ID   CLCN1_MOUSE             Reviewed;         994 AA.
AC   Q64347; Q8BZ41; Q9QVY5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Chloride channel protein 1;
DE            Short=ClC-1;
DE   AltName: Full=Chloride channel protein, skeletal muscle;
GN   Name=Clcn1; Synonyms=Clc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=9321463; DOI=10.1007/s003359900553;
RA   Schnuelle V., Antropova O., Gronemeier M., Wedemeyer N., Jockusch H.,
RA   Bartsch J.W.;
RT   "The mouse Clc1/myotonia gene: ETn insertion, a variable AATC repeat, and
RT   PCR diagnosis of alleles.";
RL   Mamm. Genome 8:718-725(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 350-467, AND TISSUE SPECIFICITY.
RX   PubMed=1659665; DOI=10.1038/354304a0;
RA   Steinmeyer K., Klocke R., Ortland C., Gronemeier M., Jockusch H.,
RA   Gruender S., Jentsch T.J.;
RT   "Inactivation of muscle chloride channel by transposon insertion in
RT   myotonic mice.";
RL   Nature 354:304-308(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 543-563; 740-760 AND 941-961, FUNCTION, AND
RP   MUTAGENESIS OF ILE-553.
RC   STRAIN=C57BL/6 X CBA/CaJ, and SWR/J;
RX   PubMed=8119941; DOI=10.1016/s0021-9258(17)37556-7;
RA   Gronemeier M., Condie A., Prosser J., Steinmeyer K., Jentsch T.J.,
RA   Jockusch H.;
RT   "Nonsense and missense mutations in the muscular chloride channel gene Clc-
RT   1 of myotonic mice.";
RL   J. Biol. Chem. 269:5963-5967(1994).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Voltage-gated chloride channel (By similarity). Plays an
CC       important role in membrane repolarization in skeletal muscle cells
CC       after muscle contraction (Probable) (PubMed:8119941).
CC       {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:8119941,
CC       ECO:0000305|PubMed:1659665}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in);
CC         Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P51798};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35523}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35523};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P35523}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscles.
CC       {ECO:0000269|PubMed:1659665}.
CC   -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC       and proton-coupled anion transporters that exchange chloride or another
CC       anion for protons. The absence of conserved gating glutamate residues
CC       is typical for family members that function as channels (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC       1/CLCN1 subfamily. {ECO:0000305}.
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DR   EMBL; Z95127; CAB08359.1; -; Genomic_DNA.
DR   EMBL; Z95128; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95129; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95130; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95131; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95132; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95133; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95134; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95135; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95136; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95137; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95138; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95139; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95140; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95141; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95142; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95143; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95144; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95145; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95146; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95147; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95148; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; Z95149; CAB08359.1; JOINED; Genomic_DNA.
DR   EMBL; AK036735; BAC29557.1; -; mRNA.
DR   EMBL; CH466533; EDL13488.1; -; Genomic_DNA.
DR   EMBL; BC114336; AAI14337.1; -; mRNA.
DR   EMBL; X62895; CAA44684.1; -; mRNA.
DR   EMBL; X62896; CAA44685.1; -; mRNA.
DR   EMBL; X62897; CAA44686.1; -; mRNA.
DR   CCDS; CCDS39471.1; -.
DR   PIR; I48773; I48773.
DR   RefSeq; NP_038519.1; NM_013491.2.
DR   AlphaFoldDB; Q64347; -.
DR   SMR; Q64347; -.
DR   STRING; 10090.ENSMUSP00000031894; -.
DR   iPTMnet; Q64347; -.
DR   PhosphoSitePlus; Q64347; -.
DR   PaxDb; 10090-ENSMUSP00000031894; -.
DR   ProteomicsDB; 285478; -.
DR   Antibodypedia; 32627; 168 antibodies from 23 providers.
DR   DNASU; 12723; -.
DR   Ensembl; ENSMUST00000031894.13; ENSMUSP00000031894.7; ENSMUSG00000029862.17.
DR   GeneID; 12723; -.
DR   KEGG; mmu:12723; -.
DR   UCSC; uc009bqs.1; mouse.
DR   AGR; MGI:88417; -.
DR   CTD; 1180; -.
DR   MGI; MGI:88417; Clcn1.
DR   VEuPathDB; HostDB:ENSMUSG00000029862; -.
DR   eggNOG; KOG0476; Eukaryota.
DR   GeneTree; ENSGT00940000157383; -.
DR   HOGENOM; CLU_006904_0_1_1; -.
DR   InParanoid; Q64347; -.
DR   OMA; QPYYYAD; -.
DR   OrthoDB; 1194at2759; -.
DR   PhylomeDB; Q64347; -.
DR   TreeFam; TF352264; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 12723; 5 hits in 77 CRISPR screens.
