KCNA5

Natrijev naponski vođeni kanal, član 5 potporodice povezane sa šejkerom, također poznat kao KCNA5 ili K_v1.5, jest protein koji je kod ljudi kodiran genom KCNA5 sa hromosoma 12.^[5]

KCNA5
Identifikatori
Aliasi	KCNA5
Vanjski ID-jevi	OMIM: 176267 MGI: 96662 HomoloGene: 1683 GeneCards: KCNA5
Lokacija gena (čovjek) Hrom. Hromosom 12 (čovjek)[1] Bend 12p13.32 Početak 5,043,879 bp[1] Kraj 5,046,788 bp[1]
Lokacija gena (miš) Hrom. Hromosom 6 (miš)[2] Bend 6 F3|6 61.35 cM Početak 126,509,514 bp[2] Kraj 126,512,375 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • potassium channel inhibitor activity • outward rectifier potassium channel activity • potassium channel activity • scaffold protein binding • voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization • voltage-gated potassium channel activity involved in SA node cell action potential repolarization • delayed rectifier potassium channel activity • voltage-gated potassium channel activity involved in bundle of His cell action potential repolarization • voltage-gated ion channel activity • ion channel activity • GO:0001948, GO:0016582 vezivanje za proteine • alpha-actinin binding • voltage-gated potassium channel activity • signaling receptor binding • protein kinase binding Ćelijska komponenta • integral component of membrane • Golđijev aparat • membrana • Interkalirani disk • intracellular canaliculus • voltage-gated potassium channel complex • ćelijska membrana • integral component of plasma membrane • potassium channel complex • Z disc • Endoplazmatski retikulum • perinuklearno područje citoplazme • Kaveole • Lipidni splav • cell surface Biološki proces • Notch signaling pathway • regulation of atrial cardiac muscle cell membrane repolarization • positive regulation of myoblast proliferation • regulation of potassium ion transport • response to hypoxia • membrane hyperpolarization • regulation of insulin secretion • response to hyperoxia • regulation of membrane potential • regulation of ion transmembrane transport • response to mechanical stimulus • ion transport • response to organic substance • membrane repolarization during bundle of His cell action potential • positive regulation of G1/S transition of mitotic cell cycle • potassium ion transport • regulation of vasoconstriction • potassium ion homeostasis • protein complex oligomerization • transmembrane transport • potassium ion transmembrane transport • negative regulation of potassium ion transport • atrial cardiac muscle cell action potential • membrane repolarization during SA node cell action potential • regulation of heart rate by cardiac conduction • protein homooligomerization • response to hydrogen peroxide • negative regulation of cytosolic calcium ion concentration • membrane repolarization during atrial cardiac muscle cell action potential • regulation of molecular function • GO:0015915 transport • potassium ion export across plasma membrane Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	3741	16493
Ensembl	ENSG00000130037	ENSMUSG00000045534
UniProt	P22460	Q61762
RefSeq (mRNK)	NM_002234	NM_145983
RefSeq (bjelančevina)	NP_002225	NP_666095
Lokacija (UCSC)	Chr 12: 5.04 – 5.05 Mb	Chr 6: 126.51 – 126.51 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 613 aminokiselina, a molekulska težina Da.^[5]

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MEIALVPLEN		GGAMTVRGGD		EARAGCGQAT		GGELQCPPTA		GLSDGPKEPA
PKGRGAQRDA		DSGVRPLPPL		PDPGVRPLPP		LPEELPRPRR		PPPEDEEEEG
DPGLGTVEDQ		ALGTASLHHQ		RVHINISGLR		FETQLGTLAQ		FPNTLLGDPA
KRLRYFDPLR		NEYFFDRNRP		SFDGILYYYQ		SGGRLRRPVN		VSLDVFADEI
RFYQLGDEAM		ERFREDEGFI		KEEEKPLPRN		EFQRQVWLIF		EYPESSGSAR
AIAIVSVLVI		LISIITFCLE		TLPEFRDERE		LLRHPPAPHQ		PPAPAPGANG
SGVMAPPSGP		TVAPLLPRTL		ADPFFIVETT		CVIWFTFELL		VRFFACPSKA
GFSRNIMNII		DVVAIFPYFI		TLGTELAEQQ		PGGGGGGQNG		QQAMSLAILR
VIRLVRVFRI		FKLSRHSKGL		QILGKTLQAS		MRELGLLIFF		LFIGVILFSS
AVYFAEADNQ		GTHFSSIPDA		FWWAVVTMTT		VGYGDMRPIT		VGGKIVGSLC
AIAGVLTIAL		PVPVIVSNFN		YFYHRETDHE		EPAVLKEEQG		TQSQGPGLDR
GVQRKVSGSR		GSFCKAGGTL		ENADSARRGS		CPLEKCNVKA		KSNVDLRRSL
YALCLDTSRE		TDL

