S12A6_HUMAN
ID S12A6_HUMAN Reviewed; 1150 AA.
AC Q9UHW9; A0AV76; Q2VI00; Q7Z2E7; Q7Z4G5; Q8TDD4; Q9UFR2; Q9Y642; Q9Y665;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Solute carrier family 12 member 6;
DE AltName: Full=Electroneutral potassium-chloride cotransporter 3;
DE AltName: Full=K-Cl cotransporter 3;
GN Name=SLC12A6; Synonyms=KCC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TOPOLOGY.
RC TISSUE=Placenta;
RX PubMed=10600773; DOI=10.1152/ajpcell.1999.277.6.c1210;
RA Race J.E., Makhlouf F.N., Logue P.J., Wilson F.H., Dunham P.B.,
RA Holtzman E.J.;
RT "Molecular cloning and functional characterization of KCC3, a new K-Cl
RT cotransporter.";
RL Am. J. Physiol. 277:C1210-C1219(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), GLYCOSYLATION, AND REGULATION BY
RP VEGF AND TNF.
RC TISSUE=Umbilical vein;
RX PubMed=10187864; DOI=10.1074/jbc.274.15.10661;
RA Hiki K., D'Andrea R.J., Furze J., Crawford J., Woollatt E.,
RA Sutherland G.R., Vadas M.A., Gamble J.R.;
RT "Cloning, characterization, and chromosomal location of a novel human K+-
RT Cl- cotransporter.";
RL J. Biol. Chem. 274:10661-10667(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10347194; DOI=10.1074/jbc.274.23.16355;
RA Mount D.B., Mercado A., Song L., Xu J., George A.L. Jr., Delpire E.,
RA Gamba G.;
RT "Cloning and characterization of KCC3 and KCC4, new members of the cation-
RT chloride cotransporter gene family.";
RL J. Biol. Chem. 274:16355-16362(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP GLYCOSYLATION, AND DISEASE.
RX PubMed=12368912; DOI=10.1038/ng1002;
RA Howard H.C., Mount D.B., Rochefort D., Byun N., Dupre N., Lu J., Fan X.,
RA Song L., Riviere J.-B., Prevost C., Horst J., Simonati A., Lemcke B.,
RA Welch R., England R., Zhan F.Q., Mercado A., Siesser W.B., George A.L. Jr.,
RA McDonald M.P., Bouchard J.-P., Mathieu J., Delpire E., Rouleau G.A.;
RT "The K-Cl cotransporter KCC3 is mutant in a severe peripheral neuropathy
RT associated with agenesis of the corpus callosum.";
RL Nat. Genet. 32:384-392(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5), ALTERNATIVE SPLICING
RP (ISOFORM 6), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16048901; DOI=10.1152/ajprenal.00464.2004;
RA Mercado A., Vazquez N., Song L., Cortes R., Enck A.H., Welch R.,
RA Delpire E., Gamba G., Mount D.B.;
RT "NH2-terminal heterogeneity in the KCC3 K+-Cl- cotransporter.";
RL Am. J. Physiol. 289:F1246-1261(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-1150 (ISOFORM 1).
RC TISSUE=Testis;
RA Guo J.H., Yu L.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-1150 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [12]
RP SUBUNIT.
RX PubMed=11551954; DOI=10.1074/jbc.m107155200;
RA Casula S., Shmukler B.E., Wilhelm S., Stuart-Tilley A.K., Su W.,
RA Chernova M.N., Brugnara C., Alper S.L.;
RT "A dominant negative mutant of the KCC1 K-Cl cotransporter: both N- and C-
RT terminal cytoplasmic domains are required for K-Cl cotransport activity.";
RL J. Biol. Chem. 276:41870-41878(2001).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACTIVITY REGULATION.
RX PubMed=21613606; DOI=10.1152/ajpcell.00070.2011;
RA Cruz-Rangel S., Melo Z., Vazquez N., Meade P., Bobadilla N.A.,
RA Pasantes-Morales H., Gamba G., Mercado A.;
RT "Similar Effects of all WNK3 Variants upon SLC12 Cotransporters.";
RL Am. J. Physiol. 301:C601-C608(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-120; SER-148 AND
RP SER-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport. May
CC be activated by cell swelling. May contribute to cell volume
CC homeostasis in single cells.
