S12A9_RAT
ID S12A9_RAT Reviewed; 914 AA.
AC Q66HR0; Q99NC8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Solute carrier family 12 member 9;
DE AltName: Full=Cation-chloride cotransporter 6;
GN Name=Slc12a9; Synonyms=Ccc6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Imai M., Ishibashi K.;
RT "Molecular cloning of a new member of cation-chloride cotransporter.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAB40440.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB023645; BAB40440.1; ALT_FRAME; mRNA.
DR EMBL; BC081728; AAH81728.1; -; mRNA.
DR RefSeq; NP_599232.1; NM_134405.1.
DR AlphaFoldDB; Q66HR0; -.
DR SMR; Q66HR0; -.
DR BioGRID; 251253; 1.
DR IntAct; Q66HR0; 6.
DR MINT; Q66HR0; -.
DR GlyGen; Q66HR0; 3 sites.
DR iPTMnet; Q66HR0; -.
DR PhosphoSitePlus; Q66HR0; -.
DR jPOST; Q66HR0; -.
DR PaxDb; Q66HR0; -.
DR Ensembl; ENSRNOT00000076829; ENSRNOP00000068426; ENSRNOG00000048487.
DR GeneID; 171443; -.
DR KEGG; rno:171443; -.
DR CTD; 56996; -.
DR RGD; 620747; Slc12a9.
DR eggNOG; KOG1288; Eukaryota.
DR GeneTree; ENSGT00940000159400; -.
DR InParanoid; Q66HR0; -.
DR OrthoDB; 515568at2759; -.
DR PhylomeDB; Q66HR0; -.
DR PRO; PR:Q66HR0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_0000331417"
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 843..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 59
FT /note="R -> K (in Ref. 1; BAB40440)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="D -> G (in Ref. 1; BAB40440)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="A -> S (in Ref. 1; BAB40440)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="E -> K (in Ref. 1; BAB40440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 96005 MW; 4080AA02E4290205 CRC64;
MASENSPLLA YRLLGEEGAA FPPNGAGGSG VASARKLSTF LGVVVPTVLS MFSIVVFLRI
GFVVGHAGLL QALAMLLVAY VILALTVLSV CAIATNGAVR GGGAYFMISR TLGPEVGGSI
GLMFYLANVC GCAVSLLGLV ESILDVFGAD VTGSSGIKVL PQGYGWNLLY GSLLLGLVGG
VCALGAGLYA RASFLTFLLV SGSLASVLVS FVAVGPRNIT LAPRPGTNGS SVPPRHGHFT
GFNGSTLKDN LGAGYAEDYT TGAMMTFASV FAVLFNGCTG IMAGANMSGE LKDPSRAIPL
GTIIAVAYTF FIYILLFFLS SFTCDRALLQ GDYGFFRDIS 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 LSRGSGSSAQ
LHHVDVWPLN LLRPRGGPGY VDVCGLFLLQ MATILSMVPA WHSARLRIFL CLGPREAPGA
AEGRLRALLS QLRIRAEVQE VVWGEGAEAG EPEEEEGDFV NGGRGDEEAE ALACSANALV
RAQQGRGTGG GPGGPEGRDG EEGPTTALTF LYLPRPPADP ARYPRYLALL ETLSRDLGPT
LLIHGVTPVT CTDL
