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WASH complex subunit 5 (Strumpellin) (WASH complex subunit strumpellin)

 WASC5_HUMAN             Reviewed;        1159 AA.
Q12768; A8K4R7; Q3KQX5; Q8TBQ2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
12-SEP-2018, entry version 136.
RecName: Full=WASH complex subunit 5 {ECO:0000312|HGNC:HGNC:28984};
AltName: Full=Strumpellin;
AltName: Full=WASH complex subunit strumpellin {ECO:0000305};
Name=WASHC5 {ECO:0000312|HGNC:HGNC:28984}; Synonyms=KIAA0196;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
FUNCTION OF THE WASH COMPLEX, AND IDENTIFICATION IN THE WASH COMPLEX.
PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
"The Arp2/3 activator WASH controls the fission of endosomes through a
large multiprotein complex.";
Dev. Cell 17:712-723(2009).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VCP,
FUNCTION, AND CHARACTERIZATION OF VARIANT SPG8 ASP-471.
PubMed=20833645; DOI=10.1093/brain/awq222;
Clemen C.S., Tangavelou K., Strucksberg K.H., Just S., Gaertner L.,
Regus-Leidig H., Stumpf M., Reimann J., Coras R., Morgan R.O.,
Fernandez M.P., Hofmann A., Muller S., Schoser B., Hanisch F.G.,
Rottbauer W., Blumcke I., von Horsten S., Eichinger L., Schroder R.;
"Strumpellin is a novel valosin-containing protein binding partner
linking hereditary spastic paraplegia to protein aggregation
diseases.";
Brain 133:2920-2941(2010).
[8]
IDENTIFICATION IN THE WASH CORE COMPLEX, AND FUNCTION OF THE WASH CORE
COMPLEX.
PubMed=20498093; DOI=10.1073/pnas.0913293107;
Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z.,
Rosen M.K., Billadeau D.D.;
"WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome
protein (WASP) family are controlled by analogous structurally related
complexes.";
Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS SPG8
ASP-471; PHE-619 AND PHE-626.
PubMed=23085491; DOI=10.1016/j.bbadis.2012.10.011;
Freeman C., Seaman M.N., Reid E.;
"The hereditary spastic paraplegia protein strumpellin:
characterisation in neurons and of the effect of disease mutations on
WASH complex assembly and function.";
Biochim. Biophys. Acta 1832:160-173(2013).
[11]
INVOLVEMENT IN RTSC1.
PubMed=24065355; DOI=10.1136/jmedgenet-2013-101715;
Elliott A.M., Simard L.R., Coghlan G., Chudley A.E., Chodirker B.N.,
Greenberg C.R., Burch T., Ly V., Hatch G.M., Zelinski T.;
"A novel mutation in KIAA0196: identification of a gene involved in
Ritscher-Schinzel/3C syndrome in a First Nations cohort.";
J. Med. Genet. 50:819-822(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PI4K2A.
PubMed=23676666; DOI=10.1091/mbc.E13-02-0088;
Ryder P.V., Vistein R., Gokhale A., Seaman M.N., Puthenveedu M.A.,
Faundez V.;
"The WASH complex, an endosomal Arp2/3 activator, interacts with the
Hermansky-Pudlak syndrome complex BLOC-1 and its cargo
phosphatidylinositol-4-kinase type IIalpha.";
Mol. Biol. Cell 24:2269-2284(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
VARIANTS SPG8 ASP-471; PHE-619 AND PHE-626, AND CHARACTERIZATION OF
VARIANTS SPG8 PHE-619 AND PHE-626.
PubMed=17160902; DOI=10.1086/510782;
Valdmanis P.N., Meijer I.A., Reynolds A., Lei A., MacLeod P.,
Schlesinger D., Zatz M., Reid E., Dion P.A., Drapeau P., Rouleau G.A.;
"Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary
spastic paraplegia.";
Am. J. Hum. Genet. 80:152-161(2007).
[16]
VARIANT SPG8 THR-226.
PubMed=23881105; DOI=10.1007/s00415-013-7044-6;
Bettencourt C., Morris H.R., Singleton A.B., Hardy J., Houlden H.;
"Exome sequencing expands the mutational spectrum of SPG8 in a family
with spasticity responsive to L-DOPA treatment.";
J. Neurol. 260:2414-2416(2013).
[17]
VARIANT SPG8 ALA-696.
