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Solute carrier family 12 member 1 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2) (Kidney-specific Na-K-Cl symporter)

 S12A1_RAT               Reviewed;        1095 AA.
P55016;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Solute carrier family 12 member 1;
AltName: Full=Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2;
AltName: Full=Kidney-specific Na-K-Cl symporter;
Name=Slc12a1; Synonyms=Nkcc2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=8021284;
Gamba G., Miyanoshita A., Lombardi M., Lytton J., Lee W.S.,
Hediger M.A., Hebert S.C.;
"Molecular cloning, primary structure, and characterization of two
members of the mammalian electroneutral sodium-(potassium)-chloride
cotransporter family expressed in kidney.";
J. Biol. Chem. 269:17713-17722(1994).
[2]
PHOSPHORYLATION AT SER-126.
PubMed=17341212; DOI=10.1042/BJ20061850;
Fraser S.A., Gimenez I., Cook N., Jennings I., Katerelos M.,
Katsis F., Levidiotis V., Kemp B.E., Power D.A.;
"Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by
AMP-activated protein kinase (AMPK).";
Biochem. J. 405:85-93(2007).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114; SER-116 AND
SER-144, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Electrically silent transporter system. Mediates sodium
and chloride reabsorption. Plays a vital role in the regulation of
ionic balance and cell volume.
-!- ENZYME REGULATION: Activated by WNK3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Predominant in kidney.
-!- SIMILARITY: Belongs to the SLC12A transporter family.
{ECO:0000305}.
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EMBL; U10096; AAA21251.1; -; mRNA.
PIR; A54145; A54145.
UniGene; Rn.14799; -.
STRING; 10116.ENSRNOP00000008857; -.
TCDB; 2.A.30.1.1; the cation-chloride cotransporter (ccc) family.
iPTMnet; P55016; -.
PhosphoSitePlus; P55016; -.
PaxDb; P55016; -.
PRIDE; P55016; -.
UCSC; RGD:3685; rat.
RGD; 3685; Slc12a1.
eggNOG; KOG2083; Eukaryota.
eggNOG; COG0531; LUCA.
HOGENOM; HOG000062855; -.
HOVERGEN; HBG052851; -.
InParanoid; P55016; -.
PhylomeDB; P55016; -.
PRO; PR:P55016; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0008511; F:sodium:potassium:chloride symporter activity; IDA:RGD.
GO; GO:0006821; P:chloride transport; IDA:RGD.
GO; GO:0016101; P:diterpenoid metabolic process; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0006813; P:potassium ion transport; IDA:RGD.
GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:RGD.
GO; GO:0070294; P:renal sodium ion absorption; IC:BHF-UCL.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
InterPro; IPR004841; AA-permease/SLC12A_dom.
InterPro; IPR013612; AA_permease_N.
InterPro; IPR002443; Na/K/Cl_cotranspt.
InterPro; IPR018491; SLC12_C.
InterPro; IPR002445; Slc12a1.
InterPro; IPR004842; SLC12A_fam.
PANTHER; PTHR11827:SF58; PTHR11827:SF58; 1.
Pfam; PF00324; AA_permease; 1.
Pfam; PF08403; AA_permease_N; 1.
Pfam; PF03522; SLC12; 1.
PRINTS; PR01207; NAKCLTRNSPRT.
PRINTS; PR01209; NAKCLTRSPRT2.
TIGRFAMs; TIGR00930; 2a30; 1.
1: Evidence at protein level;
Chloride; Complete proteome; Glycoprotein; Ion transport; Membrane;
Phosphoprotein; Potassium; Potassium transport; Reference proteome;
Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1095 Solute carrier family 12 member 1.
/FTId=PRO_0000178021.
TOPO_DOM 1 173 Cytoplasmic. {ECO:0000255}.
TRANSMEM 174 194 Helical. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
TOPO_DOM 219 255 Cytoplasmic. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TRANSMEM 299 319 Helical. {ECO:0000255}.
