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   27-MAR-2024, entry version 162.
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; 67.
DR   IntAct; Q9BXP2; 20.
DR   STRING; 9606.ENSP00000275730; -.
DR   TCDB; 2.A.30.1.6; the cation-chloride cotransporter (ccc) family.
DR   GlyCosmos; Q9BXP2; 2 sites, No reported glycans.
DR   GlyGen; Q9BXP2; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BXP2; -.
DR   PhosphoSitePlus; Q9BXP2; -.
DR   SwissPalm; Q9BXP2; -.
DR   BioMuta; SLC12A9; -.
DR   DMDM; 74752435; -.
DR   EPD; Q9BXP2; -.
DR   jPOST; Q9BXP2; -.
DR   MassIVE; Q9BXP2; -.
DR   MaxQB; Q9BXP2; -.
DR   PaxDb; 9606-ENSP00000275730; -.
DR   PeptideAtlas; Q9BXP2; -.
DR   ProteomicsDB; 27743; -.
DR   ProteomicsDB; 79472; -. [Q9BXP2-1]
DR   ProteomicsDB; 79473; -. [Q9BXP2-2]
DR   ProteomicsDB; 79474; -. [Q9BXP2-3]
DR   Pumba; Q9BXP2; -.
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   AGR; HGNC:17435; -.
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; VANVFSC; -.
DR   OrthoDB; 5490251at2759; -.
DR   PhylomeDB; Q9BXP2; -.
DR   TreeFam; TF313191; -.
DR   PathwayCommons; Q9BXP2; -.
DR   SignaLink; Q9BXP2; -.
DR   BioGRID-ORCS; 56996; 25 hits in 1179 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 162 other cell types or tissues.
DR   ExpressionAtlas; Q9BXP2; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015377; F:chloride:monoatomic cation 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   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR018491; SLC12_C.
DR   InterPro; IPR004842; SLC12A_fam.
DR   PANTHER; PTHR11827:SF98; SOLUTE CARRIER FAMILY 12 MEMBER 9; 1.
DR   PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   Pfam; PF03522; SLC12; 1.
DR   Genevisible; Q9BXP2; HS.
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
//