CLCN1_MOUSE
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 03-AUG-2022, entry version 166.
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; Q64347; -.
DR PRIDE; Q64347; -.
DR ProteomicsDB; 285478; -.
DR Antibodypedia; 32627; 151 antibodies from 23 providers.
DR DNASU; 12723; -.
DR Ensembl; ENSMUST00000031894; ENSMUSP00000031894; ENSMUSG00000029862.
DR GeneID; 12723; -.
DR KEGG; mmu:12723; -.
DR UCSC; uc009bqs.1; mouse.
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; FFANCTW; -.
DR OrthoDB; 1131873at2759; -.
DR PhylomeDB; Q64347; -.
DR TreeFam; TF352264; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 12723; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q64347; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q64347; protein.
DR Bgee; ENSMUSG00000029862; Expressed in hindlimb stylopod muscle and 86 other tissues.
DR ExpressionAtlas; Q64347; baseline and differential.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of 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 GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; -; 2.
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 Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01112; CLCHANNEL1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 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