PubMed=23455931; DOI=10.1007/s00415-013-6870-x;
de Bot S.T., Vermeer S., Buijsman W., Heister A., Voorendt M.,
Verrips A., Scheffer H., Kremer H.P., van de Warrenburg B.P.,
Kamsteeg E.J.;
"Pure adult-onset Spastic Paraplegia caused by a novel mutation in the
KIAA0196 (SPG8) gene.";
J. Neurol. 260:1765-1769(2013).
[18]
VARIANT SPG8 ALA-620.
PubMed=25454649; DOI=10.1016/j.jns.2014.10.018;
Jahic A., Kreuz F., Zacher P., Fiedler J., Bier A., Reif S.,
Rieger M., Krueger S., Beetz C., Plaschke J.;
"A novel strumpellin mutation and potential pitfalls in the molecular
diagnosis of hereditary spastic paraplegia type SPG8.";
J. Neurol. Sci. 347:372-374(2014).
-!- FUNCTION: Acts at least in part as component of the WASH core
complex whose assembly at the surface of endosomes seems to
inhibit WASH nucleation-promoting factor (NPF) activity in
recruiting and activating the Arp2/3 complex to induce actin
polymerization, and which is involved in regulation of the fission
of tubules that serve as transport intermediates during endosome
sorting (PubMed:19922875, PubMed:20498093). May be involved in
axonal outgrowth. Involved in cellular localization of ADRB2
(PubMed:23085491). Involved in cellular trafficking of BLOC-1
complex cargos such as ATP7A and VAMP7 (PubMed:23676666).
{ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20833645,
ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}.
-!- SUBUNIT: Component of the WASH core complex also described as WASH
regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or
WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5.
The WASH core complex associates via WASHC2 with the F-actin-
capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and
CAPZB) in a transient or substoichiometric manner which was
initially described as WASH complex. Interacts with VCP, PI4K2A.
{ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:23676666}.
-!- INTERACTION:
Q13596:SNX1; NbExp=2; IntAct=EBI-2563794, EBI-2822329;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20833645}. Endoplasmic reticulum
{ECO:0000269|PubMed:20833645}. Early endosome
{ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}.
Note=Colocalizes with SYP/synaptophysin in the external molecular
layer of the dentate gyrus and in motoneurons of the ventral horn
of spinal cord. {ECO:0000269|PubMed:20833645}.
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:20833645}.
-!- DISEASE: Spastic paraplegia 8, autosomal dominant (SPG8)
[MIM:603563]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:17160902,
ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:23085491,
ECO:0000269|PubMed:23455931, ECO:0000269|PubMed:23881105,
ECO:0000269|PubMed:25454649}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ritscher-Schinzel syndrome 1 (RTSC1) [MIM:220210]: A
developmental malformation syndrome characterized by craniofacial
abnormalities, congenital heart defects, and cerebellar brain
malformations. Facial features include prominent occiput,
prominent forehead, low-set ears, downslanting palpebral fissures,
depressed nasal bridge, and micrognathia. Cardiac defects can
include septal defects and aortic stenosis, among others, and
brain imaging shows Dandy-Walker malformation, cerebellar vermis
hypoplasia, posterior fossa cysts, and ventricular dilatation.
Affected individuals have severe developmental delay.
{ECO:0000269|PubMed:24065355}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the strumpellin family. {ECO:0000305}.
-!- CAUTION: The function of the WASH complex is debated. One study
using partially purified samples reported a nucleation-promoting
factor (NPF) activity (PubMed:19922875). In another study, the
reconstituted and highly purified recombinant WASH core complex
did not show activity toward Arp2/3 complex suggesting a rather
inhibitory role towards WASH NPF activity (PubMed:20498093).
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA12109.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D83780; BAA12109.2; ALT_INIT; mRNA.
EMBL; AK291032; BAF83721.1; -; mRNA.
EMBL; CH471060; EAW92081.1; -; Genomic_DNA.
EMBL; BC026951; AAH26951.1; -; mRNA.