CC -!- ACTIVITY REGULATION: Activated by N-ethylmaleimide (NEM). Inhibited by
CC DIOA, bumetanide and furosemide. Inhibited by WNK3.
CC {ECO:0000269|PubMed:21613606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 mM for extracellular Rb(+) (isoform 1)
CC {ECO:0000269|PubMed:16048901};
CC KM=7.3 mM for extracellular Cl(-) (isoform 1)
CC {ECO:0000269|PubMed:16048901};
CC KM=17.2 mM for extracellular Rb(+) (isoform 2)
CC {ECO:0000269|PubMed:16048901};
CC KM=8.2 mM for extracellular Cl(-) (isoform 2)
CC {ECO:0000269|PubMed:16048901};
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC cotransporters. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=KCC3a;
CC IsoId=Q9UHW9-1; Sequence=Displayed;
CC Name=2; Synonyms=KCC3b;
CC IsoId=Q9UHW9-2; Sequence=VSP_006115, VSP_006116;
CC Name=3; Synonyms=KCC3a-X2M;
CC IsoId=Q9UHW9-3; Sequence=VSP_041389;
CC Name=4; Synonyms=KCC3a-S3;
CC IsoId=Q9UHW9-4; Sequence=VSP_041388;
CC Name=5; Synonyms=KCC3a-S, KCC3a-S1, KCC3a-S2;
CC IsoId=Q9UHW9-5; Sequence=VSP_041387;
CC Name=6; Synonyms=KCC3b-X2M;
CC IsoId=Q9UHW9-6; Sequence=VSP_006115, VSP_006116, VSP_041389;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain and kidney.
CC Detected at lower levels in skeletal muscle, placenta, lung and
CC pancreas. Detected in umbilical vein endothelial cells. Isoform 2 is
CC more abundant in kidney. Isoform 5 is testis specific. Expressed in the
CC proximal tubule of the kidney (at protein level).
CC {ECO:0000269|PubMed:16048901}.
CC -!- INDUCTION: Up-regulated by VEGF. Down-regulated by TNF.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10187864,
CC ECO:0000269|PubMed:12368912}.
CC -!- DISEASE: Agenesis of the corpus callosum, with peripheral neuropathy
CC (ACCPN) [MIM:218000]: A disease that is characterized by severe
CC progressive sensorimotor neuropathy, intellectual disability,
CC dysmorphic features and complete or partial agenesis of the corpus
CC callosum. Note=The disease is caused by variants affecting the gene
CC represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Does not differ in the osmotic set point of
CC swelling activation but, activation is more rapid. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Does not differ in the osmotic set point of
CC swelling activation but, activation is more rapid. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; AF116242; AAF24986.1; -; mRNA.
DR EMBL; AF108831; AAD25337.1; -; mRNA.
DR EMBL; AF105366; AAD39742.1; -; mRNA.
DR EMBL; AF314956; AAM96215.1; -; Genomic_DNA.
DR EMBL; AF314931; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314933; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314934; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314935; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314936; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314937; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314938; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314939; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314940; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314941; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314942; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314943; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314944; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314945; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314946; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314947; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314948; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314949; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314950; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314951; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314952; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314953; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314954; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314955; AAM96215.1; JOINED; Genomic_DNA.
DR EMBL; AF314956; AAM96216.1; -; Genomic_DNA.
DR EMBL; AF314932; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314933; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314934; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314935; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314936; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314937; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314938; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314939; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314940; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314941; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314942; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314943; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314944; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314945; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314946; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314947; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314948; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314949; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314950; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314951; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314952; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314953; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314954; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF314955; AAM96216.1; JOINED; Genomic_DNA.
DR EMBL; AF531258; AAQ10026.1; -; mRNA.
DR EMBL; AF531259; AAQ10027.1; -; mRNA.
DR EMBL; AF531260; AAQ10028.1; -; mRNA.
DR EMBL; DQ138323; ABA02873.1; -; mRNA.
DR EMBL; AK315283; BAG37692.1; -; mRNA.
DR EMBL; AC021822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92295.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92297.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92301.1; -; Genomic_DNA.
DR EMBL; BC126241; AAI26242.1; -; mRNA.
DR EMBL; BC126243; AAI26244.1; -; mRNA.
