3)

Calcium-activated

{{Main|Calcium-activated potassium channel|l1=Calcium-activated potassium channels}}
BK
{{Main|BK channel|l1=BK channels}}
  • KCa1.1 (BK, Slo1, Maxi-K, {{Gene|KCNMA1}})
SK
{{Main|SK channel|l1=SK channels}}
  • KCa2.x: KCa2.1 (KCNN1) - SK1, KCa2.2 (KCNN2) - SK2, KCa2.3 (KCNN3) - SK3
  • KCa3.x: KCa3.1 (KCNN4) - SK4
  • KCa4.x: KCa4.1 (KCNT1) - SLACK, KCa4.2 (KCNT2) - SLICK
IK
{{Main|IK channel|l1=IK channels}}
  • KCa3.1 (IKCa1, SK4, {{Gene|KCNN4}})
Other subfamilies
  • KCa5.1 (Slo3, {{Gene|KCNU1}})

Inward-rectifier potassium

{{Main|Inward-rectifier potassium ion channel}}

Sodium

  • NALCN
  • SCN1A; SCN2A; SCN2A2; SCN3A; SCN4A; SCN5A; SCN7A; SCN8A; SCN9A; SCN10A; SCN11A
  • SLC9A10; SLC9A11

Cyclic nucleotide-gated

  • CNGA1; CNGA2; CNGA3; CNGA4
  • CNGB1; CNGB3
  • HCN1; HCN2; HCN3; HCN4
  • ITPR1; ITPR2; ITPR3

Proton

  • HVCN1

Related proteins

  • TPTE, part of the larger Voltage sensitive phosphatase family

Human channels with 2 TM helices in each subunit

Potassium

Tandem pore domain potassium channel

{{Main|Tandem pore domain potassium channel}}
  • KCNK1; KCNK2; KCNK3; KCNK4; KCNK5; KCNK6; KCNK7; KCNK9; KCNK10; KCNK12; KCNK13; KCNK15; KCNK16; KCNK17; KCNK18

Non-human channels

Two-pore

{{Main|Two-pore channel|l1=Two-pore channels}}
  • TPCN1
  • TPCN2

Pore-only potassium

{{Main|Potassium channel|l1=Pore-only potassium channels}}
  • KcsA

Ligand-gated potassium

  • GluR0[2]

Voltage-gated potassium

{{Main|Voltage-gated potassium channel|l1=Voltage-gated potassium channels}}
  • KvAP[3]

Prokaryotic KCa

{{Main|Calcium-activated potassium channel#Prokaryotic KCa Channels|l1=Prokaryotic KCa channels}}
  • Kch[4][5]
  • MthK[6][7][8][9][10]
  • TrkA/TrkH[11][12]
  • KtrAB[13]
  • GsuK[14]
  • TM1088[15]

Voltage and cyclic nucleotide gated potassium

  • MlotiK1[16]

Sodium

  • NaChBac[17]
  • NaVAb[18]
  • NaVAe1[19]
  • NaVAp[20]
  • NaVMm[21]

Non-selective

  • NaK[22]

Prokaryotic inward-rectifier potassium

{{Main|Inward-rectifier potassium ion channel|l1=Inward-rectifier potassium channels}}
  • KirBac[23]

Engineered

  • NaK2CNG [24]
  • NaK2K [25]

