LIMC1_MOUSE
ID LIMC1_MOUSE Reviewed; 1057 AA.
AC Q3UH68; Q6DIC3; Q80TK1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=LIM and calponin homology domains-containing protein 1 {ECO:0000305};
GN Name=Limch1 {ECO:0000312|MGI:MGI:1924819};
GN Synonyms=Kiaa1102 {ECO:0000312|EMBL:BAC65725.1};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-1057 (ISOFORM 1).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-973, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-201; SER-204;
RP SER-207; THR-215; SER-217; SER-226; SER-231; SER-233; TYR-313; SER-471;
RP THR-472; SER-672; SER-719; SER-751; SER-757; SER-760 AND THR-899, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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: Actin stress fibers-associated protein that activates non-
CC muscle myosin IIa. Activates the non-muscle myosin IIa complex by
CC promoting the phosphorylation of its regulatory subunit MRLC/MYL9.
CC Through the activation of non-muscle myosin IIa, positively regulates
CC actin stress fibers assembly and stabilizes focal adhesions. It
CC therefore negatively regulates cell spreading and cell migration.
CC {ECO:0000250|UniProtKB:Q9UPQ0}.
CC -!- SUBUNIT: Interacts with MYH9; independently of the integration of MYH9
CC into the myosin complex. {ECO:0000250|UniProtKB:Q9UPQ0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q9UPQ0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UH68-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UH68-2; Sequence=VSP_026551, VSP_026553;
CC Name=3;
CC IsoId=Q3UH68-3; Sequence=VSP_026552, VSP_026554;
CC -!- SIMILARITY: Belongs to the LIMCH1 family. {ECO:0000305}.
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DR EMBL; AK134095; BAE22010.1; -; mRNA.
DR EMBL; AK147547; BAE27989.1; -; mRNA.
DR EMBL; AC119834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075634; AAH75634.1; -; mRNA.
DR EMBL; AK122443; BAC65725.1; -; mRNA.
DR CCDS; CCDS39102.1; -. [Q3UH68-1]
DR CCDS; CCDS57347.1; -. [Q3UH68-2]
DR RefSeq; NP_001001980.2; NM_001001980.2. [Q3UH68-1]
DR RefSeq; NP_001243051.1; NM_001256122.1. [Q3UH68-2]
DR AlphaFoldDB; Q3UH68; -.
DR SMR; Q3UH68; -.
DR BioGRID; 218768; 9.
DR IntAct; Q3UH68; 3.
DR MINT; Q3UH68; -.
DR STRING; 10090.ENSMUSP00000098723; -.
DR iPTMnet; Q3UH68; -.
DR PhosphoSitePlus; Q3UH68; -.
DR MaxQB; Q3UH68; -.
DR PaxDb; Q3UH68; -.
DR PeptideAtlas; Q3UH68; -.
DR PRIDE; Q3UH68; -.
DR ProteomicsDB; 292254; -. [Q3UH68-1]
DR ProteomicsDB; 292255; -. [Q3UH68-2]
DR ProteomicsDB; 292256; -. [Q3UH68-3]
DR Antibodypedia; 1336; 72 antibodies from 17 providers.
DR DNASU; 77569; -.
DR Ensembl; ENSMUST00000038188; ENSMUSP00000043163; ENSMUSG00000037736. [Q3UH68-2]
DR Ensembl; ENSMUST00000101164; ENSMUSP00000098723; ENSMUSG00000037736. [Q3UH68-1]
DR GeneID; 77569; -.
DR KEGG; mmu:77569; -.
DR UCSC; uc008xph.1; mouse. [Q3UH68-1]
DR UCSC; uc008xpj.1; mouse. [Q3UH68-2]
DR CTD; 22998; -.
DR MGI; MGI:1924819; Limch1.
DR VEuPathDB; HostDB:ENSMUSG00000037736; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183159; -.
DR HOGENOM; CLU_003242_1_0_1; -.
DR InParanoid; Q3UH68; -.
DR OrthoDB; 298177at2759; -.