DR EMBL; AF477977; AAL85335.1; -; mRNA.
DR EMBL; AL117500; CAB55965.1; -; mRNA.
DR CCDS; CCDS10036.1; -. [Q9UHW9-2]
DR CCDS; CCDS42010.1; -. [Q9UHW9-3]
DR CCDS; CCDS42011.1; -. [Q9UHW9-4]
DR CCDS; CCDS42012.1; -. [Q9UHW9-5]
DR CCDS; CCDS58352.1; -. [Q9UHW9-1]
DR PIR; T17275; T17275.
DR RefSeq; NP_001035959.1; NM_001042494.1. [Q9UHW9-5]
DR RefSeq; NP_001035960.1; NM_001042495.1. [Q9UHW9-5]
DR RefSeq; NP_001035961.1; NM_001042496.1. [Q9UHW9-4]
DR RefSeq; NP_001035962.1; NM_001042497.1. [Q9UHW9-3]
DR RefSeq; NP_005126.1; NM_005135.2. [Q9UHW9-2]
DR RefSeq; NP_598408.1; NM_133647.1. [Q9UHW9-1]
DR PDB; 6M1Y; EM; 3.20 A; A/B=71-1150.
DR PDB; 6M22; EM; 2.70 A; A/B=71-1150.
DR PDB; 6Y5R; EM; 3.76 A; A/B=71-1150.
DR PDB; 6Y5V; EM; 4.08 A; A/B=71-1150.
DR PDB; 7AIN; EM; 3.20 A; A/B=71-1150.
DR PDB; 7AIO; EM; 3.31 A; A/B=71-1150.
DR PDB; 7D90; EM; 3.60 A; A/B=1-1150.
DR PDB; 7NGB; EM; 3.64 A; A/B=71-1150.
DR PDBsum; 6M1Y; -.
DR PDBsum; 6M22; -.
DR PDBsum; 6Y5R; -.
DR PDBsum; 6Y5V; -.
DR PDBsum; 7AIN; -.
DR PDBsum; 7AIO; -.
DR PDBsum; 7D90; -.
DR PDBsum; 7NGB; -.
DR AlphaFoldDB; Q9UHW9; -.
DR SMR; Q9UHW9; -.
DR BioGRID; 115311; 80.
DR IntAct; Q9UHW9; 23.
DR MINT; Q9UHW9; -.
DR STRING; 9606.ENSP00000346112; -.
DR DrugBank; DB00761; Potassium chloride.
DR TCDB; 2.A.30.1.15; the cation-chloride cotransporter (ccc) family.
DR GlyConnect; 1762; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UHW9; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9UHW9; -.
DR PhosphoSitePlus; Q9UHW9; -.
DR BioMuta; SLC12A6; -.
DR DMDM; 27151690; -.
DR EPD; Q9UHW9; -.
DR jPOST; Q9UHW9; -.
DR MassIVE; Q9UHW9; -.
DR MaxQB; Q9UHW9; -.
DR PaxDb; Q9UHW9; -.
DR PeptideAtlas; Q9UHW9; -.
DR PRIDE; Q9UHW9; -.
DR ProteomicsDB; 84422; -. [Q9UHW9-1]
DR ProteomicsDB; 84423; -. [Q9UHW9-2]
DR ProteomicsDB; 84424; -. [Q9UHW9-3]
DR ProteomicsDB; 84425; -. [Q9UHW9-4]
DR ProteomicsDB; 84426; -. [Q9UHW9-5]
DR ProteomicsDB; 84427; -. [Q9UHW9-6]
DR Antibodypedia; 22708; 218 antibodies from 29 providers.
DR DNASU; 9990; -.
DR Ensembl; ENST00000290209.9; ENSP00000290209.5; ENSG00000140199.13. [Q9UHW9-2]
DR Ensembl; ENST00000354181.8; ENSP00000346112.3; ENSG00000140199.13. [Q9UHW9-1]
DR Ensembl; ENST00000397702.6; ENSP00000380814.2; ENSG00000140199.13. [Q9UHW9-5]
DR Ensembl; ENST00000397707.6; ENSP00000380819.2; ENSG00000140199.13. [Q9UHW9-3]
DR Ensembl; ENST00000458406.6; ENSP00000387725.2; ENSG00000140199.13. [Q9UHW9-5]
DR Ensembl; ENST00000558589.5; ENSP00000452776.1; ENSG00000140199.13. [Q9UHW9-4]
DR Ensembl; ENST00000558667.5; ENSP00000453473.1; ENSG00000140199.13. [Q9UHW9-1]
DR Ensembl; ENST00000560611.5; ENSP00000454168.1; ENSG00000140199.13. [Q9UHW9-1]
DR GeneID; 9990; -.