References

1. ^{{cite journal | vauthors = Choe S | title = Potassium channel structures | journal = Nature Reviews. Neuroscience | volume = 3 | issue = 2 | pages = 115–21 | date = February 2002 | pmid = 11836519 | doi = 10.1038/nrn727 }}
2. ^{{cite journal | vauthors = Chen GQ, Cui C, Mayer ML, Gouaux E | title = Functional characterization of a potassium-selective prokaryotic glutamate receptor | journal = Nature | volume = 402 | issue = 6763 | pages = 817–21 | date = December 1999 | pmid = 10617203 | doi = 10.1038/45568 | bibcode = 1999Natur.402..817C }}
3. ^{{cite journal | vauthors = Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R | title = X-ray structure of a voltage-dependent K+ channel | journal = Nature | volume = 423 | issue = 6935 | pages = 33–41 | date = May 2003 | pmid = 12721618 | doi = 10.1038/nature01580 | bibcode = 2003Natur.423...33J }}
4. ^{{cite journal | vauthors = Milkman R | title = An Escherichia coli homologue of eukaryotic potassium channel proteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 9 | pages = 3510–4 | date = April 1994 | pmid = 8170937 | pmc = 43609 | doi = 10.1073/pnas.91.9.3510 | bibcode = 1994PNAS...91.3510M }}
5. ^{{cite journal | vauthors = Jiang Y, Pico A, Cadene M, Chait BT, MacKinnon R | title = Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel | journal = Neuron | volume = 29 | issue = 3 | pages = 593–601 | date = March 2001 | pmid = 11301020 | doi = 10.1016/s0896-6273(01)00236-7 }}
6. ^{{cite journal | vauthors = Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R | title = Crystal structure and mechanism of a calcium-gated potassium channel | journal = Nature | volume = 417 | issue = 6888 | pages = 515–22 | date = May 2002 | pmid = 12037559 | doi = 10.1038/417515a | bibcode = 2002Natur.417..515J }}
7. ^{{cite journal | vauthors = Smith FJ, Pau VP, Cingolani G, Rothberg BS | title = Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain | journal = Nature Communications | volume = 4 | pages = 2621 | year = 2013 | pmid = 24126388 | doi = 10.1038/ncomms3621 | bibcode = 2013NatCo...4E2621S }}
8. ^{{cite journal | vauthors = Ye S, Li Y, Chen L, Jiang Y | title = Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels | journal = Cell | volume = 126 | issue = 6 | pages = 1161–73 | date = September 2006 | pmid = 16990139 | doi = 10.1016/j.cell.2006.08.029 }}
9. ^{{cite journal | vauthors = Dvir H, Valera E, Choe S | title = Structure of the MthK RCK in complex with cadmium | journal = Journal of Structural Biology | volume = 171 | issue = 2 | pages = 231–7 | date = August 2010 | pmid = 20371380 | pmc = 2956275 | doi = 10.1016/j.jsb.2010.03.020 }}
10. ^{{cite journal | vauthors = Smith FJ, Pau VP, Cingolani G, Rothberg BS | title = Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation | journal = Structure | volume = 20 | issue = 12 | pages = 2038–47 | date = December 2012 | pmid = 23085076 | pmc = 3518701 | doi = 10.1016/j.str.2012.09.014 }}
11. ^{{cite journal | vauthors = Cao Y, Jin X, Huang H, Derebe MG, Levin EJ, Kabaleeswaran V, Pan Y, Punta M, Love J, Weng J, Quick M, Ye S, Kloss B, Bruni R, Martinez-Hackert E, Hendrickson WA, Rost B, Javitch JA, Rajashankar KR, Jiang Y, Zhou M | title = Crystal structure of a potassium ion transporter, TrkH | journal = Nature | volume = 471 | issue = 7338 | pages = 336–40 | date = March 2011 | pmid = 21317882 | pmc = 3077569 | doi = 10.1038/nature09731 | bibcode = 2011Natur.471..336C }}
12. ^{{cite journal | vauthors = Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M | title = Gating of the TrkH ion channel by its associated RCK protein TrkA | journal = Nature | volume = 496 | issue = 7445 | pages = 317–22 | date = April 2013 | pmid = 23598339 | pmc = 3726529 | doi = 10.1038/nature12056 | bibcode = 2013Natur.496..317C }}
13. ^{{cite journal | vauthors = Vieira-Pires RS, Szollosi A, Morais-Cabral JH | title = The structure of the KtrAB potassium transporter | journal = Nature | volume = 496 | issue = 7445 | pages = 323–8 | date = April 2013 | pmid = 23598340 | doi = 10.1038/nature12055 | bibcode = 2013Natur.496..323V }}
