S12A9_HUMAN
ID S12A9_HUMAN Reviewed; 914 AA.
AC Q9BXP2; B7Z740; D6W5X0; D6W5X2; F5H8C2; Q9BWL2; Q9BXP1; Q9BYI0; Q9NQR5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Solute carrier family 12 member 9;
DE AltName: Full=Cation-chloride cotransporter 6;
DE Short=hCCC6;
DE AltName: Full=Cation-chloride cotransporter-interacting protein 1;
DE Short=CCC-interacting protein 1;
DE Short=hCIP1;
DE AltName: Full=Potassium-chloride transporter 9;
DE AltName: Full=WO3.3;
GN Name=SLC12A9; Synonyms=CCC6, CIP1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH SLC12A1.
RC TISSUE=Heart;
RX PubMed=10871601; DOI=10.1074/jbc.m000108200;
RA Caron L., Rousseau F., Gagnon E., Isenring P.;
RT "Cloning and functional characterization of a cation-Cl-cotransporter-
RT interacting protein.";
RL J. Biol. Chem. 275:32027-32036(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ishibashi K.;
RT "Molecular cloning of human cation chloride cotransporter 6.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Synovium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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: 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. {ECO:0000269|PubMed:10871601}.
CC -!- SUBUNIT: Interacts with SLC12A1. {ECO:0000269|PubMed:10871601}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10871601};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10871601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BXP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXP2-2; Sequence=VSP_033192, VSP_033193, VSP_033194;
CC Name=3;
CC IsoId=Q9BXP2-3; Sequence=VSP_033193, VSP_033194;
CC Name=4;
CC IsoId=Q9BXP2-4; Sequence=VSP_045591, VSP_045592;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, brain and kidney.
CC Lower expression in lung, liver and heart.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; AF284422; AAF88060.1; -; mRNA.
DR EMBL; AF312032; AAK21008.1; -; Genomic_DNA.
DR EMBL; AF312032; AAK21009.1; -; Genomic_DNA.
DR EMBL; AB033284; BAB40456.1; -; mRNA.
DR EMBL; AK301411; BAH13476.1; -; mRNA.
DR EMBL; AC011895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23818.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76475.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76476.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76483.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76480.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76484.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76485.1; -; Genomic_DNA.
DR EMBL; BC000154; AAH00154.1; -; mRNA.
DR CCDS; CCDS5707.1; -. [Q9BXP2-1]
DR CCDS; CCDS59068.1; -. [Q9BXP2-4]
DR CCDS; CCDS59069.1; -. [Q9BXP2-2]
DR RefSeq; NP_001254741.1; NM_001267812.1. [Q9BXP2-4]
DR RefSeq; NP_001254743.1; NM_001267814.1. [Q9BXP2-2]
DR RefSeq; NP_064631.2; NM_020246.3. [Q9BXP2-1]
DR AlphaFoldDB; Q9BXP2; -.
DR SMR; Q9BXP2; -.
DR BioGRID; 121311; 65.
DR IntAct; Q9BXP2; 19.
DR STRING; 9606.ENSP00000275730; -.
DR TCDB; 2.A.30.1.6; the cation-chloride cotransporter (ccc) family.
DR GlyGen; Q9BXP2; 2 sites.
DR iPTMnet; Q9BXP2; -.
DR PhosphoSitePlus; Q9BXP2; -.
DR BioMuta; SLC12A9; -.
DR DMDM; 74752435; -.
DR EPD; Q9BXP2; -.
DR jPOST; Q9BXP2; -.
DR MassIVE; Q9BXP2; -.
DR MaxQB; Q9BXP2; -.
DR PaxDb; Q9BXP2; -.
DR PeptideAtlas; Q9BXP2; -.
DR PRIDE; Q9BXP2; -.
DR ProteomicsDB; 27743; -.
DR ProteomicsDB; 79472; -. [Q9BXP2-1]
DR ProteomicsDB; 79473; -. [Q9BXP2-2]
DR ProteomicsDB; 79474; -. [Q9BXP2-3]
DR Antibodypedia; 74017; 36 antibodies from 9 providers.
DR DNASU; 56996; -.
DR Ensembl; ENST00000354161.8; ENSP00000275730.4; ENSG00000146828.18. [Q9BXP2-1]
DR Ensembl; ENST00000415287.5; ENSP00000413796.1; ENSG00000146828.18. [Q9BXP2-2]
DR Ensembl; ENST00000540482.5; ENSP00000443702.1; ENSG00000146828.18. [Q9BXP2-4]
DR GeneID; 56996; -.
DR KEGG; hsa:56996; -.
DR MANE-Select; ENST00000354161.8; ENSP00000275730.4; NM_020246.4; NP_064631.2.
DR UCSC; uc003uwp.5; human. [Q9BXP2-1]
DR CTD; 56996; -.