DR KEGG; hsa:9990; -.
DR MANE-Select; ENST00000354181.8; ENSP00000346112.3; NM_001365088.1; NP_001352017.1.
DR UCSC; uc001zhv.4; human. [Q9UHW9-1]
DR CTD; 9990; -.
DR DisGeNET; 9990; -.
DR GeneCards; SLC12A6; -.
DR GeneReviews; SLC12A6; -.
DR HGNC; HGNC:10914; SLC12A6.
DR HPA; ENSG00000140199; Low tissue specificity.
DR MalaCards; SLC12A6; -.
DR MIM; 218000; phenotype.
DR MIM; 604878; gene.
DR neXtProt; NX_Q9UHW9; -.
DR OpenTargets; ENSG00000140199; -.
DR Orphanet; 1496; Corpus callosum agenesis-neuronopathy syndrome.
DR PharmGKB; PA35808; -.
DR VEuPathDB; HostDB:ENSG00000140199; -.
DR eggNOG; KOG2082; Eukaryota.
DR GeneTree; ENSGT00940000160238; -.
DR HOGENOM; CLU_001883_1_2_1; -.
DR InParanoid; Q9UHW9; -.
DR OMA; KNWRPHI; -.
DR PhylomeDB; Q9UHW9; -.
DR TreeFam; TF313657; -.
DR PathwayCommons; Q9UHW9; -.
DR Reactome; R-HSA-426117; Cation-coupled Chloride cotransporters.
DR Reactome; R-HSA-5619039; Defective SLC12A6 causes agenesis of the corpus callosum, with peripheral neuropathy (ACCPN).
DR SignaLink; Q9UHW9; -.
DR SIGNOR; Q9UHW9; -.
DR BioGRID-ORCS; 9990; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; SLC12A6; human.
DR GeneWiki; SLC12A6; -.
DR GenomeRNAi; 9990; -.
DR Pharos; Q9UHW9; Tbio.
DR PRO; PR:Q9UHW9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UHW9; protein.
DR Bgee; ENSG00000140199; Expressed in esophagus squamous epithelium and 191 other tissues.
DR ExpressionAtlas; Q9UHW9; baseline and differential.
DR Genevisible; Q9UHW9; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0140157; P:ammonium import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0071476; P:cellular hypotonic response; IMP:ParkinsonsUK-UCL.
DR GO; GO:0071477; P:cellular hypotonic salinity response; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; 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:0006811; P:ion transport; IDA:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:ParkinsonsUK-UCL.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR030364; KCC3.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF66; PTHR11827:SF66; 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 3D-structure; Alternative promoter usage; Alternative splicing;
KW Cell membrane; Chloride; Glycoprotein; Ion transport; Membrane; Neuropathy;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1150
FT /note="Solute carrier family 12 member 6"
FT /id="PRO_0000178037"
FT TOPO_DOM 1..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..1150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16048901"
FT /id="VSP_041387"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10187864,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_006115"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16048901"
FT /id="VSP_041388"
FT VAR_SEQ 52..90
FT /note="PETSRSEPMSEMSGATTSLATVALDPPSDRTSHPQDVIE -> MPHFTVTKV
FT EDPEEGAAASISQEPSLADIKARIQDSDEP (in isoform 2 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:10187864,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_006116"
FT VAR_SEQ 91..105
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16048901"
FT /id="VSP_041389"
FT VARIANT 415
FT /note="F -> S (in dbSNP:rs2705339)"
FT /id="VAR_014960"
FT CONFLICT 802
FT /note="E -> H (in Ref. 1; AAF24986)"
FT /evidence="ECO:0000305"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:7AIN"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 216..241
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 269..292
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 312..335
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 344..364
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 404..408
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:6M1Y"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 499..503
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 512..541
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 553..557
