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Protein

Solute carrier family 12 member 7

Gene

Slc12a7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May mediate K+ uptake into Deiters' cells in the cochlea and contribute to K+ recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl- extrusion in the kidney and contribute to renal acidification (By similarity).By similarity

Enzyme regulationi

Inhibited by WNK3.By similarity

GO - Molecular functioni

  • potassium:chloride symporter activity Source: RGD
  • potassium ion symporter activity Source: GO_Central

GO - Biological processi

  • cell volume homeostasis Source: RGD
  • synaptic transmission Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Ion transport, Potassium transport, Symport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiR-RNO-426117. Cation-coupled Chloride cotransporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 12 member 7
Alternative name(s):
Electroneutral potassium-chloride cotransporter 4
K-Cl cotransporter 4
Gene namesi
Name:Slc12a7Imported
Synonyms:Kcc4Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1359672. Slc12a7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 118118CytoplasmicSequence analysisAdd
BLAST
Transmembranei119 – 13921HelicalSequence analysisAdd
BLAST
Transmembranei141 – 16121HelicalSequence analysisAdd
BLAST
Topological domaini162 – 20039CytoplasmicSequence analysisAdd
BLAST
Transmembranei201 – 22121HelicalSequence analysisAdd
BLAST
Transmembranei253 – 27321HelicalSequence analysisAdd
BLAST
Topological domaini274 – 2752CytoplasmicSequence analysis
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence analysisAdd
BLAST
Topological domaini437 – 45519CytoplasmicSequence analysisAdd
BLAST
Transmembranei456 – 47621HelicalSequence analysisAdd
BLAST
Transmembranei494 – 51421HelicalSequence analysisAdd
BLAST
Topological domaini515 – 55339CytoplasmicSequence analysisAdd
BLAST
Transmembranei554 – 57421HelicalSequence analysisAdd
BLAST
Transmembranei577 – 59721HelicalSequence analysisAdd
BLAST
Topological domaini598 – 62427CytoplasmicSequence analysisAdd
BLAST
Transmembranei625 – 64521HelicalSequence analysisAdd
BLAST
Transmembranei845 – 86521HelicalSequence analysisAdd
BLAST
Topological domaini866 – 1083218CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10831083Solute carrier family 12 member 7PRO_0000299076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei62 – 621PhosphoserineBy similarity
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence analysis
Modified residuei973 – 9731PhosphothreonineBy similarity
Modified residuei980 – 9801PhosphothreonineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ5RK27.
PRIDEiQ5RK27.

PTM databases

iPTMnetiQ5RK27.

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney, liver and pancreas. Expressed in choroid plexus and suprachiasmatic nucleus.1 Publication

Gene expression databases

ExpressionAtlasiQ5RK27. baseline and differential.
GenevisibleiQ5RK27. RN.

Interactioni

Subunit structurei

Homomultimer and heteromultimer with other K-Cl cotransporters.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022635.

Structurei

3D structure databases

ProteinModelPortaliQ5RK27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SLC12A transporter family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2082. Eukaryota.
COG0531. LUCA.
GeneTreeiENSGT00760000119053.
HOGENOMiHOG000092644.
HOVERGENiHBG052852.
InParanoidiQ5RK27.
KOiK13627.
OMAiLMAWPQS.
OrthoDBiEOG78M01J.
PhylomeDBiQ5RK27.
TreeFamiTF313657.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR030354. KCC4.
IPR000076. KCL_cotranspt.
IPR018491. SLC12_C.
IPR004842. SLC12A_fam.
[Graphical view]
PANTHERiPTHR11827:SF47. PTHR11827:SF47. 4 hits.
PfamiPF00324. AA_permease. 2 hits.
PF03522. SLC12. 2 hits.
[Graphical view]
PRINTSiPR01081. KCLTRNSPORT.
TIGRFAMsiTIGR00930. 2a30. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5RK27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTNFTVVPV EARADGAGDE AAERTEEPGS PESADPACPT PGDGNPRENS
60 70 80 90 100
PFINNVEVER ESYFEGKNMA LFEEEMDSNP MVSSLLNKLA NYTNLSQGVV
110 120 130 140 150
EHEEDEDSRR REIKAPRMGT FIGVYLPCLQ NILGVILFLR LTWIVGAAGV
160 170 180 190 200
LESFLIVAMC CTCTMLTAIS MSAIATNGVV PAGGSYYMIS RSLGPEFGGA
210 220 230 240 250
VGLCFYLGTT FAGAMYILGT IEIFLTYISP SAAIFQAETA DGEAAALLNN
260 270 280 290 300
MRVYGSCALA LMAVVVFVGV KYVNKLALVF LACVVLSILA IYAGVIKTAF
310 320 330 340 350
APPDIPVCLL GNRTLANRNF DTCAKMQVVS NGTVTTALWR LFCNGSSLGA
360 370 380 390 400
SCDEYFVQNN VTEIQGIPGV ASGVFLDNLW STYSDKGAFV EKKGVSSVPV
410 420 430 440 450
SEESRPGGLP YVLTDIMTYF TMLVGIYFPS VTGIMAGSNR SGDLKDAQKS
460 470 480 490 500
IPTGTILAIV TTSFIYLSCI VLFGACIEGV VLRDKFGEAL QGNLVIGMLA
510 520 530 540 550
WPSPWVIVIG SFFSTCGAGL QSLTGAPRLL QAIARDGIIP FLQVFGHGKA
560 570 580 590 600
NGEPTWALLL TALICETGIL IASLDSVAPI LSMFFLMCYM FVNLACAVQT
610 620 630 640 650
LLRTPNWRPR FKFYHWTLSF LGMSLCLALM FICSWYYALF AMLIAGCIYK
660 670 680 690 700
YIEYRGAEKE WGDGIRGLSL NAARYALLRV EHGPPHTKNW RPQVLVMLNL
710 720 730 740 750
DSEQCVKHPR LLSFTSQLKA GKGLTIVGSV LEGTYLDKHV EAQRAEENIR
760 770 780 790 800
SLMSAEKMKG FCQLVVSSNL RDGASHLIQS AGLGGMKHNT VLMAWPEAWK
810 820 830 840 850
QADNPFSWKN FVDTVRDTTA AHQALLVAKN IDLFPQNQER FSDGNIDVWW
860 870 880 890 900
IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQVDDNSIQ MKKDLQMFLY
910 920 930 940 950
HLRISAEVEV VEMVENDISA FTYEKTLMME QRSQMLKQMQ LSKNEREREA
960 970 980 990 1000
QLIHDRNTAS HTVATARTEA PPTPDKVQMT WTKEKLIAEK HRNKDTGTSG
1010 1020 1030 1040 1050
FKDLFSLKPD QSNVRRMHTA VKLNGVVLNK SQDAQLVLLN MPGPPKSRQG
1060 1070 1080
DENYMEFLEV LTEGLNRVLL VRGGGREVIT IYS
Length:1,083
Mass (Da):119,378
Last modified:August 21, 2007 - v2
Checksum:i111C2D9EE0A16BA5
GO

