Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Small conductance calcium-activated potassium channel protein 3

Gene

Kcnn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_315822. Ca2+ activated K+ channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Small conductance calcium-activated potassium channel protein 3
Short name:
SK3
Short name:
SKCa 3
Short name:
SKCa3
Alternative name(s):
KCa2.3
Gene namesi
Name:Kcnn3
Synonyms:Sk3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2153183. Kcnn3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei289 – 30921Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei316 – 33621Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei367 – 38721Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei406 – 42621Helical; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei455 – 47521Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Intramembranei495 – 51521Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Transmembranei524 – 54421Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • filopodium Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • neuromuscular junction Source: Ensembl
  • neuronal cell body Source: GO_Central
  • neuron projection Source: Ensembl
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Small conductance calcium-activated potassium channel protein 3PRO_0000155014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei310 – 3101PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP58391.
PRIDEiP58391.

PTM databases

PhosphoSiteiP58391.

Expressioni

Tissue specificityi

Expressed at low levels in atrial and ventricular myocytes (at protein level).1 Publication

Interactioni

Subunit structurei

Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity).By similarity

Protein-protein interaction databases

IntActiP58391. 2 interactions.
MINTiMINT-4099712.
STRINGi10090.ENSMUSP00000000811.

Structurei

3D structure databases

ProteinModelPortaliP58391.
SMRiP58391. Positions 545-675.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni562 – 63877Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 6143Pro-richAdd
BLAST
Compositional biasi30 – 9566Gln-richAdd
BLAST
Compositional biasi684 – 6885Poly-Gln
Compositional biasi728 – 7314Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP58391.
KOiK04944.
OMAiVYNALFY.
OrthoDBiEOG73FQMC.
PhylomeDBiP58391.
TreeFamiTF315015.

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.

Sequencei

Sequence statusi: Complete.

P58391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQPPPPP APPAVPQQPP
60 70 80 90 100
GPLLQPQPPQ PQQQQSQQQQ QQQSQQQQQQ APLHPLPQLA QLQSQLVHPG
110 120 130 140 150
LLHSSPTAFR APTSANSTAI LHPSSRQGSQ LNLNDHLLGH SPSSTATSGP
160 170 180 190 200
GGGSRHRQAS PLVHRRDSNP FTEIAMSSCK YSGGVMKPLS RLSASRRNLI
210 220 230 240 250
EAEPEGQPLQ LFSPSNPPEI IISSREDNHA HQTLLHHPNA THNHQHAGTT
260 270 280 290 300
AGSTTFPKAN KRKNQNIGYK LGHRRALFEK RKRLSDYALI FGMFGIVVMV
310 320 330 340 350
IETELSWGLY SKDSMFSLAL KCLISLSTVI LLGLIIAYHT REVQLFVIDN
360 370 380 390 400
GADDWRIAMT YERILYISLE MLVCAIHPIP GEYKFFWTAR LAFSYTPSRA
410 420 430 440 450
EADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA LNKINFNTRF
460 470 480 490 500
VMKTLMTICP GTVLLVFSIS LWIIAAWTVR VCERYHDQQD VTSNFLGAMW
510 520 530 540 550
LISITFLSIG YGDMVPHTYC GKGVCLLTGI MGAGCTALVV AVVARKLELT
560 570 580 590 600
KAEKHVHNFM MDTQLTKRIK NAAANVLRET WLIYKHTKLL KKIDHAKVRK
610 620 630 640 650
HQRKFLQAIH QLRGVKMEQR KLSDQANTLV DLSKMQNVMY DLITELNDRS
660 670 680 690 700
EDLEKQIGSL ESKLEHLTAS FNSLPLLIAD TLRQQQQQLL TAFVEARGIS
710 720 730
VAVGTSHAPP SDSPIGISST SFPTPYTSSS SC
Length:732
Mass (Da):81,333
Last modified:October 16, 2013 - v2
Checksum:i62347E83FFE9DC9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801Missing in AAK48902 (PubMed:11557517).Curated
Sequence conflicti365 – 3651L → F in AAK48902 (PubMed:11557517).Curated
Sequence conflicti574 – 5741A → T in AAK48902 (PubMed:11557517).Curated
Sequence conflicti583 – 5831I → V in AAK48902 (PubMed:11557517).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF357241 mRNA. Translation: AAK48902.1.
AK137738 mRNA. Translation: BAE23484.1.
AC166364 Genomic DNA. No translation available.
AC171273 Genomic DNA. No translation available.
BC106769 mRNA. Translation: AAI06770.1.
BC106770 mRNA. Translation: AAI06771.1.
CCDSiCCDS38495.1.
RefSeqiNP_536714.2. NM_080466.2.
UniGeneiMm.120250.

Genome annotation databases

EnsembliENSMUST00000000811; ENSMUSP00000000811; ENSMUSG00000000794.
GeneIDi140493.
KEGGimmu:140493.
UCSCiuc012cso.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF357241 mRNA. Translation: AAK48902.1.
AK137738 mRNA. Translation: BAE23484.1.
AC166364 Genomic DNA. No translation available.
AC171273 Genomic DNA. No translation available.
BC106769 mRNA. Translation: AAI06770.1.
BC106770 mRNA. Translation: AAI06771.1.
CCDSiCCDS38495.1.
RefSeqiNP_536714.2. NM_080466.2.
UniGeneiMm.120250.

3D structure databases

ProteinModelPortaliP58391.
SMRiP58391. Positions 545-675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP58391. 2 interactions.
MINTiMINT-4099712.
STRINGi10090.ENSMUSP00000000811.

PTM databases

PhosphoSiteiP58391.

Proteomic databases

PaxDbiP58391.
PRIDEiP58391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000811; ENSMUSP00000000811; ENSMUSG00000000794.
GeneIDi140493.
KEGGimmu:140493.
UCSCiuc012cso.1. mouse.

Organism-specific databases

CTDi3782.
MGIiMGI:2153183. Kcnn3.

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP58391.
KOiK04944.
OMAiVYNALFY.
OrthoDBiEOG73FQMC.
PhylomeDBiP58391.
TreeFamiTF315015.

Enzyme and pathway databases

ReactomeiREACT_315822. Ca2+ activated K+ channels.

Miscellaneous databases

NextBioi369816.
PROiP58391.
SOURCEiSearch...

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular properties of small-conductance Ca2+-activated K+ channels expressed in murine colonic smooth muscle."
    Ro S., Hatton W.J., Koh S.D., Horowitz B.
    Am. J. Physiol. 281:G964-G973(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Colon.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Differential expression of small-conductance Ca2+-activated K+ channels SK1, SK2, and SK3 in mouse atrial and ventricular myocytes."
    Tuteja D., Xu D., Timofeyev V., Lu L., Sharma D., Zhang Z., Xu Y., Nie L., Vazquez A.E., Young J.N., Glatter K.A., Chiamvimonvat N.
    Am. J. Physiol. 289:H2714-H2723(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiKCNN3_MOUSE
AccessioniPrimary (citable) accession number: P58391
Secondary accession number(s): Q3UUY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 16, 2013
Last modified: June 24, 2015
This is version 102 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.