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 570..599
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 605..610
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 621..635
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 639..666
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 681..696
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 701..723
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 729..745
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:6M1Y"
FT STRAND 759..762
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:7AIN"
FT HELIX 775..784
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 790..798
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 804..820
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 825..834
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 835..844
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 847..852
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 854..859
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 862..866
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 872..885
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 889..895
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 896..898
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 910..915
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 920..930
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:6M1Y"
FT TURN 935..938
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 940..947
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 954..965
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 966..968
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 971..977
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 980..982
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 984..987
FT /evidence="ECO:0007829|PDB:6M1Y"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:6M1Y"
FT TURN 991..993
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 994..1001
FT /evidence="ECO:0007829|PDB:6M1Y"
FT STRAND 1002..1004
FT /evidence="ECO:0007829|PDB:6M1Y"
FT STRAND 1008..1010
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 1015..1019
FT /evidence="ECO:0007829|PDB:6M1Y"
FT TURN 1081..1087
FT /evidence="ECO:0007829|PDB:6M22"
FT HELIX 1088..1098
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 1104..1107
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 1113..1116
FT /evidence="ECO:0007829|PDB:6M1Y"
FT HELIX 1118..1128
FT /evidence="ECO:0007829|PDB:6M22"
FT TURN 1129..1131
FT /evidence="ECO:0007829|PDB:6M22"
FT STRAND 1133..1139
FT /evidence="ECO:0007829|PDB:6M22"
SQ SEQUENCE 1150 AA; 127617 MW; F8BDD39181294EDD CRC64;
MHPPETTTKM ASVRFMVTPT KIDDIPGLSD TSPDLSSRSS SRVRFSSRES VPETSRSEPM
SEMSGATTSL ATVALDPPSD RTSHPQDVIE DLSQNSITGE HSQLLDDGHK KARNAYLNNS
NYEEGDEYFD KNLALFEEEM DTRPKVSSLL NRMANYTNLT QGAKEHEEAE NITEGKKKPT
KTPQMGTFMG VYLPCLQNIF GVILFLRLTW VVGTAGVLQA FAIVLICCCC TMLTAISMSA
IATNGVVPAG GSYFMISRAL GPEFGGAVGL CFYLGTTFAA AMYILGAIEI FLVYIVPRAA
IFHSDDALKE SAAMLNNMRV YGTAFLVLMV LVVFIGVRYV NKFASLFLAC VIVSILAIYA
GAIKSSFAPP HFPVCMLGNR TLSSRHIDVC SKTKEINNMT VPSKLWGFFC NSSQFFNATC
DEYFVHNNVT SIQGIPGLAS GIITENLWSN YLPKGEIIEK PSAKSSDVLG SLNHEYVLVD
ITTSFTLLVG IFFPSVTGIM AGSNRSGDLK DAQKSIPIGT ILAILTTSFV YLSNVVLFGA
CIEGVVLRDK FGDAVKGNLV VGTLSWPSPW VIVIGSFFST CGAGLQSLTG APRLLQAIAK
DNIIPFLRVF GHSKANGEPT WALLLTAAIA ELGILIASLD LVAPILSMFF LMCYLFVNLA
CALQTLLRTP NWRPRFRYYH WALSFMGMSI CLALMFISSW YYAIVAMVIA GMIYKYIEYQ
GAEKEWGDGI RGLSLSAARF ALLRLEEGPP HTKNWRPQLL VLLKLDEDLH VKHPRLLTFA
SQLKAGKGLT IVGSVIVGNF LENYGEALAA EQTIKHLMEA EKVKGFCQLV VAAKLREGIS
HLIQSCGLGG MKHNTVVMGW PNGWRQSEDA RAWKTFIGTV RVTTAAHLAL LVAKNISFFP
SNVEQFSEGN IDVWWIVHDG GMLMLLPFLL KQHKVWRKCS IRIFTVAQLE DNSIQMKKDL
ATFLYHLRIE AEVEVVEMHD SDISAYTYER TLMMEQRSQM LRHMRLSKTE RDREAQLVKD
RNSMLRLTSI GSDEDEETET YQEKVHMTWT KDKYMASRGQ KAKSMEGFQD LLNMRPDQSN
VRRMHTAVKL NEVIVNKSHE AKLVLLNMPG PPRNPEGDEN YMEFLEVLTE GLERVLLVRG
GGSEVITIYS
