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   27-MAR-2024, entry version 142.
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   BioGRID; 219968; 1.
DR   STRING; 10090.ENSMUSP00000038106; -.
DR   GlyConnect; 2732; 5 N-Linked glycans (2 sites).
DR   GlyCosmos; Q99MR3; 2 sites, 5 glycans.
DR   GlyGen; Q99MR3; 3 sites, 5 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q99MR3; -.
DR   PhosphoSitePlus; Q99MR3; -.
DR   SwissPalm; Q99MR3; -.
DR   EPD; Q99MR3; -.
DR   jPOST; Q99MR3; -.
DR   MaxQB; Q99MR3; -.
DR   PaxDb; 10090-ENSMUSP00000038106; -.
DR   PeptideAtlas; Q99MR3; -.
DR   ProteomicsDB; 253345; -.
DR   Pumba; Q99MR3; -.
DR   Antibodypedia; 74017; 36 antibodies from 9 providers.
DR   DNASU; 83704; -.
DR   Ensembl; ENSMUST00000039991.14; ENSMUSP00000038106.8; ENSMUSG00000037344.15.
DR   GeneID; 83704; -.
DR   KEGG; mmu:83704; -.
DR   UCSC; uc009ace.2; mouse.
DR   AGR; MGI:1933532; -.
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; VANVFSC; -.
DR   OrthoDB; 5490251at2759; -.
DR   PhylomeDB; Q99MR3; -.
DR   TreeFam; TF313191; -.
DR   BioGRID-ORCS; 83704; 6 hits in 79 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 240 other cell types or tissues.
DR   ExpressionAtlas; Q99MR3; baseline and differential.
DR   GO; GO:0016020; C: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   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR018491; SLC12_C.
DR   InterPro; IPR004842; SLC12A_fam.
DR   PANTHER; PTHR11827:SF98; SOLUTE CARRIER FAMILY 12 MEMBER 9; 1.
DR   PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   Pfam; PF03522; SLC12; 1.
DR   Genevisible; Q99MR3; MM.
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
//