S12A7_RABIT
ID S12A7_RABIT Reviewed; 1106 AA.
AC Q7YRU6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Solute carrier family 12 member 7;
DE AltName: Full=K-Cl cotransporter 4;
DE AltName: Full=Potassium-chloride cotransporter isoform 4;
GN Name=SLC12A7 {ECO:0000250|UniProtKB:Q9WVL3};
GN Synonyms=KCC4 {ECO:0000312|EMBL:AAP84988.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP84988.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney {ECO:0000312|EMBL:AAP84988.1};
RX PubMed=12709395; DOI=10.1152/ajprenal.00389.2002;
RA Velazquez H., Silva T.;
RT "Cloning and localization of KCC4 in rabbit kidney: expression in distal
RT convoluted tubule.";
RL Am. J. Physiol. 285:F49-F58(2003).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when
CC activated by cell swelling. May mediate K(+) uptake into Deiters' cells
CC in the cochlea and contribute to K(+) recycling in the inner ear.
CC Important for the survival of cochlear outer and inner hair cells and
CC the maintenance of the organ of Corti. May be required for basolateral
CC Cl(-) extrusion in the kidney and contribute to renal acidification (By
CC similarity). {ECO:0000250|UniProtKB:Q9WVL3}.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC cotransporters. {ECO:0000250|UniProtKB:Q9WVL3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12709395};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12709395}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher levels in heart, kidney
CC and lung (at protein level). {ECO:0000269|PubMed:12709395}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000255}.
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DR EMBL; AF538347; AAP84988.1; -; mRNA.
DR RefSeq; NP_001075592.1; NM_001082123.1.
DR AlphaFoldDB; Q7YRU6; -.
DR SMR; Q7YRU6; -.
DR STRING; 9986.ENSOCUP00000018959; -.
DR PRIDE; Q7YRU6; -.
DR GeneID; 100008847; -.
DR KEGG; ocu:100008847; -.
DR CTD; 10723; -.
DR eggNOG; KOG2082; Eukaryota.
DR InParanoid; Q7YRU6; -.
DR OrthoDB; 349744at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR030354; KCC4.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF47; PTHR11827:SF47; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1106
FT /note="Solute carrier family 12 member 7"
FT /id="PRO_0000299075"
FT TOPO_DOM 1..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..1106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 17..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y666"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y666"
FT MOD_RES 996
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL3"
FT MOD_RES 1003
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL3"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1106 AA; 120879 MW; 9614C0300DCE23F2 CRC64;
MVYTALTWQR LHGTAAGLVP SHLPQEGEKG STHPTPRPLG TTPRVTAHIE PPRPWAAGAE
PPLPAGDGSA RESSPFIGSA AADGDSLLEG KNMALFEEEM DSNPMVSSLL NKLANYTNLS
QGVVDHEEAE DSRPRESKAP CMGTFIGVYL PCLQNILGVI LFLRLTWIVG AAGVLESFLV
VSMCCTCTML TAVSMSAIAT NGVVPAGGSY YMISRSLGPE FGGAVGLCFY LGTTFAGAMY
ILGTIEIFLT YISPGAAVFQ AETPEGEAAA LLHNMRVYGS CTLALMAVVV FVGVKYVNKL
ALVFLACVVL SILAIYAGVI KTAFDPPDIP VCLLGNRTLA RRGFDTCAKV RAVSNGTATT
ALWGLFCNGS SLDTACNEYF AQNNVTEIQG IPGVASGVLL DNLWSAYSDR GAFVEKKGVA
SVPTPEDGRA SGLPYVLSDI TTYFTVLVGI YFPSVTGIMA GSNRSGDLKD AQKSIPTGTI
LAIVTTSFIY LSCIVLFGAC IEGVVLRDKF GEALQGNLVI GMLAWPSPWV IVIGSFFSTC
GAGLQSLTGA PRLLQAIARD GIVPFLQVFG HGKANGEPTW ALLLTALICE TGILIASLDS
VAPILSMFFL MCYMFVNLAC AVQTLLRTPN WRPRFKYYHW TLSFLGMSLC LALMFICSWY
YALFAMLIAG CIYKYIEYRG AEKEWGDGIR GLSLNAARYA LLRVEHGPPH TKNWRPQVLV
MLTLDAEQRV THPRLLSFTS QLKAGKGLTI VGSVLEGTFL DKHVEAQRAE ENIRALMGAE
KMKGFCQLVV SSSLRDGCSH LIQAAGLGGM KHNTVLMAWP EAWKQPDSPY SWKYFVDTVR
DTTAAQQALL VAKNIDAFPQ NQERFSEGSI DVWWVVHDGG MLMLLPFLLR QHKVWRKCRM
RIFTVAQVDD NSVQMKKDLQ MFLYHLRISA EVEVVEMVEN DISAFTYEKT LLMEQRSQML
KQMQLTKGER EREAQLIHDR NTASHTAASR AQAPPTPDKV QMTWTKEKLT AEKHRNKDAG
AAGFRDLFSL KPDHSNVRRM HTAVKLNGVV LSRSQDAQLV LLNMPGPPKN RQGDENYMEF
LEVLTEGLNR VVLVRGGGRE VITIYS
