ID H0YMQ9_HUMAN Unreviewed; 906 AA.
AC H0YMQ9; A0A024R9N4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Solute carrier family 12 (Potassium/chloride transporters), member 6, isoform CRA_c {ECO:0000313|EMBL:EAW92298.1};
DE SubName: Full=Solute carrier family 12 member 6 {ECO:0000313|Ensembl:ENSP00000453702.1};
GN Name=SLC12A6 {ECO:0000313|EMBL:EAW92298.1,
GN ECO:0000313|Ensembl:ENSP00000453702.1};
GN ORFNames=hCG_1998565 {ECO:0000313|EMBL:EAW92298.1};
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 {ECO:0000313|Ensembl:ENSP00000453702.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|EMBL:EAW92298.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11181995; DOI=10.1126/science.1058040;
RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT "The sequence of the human genome.";
RL Science 291:1304-1351(2001).
RN [2] {ECO:0000313|EMBL:EAW92298.1}
RP NUCLEOTIDE SEQUENCE.
RA Mural R.J., Istrail S., Sutton 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 [3] {ECO:0000313|Ensembl:ENSP00000453702.1, ECO:0000313|Proteomes:UP000005640}
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., Stewart S.,
RA Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R.,
RA 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 [4] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
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).
RN [7] {ECO:0000313|Ensembl:ENSP00000453702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) + K(+)(in) = chloride(out) + K(+)(out);
CC Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00034453};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC {ECO:0000256|ARBA:ARBA00010593}.
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DR EMBL; AC021822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92298.1; -; Genomic_DNA.
DR ProteomicsDB; 40329; -.
DR Ensembl; ENST00000559664.5; ENSP00000453702.1; ENSG00000140199.13.
DR Ensembl; ENST00000561080.5; ENSP00000454069.1; ENSG00000140199.13.
DR UCSC; uc059hhd.1; human.
DR HGNC; HGNC:10914; SLC12A6.
DR VEuPathDB; HostDB:ENSG00000140199; -.
DR GeneTree; ENSGT00940000160238; -.
DR ChiTaRS; SLC12A6; human.
DR Proteomes; UP000005640; Chromosome 15.
DR Bgee; ENSG00000140199; Expressed in esophagus squamous epithelium and 192 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR NCBIfam; TIGR00930; 2a30; 1.
DR PANTHER; PTHR11827:SF66; SOLUTE CARRIER FAMILY 12 MEMBER 6; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 1.
DR PRINTS; PR01081; KCLTRNSPORT.
PE 1: Evidence at protein level;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Proteomics identification {ECO:0007829|EPD:H0YMQ9,
KW ECO:0007829|MaxQB:H0YMQ9};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Symport {ECO:0000256|ARBA:ARBA00022847};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022847}.
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..363
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 482..760
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 774..878
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
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"
SQ SEQUENCE 906 AA; 99266 MW; 20D65B400C1997D6 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 RAWKTFIAMW SNFLRATLMC GGLCMMGGCL
CYYHSY
//