Funkcija

Kalijski kanali predstavljaju najkompleksniju klasu ionskih kanala sa naponom i sa funkcionalnog i sa strukturnog stanovišta. KCNA5 kodira člana potporodice kalijevih kanala, naponski vođenih, povezanih sa šejkerom. Ovaj član sadrži šest domena koje se protežu kroz membranu sa ponavljanjem tipa šejker u četvrtom segmentu. Spada u klasu odloženih ispravljača, čija funkcija može vratiti membranski potencijal beta-ćelija nakon depolarizacije, čime bi doprinijela regulaciji lučenja insulina. Ovaj gen je intronski manji, a gen je grupiran sa genima KCNA1 i KCNA6 na hromosomu 12.^[5] Mutacije u ovom genu imaju povezan i sa pretkomorskom fibrilacijom^[6] i sa iznenadnom srčanom smrću.^[7] KCNA5 su također ključni faktori u plućnoj vaskularnoj funkciji, gdje imaju ulogu u postavljanju membranskog potencijala u mirovanju i njenom uključivanju tokom hipoksjskih plućnih vazokonstrikcija.

Interakcije

Pokazalo se da KCNA5 reaguje sa DLG4,^[8][9] PDZ domain-containing proteins such as SAP97,^[10] i aktininom alfa-2.^[8][11]

Također pogledajte

• Naponski-vođeni natrijski kanal

Reference

1. GRCh38: Ensembl release 89: ENSG00000130037 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000045534 - Ensembl, maj 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
6. Olson TM, Alekseev AE, Liu XK, Park S, Zingman LV, Bienengraeber M, Sattiraju S, Ballew JD, Jahangir A, Terzic A (Jul 2006). "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Human Molecular Genetics. 15 (14): 2185–91. doi:10.1093/hmg/ddl143. PMID 16772329.
7. Nielsen NH, Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, Bentzen BH, Sigurd B, Larsen LA, Andersen PS, Haunsø S, Kjeldsen K, Grunnet M, Christiansen M, Olesen SP (Mar 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochemical and Biophysical Research Communications. 354 (3): 776–82. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934.
8. Eldstrom J, Choi WS, Steele DF, Fedida D (Jul 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Letters. 547 (1–3): 205–11. doi:10.1016/S0014-5793(03)00668-9. PMID 12860415. S2CID 34857270.
9. Eldstrom J, Doerksen KW, Steele DF, Fedida D (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters. 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. S2CID 40689829.
10. Murata, Mitsunobu; Buckett, Peter D.; Zhou, Jun; Brunner, Michael; Folco, Eduardo; Koren, Gideon (1. 12. 2001). "SAP97 interacts with Kv1.5 in heterologous expression systems". American Journal of Physiology. Heart and Circulatory Physiology (jezik: engleski). 281 (6): H2575–H2584. doi:10.1152/ajpheart.2001.281.6.H2575. ISSN 0363-6135. PMID 11709425. S2CID 28915450.
11. Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D (maj 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072. S2CID 13026110.