EMBL; BC106015; AAI06016.1; -; mRNA.
CCDS; CCDS6355.1; -.
RefSeq; NP_055661.3; NM_014846.3.
RefSeq; XP_016869602.1; XM_017014113.1.
UniGene; Hs.270043; -.
ProteinModelPortal; Q12768; -.
BioGrid; 115226; 31.
ComplexPortal; CPX-1163; WASH complex, variant WASHC1/WASHC2C.
ComplexPortal; CPX-1168; WASH complex, variant WASH2P/WASHC2C.
ComplexPortal; CPX-1169; WASH complex, variant WASH3P/WASHC2C.
ComplexPortal; CPX-1170; WASH complex, variant WASH4P/WASHC2C.
ComplexPortal; CPX-1171; WASH complex, variant WASH6P/WASHC2C.
ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
ComplexPortal; CPX-1173; WASH complex, variant WASH2P/WASHC2A.
ComplexPortal; CPX-1174; WASH complex, variant WASH3P/WASHC2A.
ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
ComplexPortal; CPX-1176; WASH complex, variant WASH6P/WASHC2A.
CORUM; Q12768; -.
IntAct; Q12768; 17.
STRING; 9606.ENSP00000318016; -.
iPTMnet; Q12768; -.
PhosphoSitePlus; Q12768; -.
BioMuta; KIAA0196; -.
DMDM; 2495719; -.
EPD; Q12768; -.
MaxQB; Q12768; -.
PaxDb; Q12768; -.
PeptideAtlas; Q12768; -.
PRIDE; Q12768; -.
ProteomicsDB; 58911; -.
Ensembl; ENST00000318410; ENSP00000318016; ENSG00000164961.
GeneID; 9897; -.
KEGG; hsa:9897; -.
UCSC; uc003yrt.4; human.
CTD; 9897; -.
DisGeNET; 9897; -.
EuPathDB; HostDB:ENSG00000164961.15; -.
GeneCards; WASHC5; -.
GeneReviews; KIAA0196; -.
HGNC; HGNC:28984; WASHC5.
HPA; CAB034216; -.
HPA; CAB034219; -.
HPA; HPA064649; -.
HPA; HPA070916; -.
MalaCards; WASHC5; -.
MIM; 220210; phenotype.
MIM; 603563; phenotype.
MIM; 610657; gene.
neXtProt; NX_Q12768; -.
OpenTargets; ENSG00000164961; -.
Orphanet; 7; 3C syndrome.
Orphanet; 100989; Autosomal dominant spastic paraplegia type 8.
PharmGKB; PA142671624; -.
eggNOG; KOG3666; Eukaryota.
eggNOG; ENOG410XNSS; LUCA.
GeneTree; ENSGT00390000011137; -.
HOGENOM; HOG000258245; -.
HOVERGEN; HBG102793; -.
InParanoid; Q12768; -.
KO; K18464; -.
OMA; CRKPADP; -.
OrthoDB; EOG091G02GF; -.
PhylomeDB; Q12768; -.
TreeFam; TF314480; -.
GeneWiki; KIAA0196; -.
GenomeRNAi; 9897; -.
PRO; PR:Q12768; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164961; Expressed in 220 organ(s), highest expression level in corpus callosum.
CleanEx; HS_KIAA0196; -.
ExpressionAtlas; Q12768; baseline and differential.
Genevisible; Q12768; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
GO; GO:0016197; P:endosomal transport; IEA:Ensembl.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0090306; P:spindle assembly involved in meiosis; IEA:Ensembl.
InterPro; IPR019393; WASH_strumpellin.
PANTHER; PTHR15691; PTHR15691; 1.
Pfam; PF10266; Strumpellin; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Disease mutation; Endoplasmic reticulum;
Endosome; Hereditary spastic paraplegia; Mental retardation;
Neurodegeneration; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 1159 WASH complex subunit 5.
/FTId=PRO_0000050733.
MOD_RES 917 917 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
VARIANT 226 226 I -> T (in SPG8; dopamine responsive
spasticity; dbSNP:rs755285830).
{ECO:0000269|PubMed:23881105}.
/FTId=VAR_069984.