Sequence cautioni

The sequence AAH86339.1 differs from that shown.Intron retention. This sequence is incomplete at its 3'end and extensively differs from that shown in positions 214-251.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251Y → F in AAQ93481 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000133 mRNA. No translation available.
BC086339 mRNA. Translation: AAH86339.1. Sequence problems.
AY429042 mRNA. Translation: AAR10805.1.
AY387486 mRNA. Translation: AAQ93480.1.
AY387487 mRNA. Translation: AAQ93481.1.
RefSeqiNP_001013162.2. NM_001013144.2.
UniGeneiRn.64199.

Genome annotation databases

EnsembliENSRNOT00000022635; ENSRNOP00000022635; ENSRNOG00000016372.
GeneIDi308069.
KEGGirno:308069.
UCSCiRGD:1359672. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000133 mRNA. No translation available.
BC086339 mRNA. Translation: AAH86339.1. Sequence problems.
AY429042 mRNA. Translation: AAR10805.1.
AY387486 mRNA. Translation: AAQ93480.1.
AY387487 mRNA. Translation: AAQ93481.1.
RefSeqiNP_001013162.2. NM_001013144.2.
UniGeneiRn.64199.

3D structure databases

ProteinModelPortaliQ5RK27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022635.

PTM databases

iPTMnetiQ5RK27.

Proteomic databases

PaxDbiQ5RK27.
PRIDEiQ5RK27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022635; ENSRNOP00000022635; ENSRNOG00000016372.
GeneIDi308069.
KEGGirno:308069.
UCSCiRGD:1359672. rat.

Organism-specific databases

CTDi10723.
RGDi1359672. Slc12a7.

Phylogenomic databases

eggNOGiKOG2082. Eukaryota.
COG0531. LUCA.
GeneTreeiENSGT00760000119053.
HOGENOMiHOG000092644.
HOVERGENiHBG052852.
InParanoidiQ5RK27.
KOiK13627.
OMAiLMAWPQS.
OrthoDBiEOG78M01J.
PhylomeDBiQ5RK27.
TreeFamiTF313657.

Enzyme and pathway databases

ReactomeiR-RNO-426117. Cation-coupled Chloride cotransporters.

Miscellaneous databases

PROiQ5RK27.

Gene expression databases

ExpressionAtlasiQ5RK27. baseline and differential.
GenevisibleiQ5RK27. RN.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR030354. KCC4.
IPR000076. KCL_cotranspt.
IPR018491. SLC12_C.
IPR004842. SLC12A_fam.
[Graphical view]
PANTHERiPTHR11827:SF47. PTHR11827:SF47. 4 hits.
PfamiPF00324. AA_permease. 2 hits.
PF03522. SLC12. 2 hits.
[Graphical view]
PRINTSiPR01081. KCLTRNSPORT.
TIGRFAMsiTIGR00930. 2a30. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  2. "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] OF 1-213.
    Tissue: OvaryImported.
  3. "Rattus norvegicus K-CL cotransporter KCC4."
    Le Rouzic P., Stanley S.J., Luckman S.M.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-159.
    Strain: Sprague-DawleyImported.
    Tissue: PancreasImported.
  4. "Aldosterone up regulates K+-Cl- cotransporter expression and activity in arterial tissue."
    Lopez N.C., Michea L.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-105 AND 113-129.
    Strain: Sprague-DawleyImported.
  5. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiS12A7_RAT
AccessioniPrimary (citable) accession number: Q5RK27
Secondary accession number(s): Q6T7Y5, Q6TUA1, Q6TUA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: July 6, 2016
This is version 88 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.