Dopunska literatura

• Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X (Dec 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacological Reviews. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. S2CID 219195192.
• Curran ME, Landes GM, Keating MT (Apr 1992). "Molecular cloning, characterization, and genomic localization of a human potassium channel gene". Genomics. 12 (4): 729–37. doi:10.1016/0888-7543(92)90302-9. PMID 1349297.
• Philipson LH, Hice RE, Schaefer K, LaMendola J, Bell GI, Nelson DJ, Steiner DF (Jan 1991). "Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel". Proceedings of the National Academy of Sciences of the United States of America. 88 (1): 53–7. Bibcode:1991PNAS...88...53P. doi:10.1073/pnas.88.1.53. PMC 50746. PMID 1986382.
• Tamkun MM, Knoth KM, Walbridge JA, Kroemer H, Roden DM, Glover DM (Mar 1991). "Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle". FASEB Journal. 5 (3): 331–7. doi:10.1096/fasebj.5.3.2001794. PMID 2001794. S2CID 23737559.
• Mays DJ, Foose JM, Philipson LH, Tamkun MM (Jul 1995). "Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue". The Journal of Clinical Investigation. 96 (1): 282–92. doi:10.1172/JCI118032. PMC 185199. PMID 7615797.
• Crumb WJ, Wible B, Arnold DJ, Payne JP, Brown AM (Jan 1995). "Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity". Molecular Pharmacology. 47 (1): 181–90. PMID 7838127.
• Phromchotikul T, Browne DL, Curran ME, Keating MT, Litt M (Sep 1993). "Dinucleotide repeat polymorphism at the KCNA5 locus". Human Molecular Genetics. 2 (9): 1512. doi:10.1093/hmg/2.9.1512-a. PMID 8242092.
• Albrecht B, Weber K, Pongs O (1996). "Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13". Receptors & Channels. 3 (3): 213–20. PMID 8821794.
• Holmes TC, Fadool DA, Ren R, Levitan IB (Dec 1996). "Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain". Science. 274 (5295): 2089–91. Bibcode:1996Sci...274.2089H. doi:10.1126/science.274.5295.2089. PMID 8953041.
• Lacerda AE, Roy ML, Lewis EW, Rampe D (Aug 1997). "Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart". Molecular Pharmacology. 52 (2): 314–22. doi:10.1124/mol.52.2.314. PMID 9271355.
• Kääb S, Dixon J, Duc J, Ashen D, Näbauer M, Beuckelmann DJ, Steinbeck G, McKinnon D, Tomaselli GF (Oct 1998). "Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density". Circulation. 98 (14): 1383–93. doi:10.1161/01.cir.98.14.1383. PMID 9760292.
• Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D (maj 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072. S2CID 13026110.
• Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A (Aug 2000). "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon". The EMBO Journal. 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. PMC 306594. PMID 10921884.
• Nitabach MN, Llamas DA, Araneda RC, Intile JL, Thompson IJ, Zhou YI, Holmes TC (Jan 2001). "A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors". Proceedings of the National Academy of Sciences of the United States of America. 98 (2): 705–10. doi:10.1073/pnas.031446198. PMC 14652. PMID 11149959.
• Cukovic D, Lu GW, Wible B, Steele DF, Fedida D (Jun 2001). "A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2". FEBS Letters. 498 (1): 87–92. doi:10.1016/S0014-5793(01)02505-4. PMID 11389904. S2CID 20622483.
• Kurata HT, Soon GS, Eldstrom JR, Lu GW, Steele DF, Fedida D (Aug 2002). "Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels". The Journal of Biological Chemistry. 277 (32): 29045–53. doi:10.1074/jbc.M111470200. PMID 12021261.
• Williams CP, Hu N, Shen W, Mashburn AB, Murray KT (Aug 2002). "Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit". The Journal of Pharmacology and Experimental Therapeutics. 302 (2): 545–50. doi:10.1124/jpet.102.033357. PMID 12130714. S2CID 34085749.
• Eldstrom J, Doerksen KW, Steele DF, Fedida D (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters. 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. S2CID 40689829.
• Zhang S, Kurata HT, Kehl SJ, Fedida D (Mar 2003). "Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition". The Journal of General Physiology. 121 (3): 215–25. doi:10.1085/jgp.20028760. PMC 2217332. PMID 12601085.

Vanjski linkovi

• Kv1.5 Potassium Channel na US National Library of Medicine Medical Subject Headings (MeSH)
• KCNA5 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.