LRCH3_HUMAN
ID LRCH3_HUMAN Reviewed; 777 AA.
AC Q96II8; B4E0T7; Q96FP9; Q9NT52;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DISP complex protein LRCH3 {ECO:0000305|PubMed:29467281};
DE AltName: Full=Leucine-rich repeat and calponin homology domain-containing protein 3 {ECO:0000312|HGNC:HGNC:28637};
GN Name=LRCH3 {ECO:0000312|HGNC:HGNC:28637};
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 575-777 (ISOFORM 3).
RC TISSUE=Brain, and Muscle;
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 624-777 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-415; SER-419;
RP SER-611 AND SER-628, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, IDENTIFICATION IN DISP COMPLEX, SUBCELLULAR LOCATION, CAUTION,
RP AND REGION.
RX PubMed=29467281; DOI=10.15252/embr.201744884;
RA O'Loughlin T., Masters T.A., Buss F.;
RT "The MYO6 interactome reveals adaptor complexes coordinating early endosome
RT and cytoskeletal dynamics.";
RL EMBO Rep. 19:0-0(2018).
CC -!- FUNCTION: As part of the DISP complex, may regulate the association of
CC septins with actin and thereby regulate the actin cytoskeleton.
CC {ECO:0000269|PubMed:29467281}.
CC -!- SUBUNIT: Component of the DOCK7-induced septin displacement/DISP
CC complex, at least composed of DOCK7, LRCH3 and MYO6.
CC {ECO:0000269|PubMed:29467281}.
CC -!- INTERACTION:
CC Q96II8; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-8795942, EBI-10174653;
CC Q96II8-3; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-17658306, EBI-742953;
CC Q96II8-3; Q86X45: DNAAF11; NbExp=3; IntAct=EBI-17658306, EBI-9379658;
CC Q96II8-3; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-17658306, EBI-357318;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:29467281}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96II8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96II8-2; Sequence=VSP_021044;
CC Name=3;
CC IsoId=Q96II8-3; Sequence=VSP_021043;
CC Name=4;
CC IsoId=Q96II8-4; Sequence=VSP_057212, VSP_057213;
CC -!- CAUTION: Predicted to contain a signal peptide and to be secreted.
CC However, this is not consistent with an interaction with DOCK7 and MYO6
CC and the suggested function in cytoskeleton organization.
CC {ECO:0000305|PubMed:29467281}.
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DR EMBL; AK303521; BAG64549.1; -; mRNA.
DR EMBL; AC055764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007504; AAH07504.1; -; mRNA.
DR EMBL; BC010565; AAH10565.1; -; mRNA.
DR EMBL; AL137527; CAB70791.1; -; mRNA.
DR CCDS; CCDS3330.1; -. [Q96II8-3]
DR CCDS; CCDS87193.1; -. [Q96II8-2]
DR PIR; T46371; T46371.
DR RefSeq; NP_116162.1; NM_032773.3. [Q96II8-3]
DR RefSeq; XP_005269419.1; XM_005269362.2.
DR RefSeq; XP_006713854.1; XM_006713791.3.
DR AlphaFoldDB; Q96II8; -.
DR SMR; Q96II8; -.
DR BioGRID; 124307; 97.
DR IntAct; Q96II8; 46.
DR MINT; Q96II8; -.
DR STRING; 9606.ENSP00000334375; -.
DR iPTMnet; Q96II8; -.
DR MetOSite; Q96II8; -.
DR PhosphoSitePlus; Q96II8; -.
DR BioMuta; LRCH3; -.
DR DMDM; 116248531; -.
DR EPD; Q96II8; -.
DR jPOST; Q96II8; -.
DR MassIVE; Q96II8; -.
DR MaxQB; Q96II8; -.
DR PaxDb; Q96II8; -.
DR PeptideAtlas; Q96II8; -.
DR PRIDE; Q96II8; -.
DR ProteomicsDB; 5699; -.
DR ProteomicsDB; 76830; -. [Q96II8-1]
DR ProteomicsDB; 76831; -. [Q96II8-2]
DR ProteomicsDB; 76832; -. [Q96II8-3]
DR Antibodypedia; 2704; 96 antibodies from 18 providers.
DR DNASU; 84859; -.
DR Ensembl; ENST00000334859.8; ENSP00000334375.4; ENSG00000186001.14. [Q96II8-3]
DR Ensembl; ENST00000414675.6; ENSP00000394965.2; ENSG00000186001.14. [Q96II8-4]
DR Ensembl; ENST00000425562.7; ENSP00000393579.2; ENSG00000186001.14. [Q96II8-1]
DR Ensembl; ENST00000428136.2; ENSP00000394763.2; ENSG00000186001.14. [Q96II8-2]
DR Ensembl; ENST00000438796.6; ENSP00000399751.2; ENSG00000186001.14. [Q96II8-2]
DR GeneID; 84859; -.
DR KEGG; hsa:84859; -.