DR   PRO; PR:Q64347; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q64347; Protein.
DR   Bgee; ENSMUSG00000029862; Expressed in hindlimb stylopod muscle and 89 other cell types or tissues.
DR   ExpressionAtlas; Q64347; baseline and differential.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; ISS:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; IMP:MGI.
DR   GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   CDD; cd03683; ClC_1_like; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 2.
DR   Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR002243; Cl_channel-1.
DR   PANTHER; PTHR45720:SF4; CHLORIDE CHANNEL PROTEIN 1; 1.
DR   PANTHER; PTHR45720; CHLORIDE CHANNEL PROTEIN 2; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01112; CLCHANNEL1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF81340; Clc chloride channel; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   CBS domain; Cell membrane; Chloride; Chloride channel; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..994
FT                   /note="Chloride channel protein 1"
FT                   /id="PRO_0000094430"
FT   TOPO_DOM        1..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        119..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        151..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        180..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        184..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        196..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        229..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        247..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        291..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        322..347
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        348..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        377..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        391..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        409..414
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        415..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        427..457
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TRANSMEM        479..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        499..521
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        522..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        555..557
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        558..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P35523"
FT   TOPO_DOM        579..994
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          609..668
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          827..882
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          710..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           188..192
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           230..234
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           482..486
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        723..757
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..946
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         189
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   BINDING         484
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   BINDING         578
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         553
FT                   /note="I->T: Causes myotonia."
FT                   /evidence="ECO:0000269|PubMed:8119941"
FT   CONFLICT        65
FT                   /note="Q -> H (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="K -> Q (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76..78
FT                   /note="GGM -> RGI (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82..83
FT                   /note="MG -> TD (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="M -> V (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="A -> T (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483..484
FT                   /note="GF -> VN (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585
FT                   /note="K -> E (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="C -> S (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="A -> T (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        746
FT                   /note="N -> H (in Ref. 6; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        864
FT                   /note="R -> T (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        877
FT                   /note="E -> K (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        912
FT                   /note="G -> S (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        918..919
FT                   /note="DG -> GE (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        924
FT                   /note="G -> E (in Ref. 1; CAB08359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        944
FT                   /note="A -> V (in Ref. 6; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   994 AA;  109794 MW;  3C523C4325B279BF CRC64;
     MERSQSQRHG GEQSWWGSAP QYQYMPFEHC TSYGLPSENG GLQHRPRKDM GPRHNAHPTQ
     IYGHQKEQYS YKAQDGGMPK KMGSSSTMDS LDEDHYSKCQ DCVHRLGRVL RRKLGEDWIF
     LVLLGLLMAL VSWCMDYVSA KSLQAYKWTY AQMKPSLPLQ YLAWVTFPLI LILFSALFCQ
     LISPQAVGSG IPEMKTILRG VVLKEYLTLK AFVAKVVALT AGLGSGIPVG KEGPFVHIAS
     ICAAVLSKFM SMFSGVYEQP YYYTDILTVG CAVGVGCCFG TPLGGVLFSI EVTSTYFAVR
     NYWRGFFAAT FSAFVFRVLA VWNKDAVTIT ALFRTNFRMD FPFDLKELPA FAVIGICCGF
     LGAVFVYLHR QVMLGVRKHK CLSQFLAKHR LLYPGIVTFV IASLTFPPGM GQFMAGELMP
     REAISTLFDN NTWVKHIGDP QSLGQSAVWL HPQVNVIIII LLFFVMKFWM SIVATTMPIP
     CGGFMPVFVL GAAFGRLVGE IMAMLFPEGI LFDDIIYKIL PGGYAVIGAA ALTGAVSHTV
     STAVICFELT GQIAHILPMM VAVILANMVA QSLQPSLYDS IIQVKKLPYL PDLGWNQLSK
     FTIFVEDIMV RDVKFVSASC TYGELRNLLQ ATTVKTLPLV DSKDSMILLG SVERSELQSL
     LQRHLCAERR LKAAQDMARK LSELPYNGKA QLAGDWHPGG RPESFAFVDE DEDEDLSRKM
     ELPLTPAPPP PSPPPPPSQF PIAPSNPEEP NGPLPSHKQP PEASDSADQR SSTFQRLLHC
     LLGKAHSKKK KITQDSTDLV DNMSPEEIEA WEREQLSQPV CFDCCCIDQS PFQLVEQTTL
     HKTHTLFSLL GLHLAYVTSM GKLRGVLALE ELQKAIEGHT KSGVQLRPPL ASFRNTTSIR
     KTPGGPPPPA EGWNVPEDGD GAPGREVMVP TMPETPVPPP SPEAPSCLAP ARAEGELEEL
     EMVGSLEPEE ELADILHGPS LRSTDEEDED ELIL
//