WASH1_MOUSE
ID WASH1_MOUSE Reviewed; 475 AA.
AC Q8VDD8; Q3U473;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=WASH complex subunit 1 {ECO:0000312|MGI:MGI:1916017};
DE AltName: Full=WAS protein family homolog 1;
GN Name=Washc1 {ECO:0000312|MGI:MGI:1916017}; Synonyms=Orf19, Wash, Wash1;
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 [MRNA].
RX PubMed=10655549; DOI=10.1093/hmg/9.3.395;
RA Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
RA Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
RA Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S.,
RA Mercadante G., Pannone E., Archidiacono N., Rocchi M., Schlessinger D.,
RA D'Urso M.;
RT "Differentially regulated and evolved genes in the fully sequenced Xq/Yq
RT pseudoautosomal region.";
RL Hum. Mol. Genet. 9:395-401(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Cecum, and Spleen;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19732055; DOI=10.1111/j.1462-5822.2009.01380.x;
RA Haenisch J., Ehinger J., Ladwein M., Rohde M., Derivery E., Bosse T.,
RA Steffen A., Bumann D., Misselwitz B., Hardt W.D., Gautreau A.,
RA Stradal T.E., Rottner K.;
RT "Molecular dissection of Salmonella-induced membrane ruffling versus
RT invasion.";
RL Cell. Microbiol. 12:84-98(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BLOC1S2 AND TUBULIN GAMMA CHAIN.
RX PubMed=20308062; DOI=10.1074/jbc.m109.078501;
RA Monfregola J., Napolitano G., D'Urso M., Lappalainen P., Ursini M.V.;
RT "Functional characterization of Wiskott-Aldrich syndrome protein and scar
RT homolog (WASH), a bi-modular nucleation-promoting factor able to interact
RT with biogenesis of lysosome-related organelle subunit 2 (BLOS2) and gamma-
RT tubulin.";
RL J. Biol. Chem. 285:16951-16957(2010).
RN [8]
RP FUNCTION.
RX PubMed=22114305; DOI=10.1242/jcs.080986;
RA Zech T., Calaminus S.D., Caswell P., Spence H.J., Carnell M., Insall R.H.,
RA Norman J., Machesky L.M.;
RT "The Arp2/3 activator WASH regulates alpha5beta1-integrin-mediated invasive
RT migration.";
RL J. Cell Sci. 124:3753-3759(2011).
RN [9]
RP FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1.
RX PubMed=23974797; DOI=10.1038/emboj.2013.189;
RA Xia P., Wang S., Du Y., Zhao Z., Shi L., Sun L., Huang G., Ye B., Li C.,
RA Dai Z., Hou N., Cheng X., Sun Q., Li L., Yang X., Fan Z.;
RT "WASH inhibits autophagy through suppression of Beclin 1 ubiquitination.";
RL EMBO J. 32:2685-2696(2013).
RN [10]
RP FUNCTION.
RX PubMed=23275443; DOI=10.1128/mcb.01288-12;
RA Piotrowski J.T., Gomez T.S., Schoon R.A., Mangalam A.K., Billadeau D.D.;
RT "WASH knockout T cells demonstrate defective receptor trafficking,
RT proliferation, and effector function.";
RL Mol. Cell. Biol. 33:958-973(2013).
RN [11]
RP FUNCTION.
RX PubMed=24886983; DOI=10.1371/journal.pone.0098606;
RA Graham D.B., Osborne D.G., Piotrowski J.T., Gomez T.S., Gmyrek G.B.,
RA Akilesh H.M., Dani A., Billadeau D.D., Swat W.;
RT "Dendritic cells utilize the evolutionarily conserved WASH and retromer
RT complexes to promote MHCII recycling and helper T cell priming.";
RL PLoS ONE 9:E98606-E98606(2014).
RN [12]
RP FUNCTION.