DR DisGeNET; 56996; -.
DR GeneCards; SLC12A9; -.
DR HGNC; HGNC:17435; SLC12A9.
DR HPA; ENSG00000146828; Low tissue specificity.
DR MalaCards; SLC12A9; -.
DR MIM; 616861; gene.
DR neXtProt; NX_Q9BXP2; -.
DR OpenTargets; ENSG00000146828; -.
DR PharmGKB; PA134921585; -.
DR VEuPathDB; HostDB:ENSG00000146828; -.
DR eggNOG; KOG1288; Eukaryota.
DR GeneTree; ENSGT00940000159400; -.
DR HOGENOM; CLU_001883_5_0_1; -.
DR InParanoid; Q9BXP2; -.
DR OMA; NAGLYVT; -.
DR OrthoDB; 515568at2759; -.
DR PhylomeDB; Q9BXP2; -.
DR TreeFam; TF313191; -.
DR PathwayCommons; Q9BXP2; -.
DR SignaLink; Q9BXP2; -.
DR BioGRID-ORCS; 56996; 21 hits in 1087 CRISPR screens.
DR ChiTaRS; SLC12A9; human.
DR GeneWiki; SLC12A9; -.
DR GenomeRNAi; 56996; -.
DR Pharos; Q9BXP2; Tdark.
DR PRO; PR:Q9BXP2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BXP2; protein.
DR Bgee; ENSG00000146828; Expressed in granulocyte and 160 other tissues.
DR ExpressionAtlas; Q9BXP2; baseline and differential.
DR Genevisible; Q9BXP2; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015377; F:cation:chloride symporter activity; TAS:ProtInc.
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 Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..914
FT /note="Solute carrier family 12 member 9"
FT /id="PRO_0000331415"
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..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..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 642..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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 VAR_SEQ 61..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033192"
FT VAR_SEQ 620..631
FT /note="GGMKPNTLVLGF -> ESGTLLPWGFRS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045591"
FT VAR_SEQ 620..627
FT /note="GGMKPNTL -> ESNSHPLP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033193"
FT VAR_SEQ 628..914
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033194"
FT VAR_SEQ 632..914
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045592"
FT CONFLICT 10
FT /note="A -> T (in Ref. 4; BAH13476)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="T -> S (in Ref. 3; BAB40456)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="S -> A (in Ref. 3; BAB40456)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="S -> N (in Ref. 1; AAF88060)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="L -> F (in Ref. 1; AAF88060)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="E -> K (in Ref. 3; BAB40456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 96110 MW; 8096855B78078CA4 CRC64;
MASESSPLLA YRLLGEEGVA LPANGAGGPG GASARKLSTF LGVVVPTVLS MFSIVVFLRI
GFVVGHAGLL QALAMLLVAY FILALTVLSV CAIATNGAVQ GGGAYFMISR TLGPEVGGSI
GLMFYLANVC GCAVSLLGLV ESVLDVFGAD ATGPSGLRVL PQGYGWNLLY GSLLLGLVGG
VCTLGAGLYA RASFLTFLLV SGSLASVLIS FVAVGPRDIR LTPRPGPNGS SLPPRFGHFT
GFNSSTLKDN LGAGYAEDYT TGAVMNFASV FAVLFNGCTG IMAGANMSGE LKDPSRAIPL
GTIVAVAYTF FVYVLLFFLS SFTCDRTLLQ EDYGFFRAIS LWPPLVLIGI YATALSASMS
SLIGASRILH ALARDDLFGV ILAPAKVVSR GGNPWAAVLY SWGLVQLVLL AGKLNTLAAV
VTVFYLVAYA AVDLSCLSLE WASAPNFRPT FSLFSWHTCL LGVASCLLMM FLISPGAAGG
SLLLMGLLAA LLTARGGPSS WGYVSQALLF HQVRKYLLRL DVRKDHVKFW RPQLLLLVGN
PRGALPLLRL ANQLKKGGLY VLGHVTLGDL DSLPSDPVQP QYGAWLSLVD RAQVKAFVDL
TLSPSVRQGA QHLLRISGLG GMKPNTLVLG FYDDAPPQDH FLTDPAFSEP ADSTREGSSP
ALSTLFPPPR APGSPRALNP QDYVATVADA LKMNKNVVLA RASGALPPER LSRGSGGTSQ
LHHVDVWPLN LLRPRGGPGY VDVCGLFLLQ MATILGMVPA WHSARLRIFL CLGPREAPGA
AEGRLRALLS QLRIRAEVQE VVWGEGAGAG EPEAEEEGDF VNSGRGDAEA EALARSANAL
VRAQQGRGTG GGPGGPEGGD AEGPITALTF LYLPRPPADP ARYPRYLALL ETLTRDLGPT
LLVHGVTPVT CTDL