TOPO_DOM 320 323 Cytoplasmic. {ECO:0000255}.
TRANSMEM 324 344 Helical. {ECO:0000255}.
TRANSMEM 376 396 Helical. {ECO:0000255}.
TOPO_DOM 397 413 Cytoplasmic. {ECO:0000255}.
TRANSMEM 414 434 Helical. {ECO:0000255}.
TRANSMEM 481 501 Helical. {ECO:0000255}.
TOPO_DOM 502 546 Cytoplasmic. {ECO:0000255}.
TRANSMEM 547 567 Helical. {ECO:0000255}.
TRANSMEM 568 588 Helical. {ECO:0000255}.
TOPO_DOM 589 605 Cytoplasmic. {ECO:0000255}.
TRANSMEM 606 626 Helical. {ECO:0000255}.
TRANSMEM 789 809 Helical. {ECO:0000255}.
TOPO_DOM 810 1095 Cytoplasmic. {ECO:0000255}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P55014}.
MOD_RES 96 96 Phosphothreonine.
{ECO:0000250|UniProtKB:P55014}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:P55014}.
MOD_RES 114 114 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 126 126 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:17341212}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1095 AA; 120597 MW; 93C46F6ACD44363C CRC64;
MSVNIPSNSV PSGASRFQVH VINEGHGSGA AMSDSTDPPH YEETSFGDEA QNRLKISFRP
GNQECYENFL QTGETAKTDT TFHAYDSHTN TYYLQTFGHN TMDAVPKIEY YRNTGSVSGP
KVNRPSLQEI HEQLAKNVAV APGSADRVAN GDGMPGDEQA ENKEEDVTGV VKFGWVKGVL
VRCMLNIWGV MLFIRLSWIV GEAGIGLGVI IIGLSVVVTT LTGISMSAIC TNGVVRGGGA
YYLISRSLGP EFGGSIGLIF RFANAVRVAM YVVGFAETVV DLLKESDSMM VDPTNDIRII
GSITVVILLG ISVAGMEWEA KAQVILLVIL LIGIANFFIG TVIPSNNEKK SRGFFNYQAS
IFAENFGPSF TEGEGFFSVF AIFFPAATGI LAGANISGDL EDPQDAIPRG TMLAIFITTV
AYIGVAICVR ACVVRDATGS MNDTVVSGMN CNGSAACGLG YDFSRCQHEP CQYGLMNNFQ
VMSMVSGFGP LITAGIFSAT LSSALASLVS APKVFQALCK DNIFKGLQFF AKGYGKNNEP
LRGYFLTFVI AMAFILIAEL NVIAPIISNF FLASYALINF SCFHASYAKS PGWRPAYGIY
NMWVSLFGAI LCCAVMFVIN WWAAVITYVI ELFLYIYVTY KKPDVNWGSS TQALSYVSAL
DNALELTTVE DHVKNFRPQC IVLTGGPMTR PALLDITHAF TKNSGLCICC EVFVGPRKLC
VKEMNSGMAK KQAWLMKNKI KAFYAAVAAD CFRDGVRSLL QASGLGRMKP NTLVIGYKKN
WRKAPLSELE NYVGIIHDAF DFEIGVVIVR ISQGFDISPV LQVQDELEKL EQERLALEAA
IKDNDCEEGK GGIRGLFKKA GKLNITKPAP KKDSNISTIQ SMHVGEFNQK LVEASAQFKK
KQGKGTIDVW WLFDDGGLTL LIPYILTLRK KWKDCKLRIY VGGKINRIEE EKISMASLLS
KFRIKFADIH IIGDINIKPN KESWKVFEEM IEPYRLHESH KDLTTAEKLK RESPWKITDA
ELEAVKEKSY RQVRLNELLQ EHSRAANLIV LSLPVARKGS ISDLLYMAWL EILTKNLPPV
LLVRGNHKNV LTFYS


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