DR MANE-Select; ENST00000425562.7; ENSP00000393579.2; NM_001365715.1; NP_001352644.1.
DR UCSC; uc003fyj.1; human. [Q96II8-1]
DR CTD; 84859; -.
DR GeneCards; LRCH3; -.
DR HGNC; HGNC:28637; LRCH3.
DR HPA; ENSG00000186001; Low tissue specificity.
DR neXtProt; NX_Q96II8; -.
DR OpenTargets; ENSG00000186001; -.
DR PharmGKB; PA134923024; -.
DR VEuPathDB; HostDB:ENSG00000186001; -.
DR eggNOG; KOG0532; Eukaryota.
DR GeneTree; ENSGT00940000158330; -.
DR HOGENOM; CLU_008231_2_0_1; -.
DR InParanoid; Q96II8; -.
DR OMA; LYSWIFP; -.
DR OrthoDB; 378148at2759; -.
DR PhylomeDB; Q96II8; -.
DR TreeFam; TF318428; -.
DR PathwayCommons; Q96II8; -.
DR SignaLink; Q96II8; -.
DR BioGRID-ORCS; 84859; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; LRCH3; human.
DR GenomeRNAi; 84859; -.
DR Pharos; Q96II8; Tdark.
DR PRO; PR:Q96II8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96II8; protein.
DR Bgee; ENSG00000186001; Expressed in sural nerve and 183 other tissues.
DR ExpressionAtlas; Q96II8; baseline and differential.
DR Genevisible; Q96II8; HS.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0032185; P:septin cytoskeleton organization; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00033; CH; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..777
FT /note="DISP complex protein LRCH3"
FT /id="PRO_0000253484"
FT REPEAT 56..79
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 81..104
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 105..127
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 128..150
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 152..172
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 173..195
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 196..218
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 220..239
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 240..264
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 266..290
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 652..765
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 56..290
FT /note="Mediates interaction with DOCK7"
FT /evidence="ECO:0000269|PubMed:29467281"
FT REGION 382..648
FT /note="Mediates direct interaction with MYO6"
FT /evidence="ECO:0000269|PubMed:29467281"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 389..416
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057212"
FT VAR_SEQ 549..572
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057213"
FT VAR_SEQ 711..777
FT /note="PKLTMAKCRRNVENFLEACRKIGVPQEQLCLPLHILEEKGLSQVAVTVQALL
FT ELAPPKQQQHQLSAV -> VS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021043"
FT VAR_SEQ 737..777
FT /note="EQLCLPLHILEEKGLSQVAVTVQALLELAPPKQQQHQLSAV -> DNLCSPS
FT DILQLNLSVKRTVETLLSLGAHSEESSFVCLSLQLLGFVAFYCTVMLTLCVLYYWLFPA
FT R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021044"
FT VARIANT 522
FT /note="P -> L (in dbSNP:rs36078463)"
FT /id="VAR_056931"
SQ SEQUENCE 777 AA; 86083 MW; AB317F58DB98AB4A CRC64;
MAAAGLVAVA AAAEYSGTVA SGGNLPGVHC GPSSGAGPGF GPGSWSRSLD RALEEAAVTG
VLSLSGRKLR EFPRGAANHD LTDTTRADLS RNRLSEIPIE ACHFVSLENL NLYQNCIRYI
PEAILNLQAL TFLNISRNQL STLPVHLCNL PLKVLIASNN KLVSLPEEIG HLRHLMELDV
SCNEIQTIPS QIGNLEALRD LNVRRNHLVH LPEELAELPL IRLDFSCNKI TTIPVCYRNL
RHLQTITLDN NPLQSPPAQI CIKGKVHIFK YLNIQACKIA PDLPDYDRRP LGFGSCHEEL
YSSRPYGALD SGFNSVDSGD KRWSGNEPTD EFSDLPLRVA EITKEQRLRR ESQYQENRGS
LVVTNGGVEH DLDQIDYIDS CTAEEEEAEV RQPKGPDPDS LSSQFMAYIE QRRISHEGSP
VKPVAIREFQ KTEDMRRYLH QNRVPAEPSS LLSLSASHNQ LSHTDLELHQ RREQLVERTR
REAQLAALQY EEEKIRTKQI QRDAVLDFVK QKASQSPQKQ HPLLDGVDGE CPFPSRRSQH
TDDSALCMSL SGLNQVGCAA TLPHSSAFTP LKSDDRPNAL LSSPATETVH HSPAYSFPAA
IQRNQPQRPE SFLFRAGVRA ETNKGHASPL PPSAAPTTDS TDSITGQNSR QREEELELID
QLRKHIEYRL KVSLPCDLGA ALTDGVVLCH LANHVRPRSV PSIHVPSPAV PKLTMAKCRR
NVENFLEACR KIGVPQEQLC LPLHILEEKG LSQVAVTVQA LLELAPPKQQ QHQLSAV