DR TreeFam; TF332155; -.
DR BioGRID-ORCS; 77569; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Limch1; mouse.
DR PRO; PR:Q3UH68; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UH68; protein.
DR Bgee; ENSMUSG00000037736; Expressed in sciatic nerve and 246 other tissues.
DR ExpressionAtlas; Q3UH68; baseline and differential.
DR Genevisible; Q3UH68; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016460; C:myosin II complex; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032034; F:myosin II head/neck binding; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR029980; LIMCH1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15551:SF3; PTHR15551:SF3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00889; CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1057
FT /note="LIM and calponin homology domains-containing protein
FT 1"
FT /id="PRO_0000293620"
FT DOMAIN 21..128
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 985..1051
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 185..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..641
FT /note="Mediates interaction with MYH9"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT REGION 373..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..439
FT /evidence="ECO:0000255"
FT COILED 782..823
FT /evidence="ECO:0000255"
FT COMPBIAS 185..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 313
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 725
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ0"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 899
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026551"
FT VAR_SEQ 1..13
FT /note="MACPALGLEVLQP -> MHKTCTIRSFIRDFYRILFTCARPSIMSDDAESTS
FT MFDMRCEEEAAVLPHSRARQEQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026552"
FT VAR_SEQ 157..162
FT /note="LAQMRK -> MDPERQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026553"
FT VAR_SEQ 199..398
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026554"
FT CONFLICT 682
FT /note="S -> P (in Ref. 3; AAH75634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1057 AA; 118196 MW; 3989AAF7718E320C CRC64;
MACPALGLEV LQPLQPEPPP EPAFAEAQKW IEQVTGRSFG DKDFRTGLEN GILLCELLNA
IKPGLVKKIN RLPTPIAGLD NTILFLRGCK ELGLKESQLF DPSDLQDTSN RVTVKNLDYS
RKLKNVLVTI YWLGKAANSC ASYGGTTLNL KEFEGLLAQM RKETDDIDSP KRSIRDSGYI
DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSRQTPSPDV VLRGSSDGRG SDSESDLPHR
KLPDVKKDDM SARRTSHGEP KSAVPFNQYL PNKSNQTAYV PAPLRKKKAE REEFRKSWST
ATSPLGGERP FRYGPRTPVS DDAESTSMFD MRCEEEAAVL PHSRARQEQL QLINNQLREE
DDKWQDDLAR WKSRRRSASQ DLIKKEEERK KMEKLMSGED GTSERRKSIK TYREIVQEKE
RRERELHEAY KNARSQEEAE GILQQYIERF TISEAVLERL EMPKILERSH STEPNVSSFP
NDPSPMKYLR QQSLPPPKFT ATVETTIART SVPESIASAG TGSPSKIITP NTVPMLTPRP
YSQPKNSQEV LKTFKVDGKV SMNGEMAPGD EEGKEKEGPA AAAPGPSLTK SQMFEGVATV
HDSPVQVKQG SNSIEINIKK PNSAPQELTA ASEETESNGQ EDEDGEERPG TGDLEPDSAE
PQHFTTTVTR CSPTVALVEF SSNPQLKNEV PEQGQKKPED EMSGKVELVL SQKVAKPKSP
EPEATLTFPF LDKMPETNQL HLPNPSSQAD SPSSEKSPGS TPFKFWAWDP EEERRRQEKW
QQEQERLLQE RYQKEQDKLK EEWEKAQKEV EEEERRYYEE ERKIIEDTVV PFTISSSSAD
QLSTSLSVTE GSGTRNKMDL ENCPDKENER RQKTPFQEND GDSLLKTREG GLPEEQSLTP
SPSANPEISV SKGIHQDPQL EAEAGAPHCG TNPQPAQDPP RNQQIPNPPT STSEDVKPKT
LALEKTINHQ MESPGERRKS ISGKKLCSSC GLTLGKGAAM IIETLNLYFH IQCFRCGICK
GQLGDAVSGT DVRIRNGLLN CTDCYMRSRS AGQPTTL
