S12A9_MOUSE
ID S12A9_MOUSE Reviewed; 914 AA.
AC Q99MR3; E9QNN4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Solute carrier family 12 member 9;
DE AltName: Full=Cation-chloride cotransporter-interacting protein 1;
DE AltName: Full=Potassium-chloride transporter 9;
GN Name=Slc12a9; Synonyms=Cip1, Slc12a8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N;
RA Mount D.B.;
RT "Cloning of mouse Slc12a8, a new member of the cation-chloride
RT cotransporter gene family.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228 AND ASN-243.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be an inhibitor of SLC12A1. Seems to correspond to a
CC subunit of a multimeric transport system and thus, additional subunits
CC may be required for its function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLC12A1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF312033; AAK28822.1; -; Genomic_DNA.
DR EMBL; AF314957; AAL26866.1; -; mRNA.
DR EMBL; AC150682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046982; AAH46982.1; -; mRNA.
DR CCDS; CCDS19766.1; -.
DR RefSeq; NP_113583.2; NM_031406.3.
DR RefSeq; XP_006504696.1; XM_006504633.3.
DR AlphaFoldDB; Q99MR3; -.
DR SMR; Q99MR3; -.
DR STRING; 10090.ENSMUSP00000038106; -.
DR GlyConnect; 2732; 5 N-Linked glycans (2 sites).
DR GlyGen; Q99MR3; 2 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; Q99MR3; -.
DR PhosphoSitePlus; Q99MR3; -.
DR EPD; Q99MR3; -.
DR jPOST; Q99MR3; -.
DR MaxQB; Q99MR3; -.
DR PaxDb; Q99MR3; -.
DR PeptideAtlas; Q99MR3; -.
DR PRIDE; Q99MR3; -.
DR ProteomicsDB; 253345; -.
DR Antibodypedia; 74017; 36 antibodies from 9 providers.
DR DNASU; 83704; -.
DR Ensembl; ENSMUST00000039991; ENSMUSP00000038106; ENSMUSG00000037344.
DR GeneID; 83704; -.
DR KEGG; mmu:83704; -.
DR UCSC; uc009ace.2; mouse.
DR CTD; 56996; -.
DR MGI; MGI:1933532; Slc12a9.
DR VEuPathDB; HostDB:ENSMUSG00000037344; -.
DR eggNOG; KOG1288; Eukaryota.
DR GeneTree; ENSGT00940000159400; -.
DR HOGENOM; CLU_001883_3_0_1; -.
DR InParanoid; Q99MR3; -.
DR OMA; NAGLYVT; -.
DR OrthoDB; 515568at2759; -.
DR PhylomeDB; Q99MR3; -.
DR TreeFam; TF313191; -.
DR BioGRID-ORCS; 83704; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Slc12a9; mouse.
DR PRO; PR:Q99MR3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99MR3; protein.
DR Bgee; ENSMUSG00000037344; Expressed in retinal neural layer and 238 other tissues.
DR ExpressionAtlas; Q99MR3; baseline and differential.
DR Genevisible; Q99MR3; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR030345; SLC12A9.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF98; PTHR11827:SF98; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF03522; SLC12; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..914
FT /note="Solute carrier family 12 member 9"
FT /id="PRO_0000331416"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 645..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP2"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CONFLICT 34
FT /note="S -> A (in Ref. 1; AAK28822, 2; AAL26866 and 4;
FT AAH46982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 96330 MW; 769EA9EB4BD40E00 CRC64;
MASESSPLLA YRLLGEEGAA FPPNGAGVSG VPSSRKLSTF LGVVVPTVLS MFSIVVFLRI
GFVVGHAGLL QALAMLLVAY IILALTVLSV CAIATNGAVR GGGAYFMISR TLGPEVGGSI
GLMFYLANVC GCAVSLLGLV ESILDVFGAD ATGSSGIQVL PQGYGWNLLY GSLLLGLVGG
VCTLGAGLYA RASFLTFLLV SGSLASVLVS FVAVGPRNIP LAPRPGTNAS SVPHRHGHFT
GFNGSTLRDN LGAGYAEDYT TGAMMTFASV FAVLFNGCTG IMAGANMSGE LKDPSRAIPL
GTIIAVAYTF FIYILLFFLS SFTCDRALLQ EDYGFFRDIS LWPPLVLIGI YATALSASMS
SLIGASRILH ALAQDDLFGV ILAPAKVVSG GGNPWGAVLY SWGLVQLVLL AGKLNTLAAV
VTVFYLVAYA AVDLSCLSLE WASAPNFRPT FSLFSWHTCL LGVASCLLMM FLISPGAAGG
SLLLMGLLSA LLTARGGPSS WGYVSQALLF HQVRKYLLRL DVRKEHVKFW RPQLLLLVGN
PRGALPLLRL ANQLKKGGLY VLGHVTLGDL DSLPSDPVQP QYGAWLSLVD LAQVKAFVDL
TLSPSVRQGA QHLLRISGLG GMKPNTLVLG FYDDAPPQDH FLTDPAFSEP AEGTREGGSP
ALSTLFPPPR APGSPRALSP QDYVATVADA LKMNKNVVLA RACGALPPER LSRGSSSSAQ
LHHVDVWPLN LLRPRGGPGY VDVCGLFLLQ MATILSMVPA WHSARLRIFL CLGPREAPGA
AEGRLRALLS QLRIRAEVQE VVWGEGAETG EPEEEEGDFV NGGRGDEEAE ALACSANALV
RAQQGRGTVG GPGGPEGRDG EEGPTTALTF LYLPRPPADP ARYPRYLALL ETLSRDLGPT
LLIHGVTPVT CTDL