14. ^{{cite journal | vauthors = Kong C, Zeng W, Ye S, Chen L, Sauer DB, Lam Y, Derebe MG, Jiang Y | title = Distinct gating mechanisms revealed by the structures of a multi-ligand gated K(+) channel | journal = eLife | volume = 1 | pages = e00184 | date = December 2012 | pmid = 23240087 | pmc = 3510474 | doi = 10.7554/eLife.00184 }}
15. ^{{cite journal | vauthors = Deller MC, Johnson HA, Miller MD, Spraggon G, Elsliger MA, Wilson IA, Lesley SA | title = Crystal structure of a two-subunit TrkA octameric gating ring assembly | journal = PLoS One | volume = 10 | issue = 3 | pages = e0122512 | year = 2015 | pmid = 25826626 | pmc = 4380455 | doi = 10.1371/journal.pone.0122512 | bibcode = 2015PLoSO..1022512D }}
16. ^{{cite journal | vauthors = Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH | title = Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 5 | pages = 1511–5 | date = February 2008 | pmid = 18216238 | pmc = 2234175 | doi = 10.1073/pnas.0711533105 | bibcode = 2008PNAS..105.1511C }}
17. ^{{cite journal | vauthors = Ren D, Navarro B, Xu H, Yue L, Shi Q, Clapham DE | title = A prokaryotic voltage-gated sodium channel | journal = Science | volume = 294 | issue = 5550 | pages = 2372–5 | date = December 2001 | pmid = 11743207 | doi = 10.1126/science.1065635 | bibcode = 2001Sci...294.2372R }}
18. ^{{cite journal | vauthors = Payandeh J, Scheuer T, Zheng N, Catterall WA | title = The crystal structure of a voltage-gated sodium channel | journal = Nature | volume = 475 | issue = 7356 | pages = 353–8 | date = July 2011 | pmid = 21743477 | pmc = 3266868 | doi = 10.1038/nature10238 }}
19. ^{{cite journal | vauthors = Shaya D, Findeisen F, Abderemane-Ali F, Arrigoni C, Wong S, Nurva SR, Loussouarn G, Minor DL | title = Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels | journal = Journal of Molecular Biology | volume = 426 | issue = 2 | pages = 467–83 | date = January 2014 | pmid = 24120938 | pmc = 3947372 | doi = 10.1016/j.jmb.2013.10.010 }}
20. ^{{cite journal | vauthors = Zhang X, Ren W, DeCaen P, Yan C, Tao X, Tang L, Wang J, Hasegawa K, Kumasaka T, He J, Wang J, Clapham DE, Yan N | title = Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel | journal = Nature | volume = 486 | issue = 7401 | pages = 130–4 | date = May 2012 | pmid = 22678295 | pmc = 3979295 | doi = 10.1038/nature11054 | bibcode = 2012Natur.486..130Z }}
21. ^{{cite journal | vauthors = McCusker EC, Bagnéris C, Naylor CE, Cole AR, D'Avanzo N, Nichols CG, Wallace BA | title = Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing | journal = Nature Communications | volume = 3 | pages = 1102 | date = 2012 | pmid = 23033078 | pmc = 3493636 | doi = 10.1038/ncomms2077 | bibcode = 2012NatCo...3E1102M }}
22. ^{{cite journal | vauthors = Shi N, Ye S, Alam A, Chen L, Jiang Y | title = Atomic structure of a Na+- and K+-conducting channel | journal = Nature | volume = 440 | issue = 7083 | pages = 570–4 | date = March 2006 | pmid = 16467789 | doi = 10.1038/nature04508 | bibcode = 2006Natur.440..570S }}
23. ^{{cite journal | vauthors = Durell SR, Guy HR | title = A family of putative Kir potassium channels in prokaryotes | journal = BMC Evolutionary Biology | volume = 1 | pages = 14 | date = 2001 | pmid = 11806753 | pmc = 64639 |doi = 10.1186/1471-2148-1-14}}
24. ^{{cite journal | vauthors = Derebe MG, Sauer DB, Zeng W, Alam A, Shi N, Jiang Y | title = Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 108 | issue = 2 | pages = 598–602 | date = January 2011 | pmid = 21187421 | pmc = 3021048 | doi = 10.1073/pnas.1013636108 | bibcode = 2011PNAS..108..598D }}
25. ^{{cite journal | vauthors = Sauer DB, Zeng W, Raghunathan S, Jiang Y | title = Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 108 | issue = 40 | pages = 16634–9 | date = October 2011 | pmid = 21933962 | pmc = 3189067 | doi = 10.1073/pnas.1111688108 | bibcode = 2011PNAS..10816634S }}

External links

  • {{cite web | url = http://www.iuphar-db.org/IC/ReceptorFamiliesForward| title = Voltage-gated Ion Channels | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology }}
{{InterPro content|IPR005821}}

4 : Protein domains|Protein families|Transmembrane proteins|Ion channels
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