RX PubMed=24998208; DOI=10.1038/srep05596;
RA Wang F., Zhang L., Zhang G.L., Wang Z.B., Cui X.S., Kim N.H., Sun S.C.;
RT "WASH complex regulates Arp2/3 complex for actin-based polar body extrusion
RT in mouse oocytes.";
RL Sci. Rep. 4:5596-5596(2014).
RN [13]
RP INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: Acts as component of the WASH core complex that functions as
CC a nucleation-promoting factor (NPF) at the surface of endosomes, where
CC it recruits and activates the Arp2/3 complex to induce actin
CC polymerization, playing a key role in the fission of tubules that serve
CC as transport intermediates during endosome sorting (PubMed:19922875).
CC Regulates the trafficking of endosomal alpha5beta1 integrin to the
CC plasma membrane and involved in invasive cell migration
CC (PubMed:22114305). In T-cells involved in endosome-to-membrane
CC recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL;
CC proposed to be implicated in T-cell proliferation and effector function
CC (PubMed:23275443). In dendritic cells involved in endosome-to-membrane
CC recycling of major histocompatibility complex (MHC) class II probably
CC involving retromer and subsequently allowing antigen sampling, loading
CC and presentation during T-cell activation (PubMed:24886983). Involved
CC in cytokinesis and following polar body extrusion during oocyte meiotic
CC maturation (PubMed:24998208). Involved in Arp2/3 complex-dependent
CC actin assembly driving Salmonella typhimurium invasion independent of
CC ruffling (PubMed:19732055). Involved in the exocytosis of MMP14 leading
CC to matrix remodeling during invasive migration and implicating late
CC endosome-to-plasma membrane tubular connections and cooperation with
CC the exocyst complex (By similarity). Involved in negative regulation of
CC autophagy independently from its role in endosomal sorting by
CC inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity
CC (PubMed:23974797). {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:19732055,
CC ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20308062,
CC ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23275443,
CC ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:24886983,
CC ECO:0000269|PubMed:24998208, ECO:0000305|PubMed:20308062}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4 and
CC WASHC5. The WASH core complex associates with the F-actin-capping
CC protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
CC transient or substoichiometric manner which was initially described as
CC WASH complex. Interacts (via WHD1 region) with WASHC2; the interaction
CC is direct (By similarity). Interacts with BECN1; WASHC1 and AMBRA1 can
CC competitively interact with BECN1 (PubMed:23974797). Interacts with
CC BLOC1S2; may associate with the BLOC-1 complex. Interacts with tubulin
CC gamma chain (TUBG1 or TUBG2) (PubMed:20308062). Interacts with TBC1D23
CC (PubMed:29084197). {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:20308062,
CC ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:29084197}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:19922875}. Recycling endosome membrane
CC {ECO:0000269|PubMed:19922875}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:23974797}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:20308062}.
CC Note=Localization to the endosome membrane is mediated via its
CC interaction with WASHC2 (By similarity). Localized to Salmonella
CC typhimurium entry sites (PubMed:19732055).
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000269|PubMed:19732055}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:19922875}.
CC -!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
CC polymerization by the Arp2/3 complex in vitro.
CC {ECO:0000250|UniProtKB:C4AMC7}.
CC -!- PTM: Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains by
CC the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote
CC endosomal F-actin assembly. {ECO:0000250|UniProtKB:A8K0Z3}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32561.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ304796; CAC83096.1; -; mRNA.
DR EMBL; AK033616; BAC28393.1; -; mRNA.
DR EMBL; AK149967; BAE29201.1; -; mRNA.
DR EMBL; AK154400; BAE32561.1; ALT_INIT; mRNA.
DR EMBL; AK159820; BAE35400.1; -; mRNA.
DR EMBL; AK171737; BAE42641.1; -; mRNA.
DR EMBL; AK172673; BAE43124.1; -; mRNA.
DR EMBL; BC025839; AAH25839.1; -; mRNA.
DR CCDS; CCDS28944.1; -.