VARIANT 471 471 N -> D (in SPG8; does not alter
subcellular distribution; no effect on
its binding to VCP; no effect on assembly
in the WASH complex; dbSNP:rs80338865).
{ECO:0000269|PubMed:17160902,
ECO:0000269|PubMed:23085491}.
/FTId=VAR_031955.
VARIANT 619 619 L -> F (in SPG8; fails to rescue the
curly phenotype in a zebrafish model; no
effect on assembly in the WASH complex;
dbSNP:rs80338866).
{ECO:0000269|PubMed:17160902,
ECO:0000269|PubMed:23085491}.
/FTId=VAR_031956.
VARIANT 620 620 V -> A (in SPG8).
{ECO:0000269|PubMed:25454649}.
/FTId=VAR_072417.
VARIANT 626 626 V -> F (in SPG8; fails to rescue the
curly phenotype in a zebrafish model; no
effect on assembly in the WASH complex;
dbSNP:rs80338867).
{ECO:0000269|PubMed:17160902,
ECO:0000269|PubMed:23085491}.
/FTId=VAR_031957.
VARIANT 696 696 G -> A (in SPG8; dbSNP:rs397515564).
{ECO:0000269|PubMed:23455931}.
/FTId=VAR_069985.
CONFLICT 229 229 L -> R (in Ref. 4; AAH26951).
{ECO:0000305}.
SEQUENCE 1159 AA; 134286 MW; D6156D359981FC5F CRC64;
MLDFLAENNL CGQAILRIVS CGNAIIAELL RLSEFIPAVF RLKDRADQQK YGDIIFDFSY
FKGPELWESK LDAKPELQDL DEEFRENNIE IVTRFYLAFQ SVHKYIVDLN RYLDDLNEGV
YIQQTLETVL LNEDGKQLLC EALYLYGVML LVIDQKIEGE VRERMLVSYY RYSAARSSAD
SNMDDICKLL RSTGYSSQPG AKRPSNYPES YFQRVPINES FISMVIGRLR SDDIYNQVSA
YPLPEHRSTA LANQAAMLYV ILYFEPSILH THQAKMREIV DKYFPDNWVI SIYMGITVNL
VDAWEPYKAA KTALNNTLDL SNVREQASRY ATVSERVHAQ VQQFLKEGYL REEMVLDNIP
KLLNCLRDCN VAIRWLMLHT ADSACDPNNK RLRQIKDQIL TDSRYNPRIL FQLLLDTAQF
EFILKEMFKQ MLSEKQTKWE HYKKEGSERM TELADVFSGV KPLTRVEKNE NLQAWFREIS
KQILSLNYDD STAAGRKTVQ LIQALEEVQE FHQLESNLQV CQFLADTRKF LHQMIRTINI
KEEVLITMQI VGDLSFAWQL IDSFTSIMQE SIRVNPSMVT KLRATFLKLA SALDLPLLRI
NQANSPDLLS VSQYYSGELV SYVRKVLQII PESMFTSLLK IIKLQTHDII EVPTRLDKDK
LRDYAQLGPR YEVAKLTHAI SIFTEGILMM KTTLVGIIKV DPKQLLEDGI RKELVKRVAF
ALHRGLIFNP RAKPSELMPK LKELGATMDG FHRSFEYIQD YVNIYGLKIW QEEVSRIINY
NVEQECNNFL RTKIQDWQSM YQSTHIPIPK FTPVDESVTF IGRLCREILR ITDPKMTCHI
DQLNTWYDMK THQEVTSSRL FSEIQTTLGT FGLNGLDRLL CFMIVKELQN FLSMFQKIIL
RDRTVQDTLK TLMNAVSPLK SIVANSNKIY FSAIAKTQKI WTAYLEAIMK VGQMQILRQQ
IANELNYSCR FDSKHLAAAL ENLNKALLAD IEAHYQDPSL PYPKEDNTLL YEITAYLEAA
GIHNPLNKIY ITTKRLPYFP IVNFLFLIAQ LPKLQYNKNL GMVCRKPTDP VDWPPLVLGL
LTLLKQFHSR YTEQFLALIG QFICSTVEQC TSQKIPEIPA DVVGALLFLE DYVRYTKLPR
RVAEAHVPNF IFDEFRTVL


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