DR RefSeq; NP_001032846.1; NM_001037757.1.
DR RefSeq; NP_081109.1; NM_026833.1.
DR RefSeq; XP_006524922.1; XM_006524859.1.
DR RefSeq; XP_006524923.1; XM_006524860.3.
DR AlphaFoldDB; Q8VDD8; -.
DR SMR; Q8VDD8; -.
DR BioGRID; 213039; 31.
DR ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
DR IntAct; Q8VDD8; 29.
DR MINT; Q8VDD8; -.
DR STRING; 10090.ENSMUSP00000072220; -.
DR iPTMnet; Q8VDD8; -.
DR PhosphoSitePlus; Q8VDD8; -.
DR EPD; Q8VDD8; -.
DR MaxQB; Q8VDD8; -.
DR PaxDb; Q8VDD8; -.
DR PeptideAtlas; Q8VDD8; -.
DR PRIDE; Q8VDD8; -.
DR ProteomicsDB; 297623; -.
DR Ensembl; ENSMUST00000072383; ENSMUSP00000072220; ENSMUSG00000024101.
DR Ensembl; ENSMUST00000116556; ENSMUSP00000112255; ENSMUSG00000024101.
DR GeneID; 68767; -.
DR KEGG; mmu:68767; -.
DR UCSC; uc008dgy.1; mouse.
DR CTD; 100287171; -.
DR MGI; MGI:1916017; Washc1.
DR VEuPathDB; HostDB:ENSMUSG00000024101; -.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR GeneTree; ENSGT00390000016717; -.
DR HOGENOM; CLU_029156_1_0_1; -.
DR InParanoid; Q8VDD8; -.
DR OMA; MYSAAKY; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; Q8VDD8; -.
DR TreeFam; TF318222; -.
DR BioGRID-ORCS; 68767; 10 hits in 71 CRISPR screens.
DR PRO; PR:Q8VDD8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VDD8; protein.
DR Bgee; ENSMUSG00000024101; Expressed in embryonic brain and 243 other tissues.
DR ExpressionAtlas; Q8VDD8; baseline and differential.
DR Genevisible; Q8VDD8; MM.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0000145; C:exocyst; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
DR GO; GO:0002468; P:dendritic cell antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:MGI.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:MGI.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:1904109; P:positive regulation of cholesterol import; IMP:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IMP:UniProtKB.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome;
KW Isopeptide bond; Membrane; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..475
FT /note="WASH complex subunit 1"
FT /id="PRO_0000390963"
FT DOMAIN 369..391
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..167
FT /note="WHD1"
FT REGION 1..54
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 300..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..475
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT COMPBIAS 300..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:A8K0Z3"
FT CONFLICT 15
FT /note="Y -> C (in Ref. 2; BAE32561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 51659 MW; 4198C8AEE499D3C3 CRC64;
MTPVKTQCSL AGQLYAVPLI QPDLRREEAI QQVADALQYL QNISGDIFSR ISRRVELSRR
QLQAISERVS LAQAKIEKIK GSKKAIKVFS SAKYPAPEHL QEYGSIFTGA LDPGLQRRPR
YRIQSKHRPL DERALQEKLK YFPVCVNTKS EPEDEAEEGL GGLPSNISSI SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH TMLGTEEEKL FDAPLSISKR EQLERQAPEN YFYVPDLGQV
PEIDVPSYLP DLPGVADDLM YSADLGPGIA PSAPGAIPEL PAFHTEVAEP LQPELENEVL
LAAPPPPPPP PPPPPPAPTA LVSTPQPPMF PDMATAAGQV AREEDSSSSM AHTASVQGAP
KEVVDPSSGR ATLLESIRQA GGIGKAKLRS VKERKLEKKK QKEQEQVRAT SQGGDLMSDL
FNKLVMRRKG ISGKGPSTGT SEGPGGAFSR MSDSIPPLPP PQQPAGDEDE EDWES
