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WASH complex subunit 1 (CXYorf1-like protein on chromosome 9) (Protein FAM39E) (WAS protein family homolog 1)

 WASH1_HUMAN             Reviewed;         465 AA.
A8K0Z3;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 2.
25-OCT-2017, entry version 89.
RecName: Full=WASH complex subunit 1 {ECO:0000312|HGNC:HGNC:24361};
AltName: Full=CXYorf1-like protein on chromosome 9;
AltName: Full=Protein FAM39E;
AltName: Full=WAS protein family homolog 1;
Name=WASHC1 {ECO:0000312|HGNC:HGNC:24361}; Synonyms=FAM39E, WASH1;
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=Brain;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
GENE DUPLICATION.
PubMed=10655549; DOI=10.1093/hmg/9.3.395;
Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A.,
Cocchia S., Mercadante G., Pannone E., Archidiacono N., Rocchi M.,
Schlessinger D., D'Urso M.;
"Differentially regulated and evolved genes in the fully sequenced
Xq/Yq pseudoautosomal region.";
Hum. Mol. Genet. 9:395-401(2000).
[4]
GENE DUPLICATION.
PubMed=18159949; DOI=10.1371/journal.pgen.0030237;
Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E.,
Parkhurst S.M., Trask B.J.;
"Human subtelomeric WASH genes encode a new subclass of the WASP
family.";
PLoS Genet. 3:E237-E237(2007).
[5]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASHC2C,
TUBULIN-BINDING, AND MUTAGENESIS OF TRP-463.
PubMed=19922874; DOI=10.1016/j.devcel.2009.09.009;
Gomez T.S., Billadeau D.D.;
"A FAM21-containing WASH complex regulates retromer-dependent
sorting.";
Dev. Cell 17:699-711(2009).
[6]
FUNCTION, 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]
FUNCTION, 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).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22114305; DOI=10.1242/jcs.080986;
Zech T., Calaminus S.D., Caswell P., Spence H.J., Carnell M.,
Insall R.H., Norman J., Machesky L.M.;
"The Arp2/3 activator WASH regulates alpha5beta1-integrin-mediated
invasive migration.";
J. Cell Sci. 124:3753-3759(2011).
[9]
FUNCTION, UBIQUITINATION AT LYS-220, AND MUTAGENESIS OF LYS-220.
PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M.,
Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.;
"Regulation of WASH-dependent actin polymerization and protein
trafficking by ubiquitination.";
Cell 152:1051-1064(2013).
[10]
FUNCTION, INTERACTION WITH EXOC1; EXOC4 AND EXOC8, AND SUBCELLULAR
LOCATION.
PubMed=24344185; DOI=10.1083/jcb.201306162;
Monteiro P., Rosse C., Castro-Castro A., Irondelle M., Lagoutte E.,
Paul-Gilloteaux P., Desnos C., Formstecher E., Darchen F., Perrais D.,
Gautreau A., Hertzog M., Chavrier P.;
"Endosomal WASH and exocyst complexes control exocytosis of MT1-MMP at
invadopodia.";
J. Cell Biol. 203:1063-1079(2013).
-!- FUNCTION: Acts as a nucleation-promoting factor (NPF) at the
surface of endosomes, where it recruits and activates the Arp2/3
complex to induce actin polymerization, playing a key role in the
fission of tubules that serve as transport intermediates during
endosome sorting (PubMed:19922874, PubMed:19922875,
PubMed:20498093, PubMed:23452853). Its assembly in the WASH core
complex seems to inhibit its NPF activity and via WASHC2 is
required for its membrane targeting (PubMed:20498093). Involved in
endocytic trafficking of EGF (By similarity). Involved in
transferrin receptor recycling. Regulates the trafficking of
endosomal alpha5beta1 integrin to the plasma membrane and involved
in invasive cell migration (PubMed:22114305). In T-cells involved
in endosome-to-membrane recycling of receptors including T-cell
receptor (TCR), CD28 and ITGAL; proposed to be implicated in T
cell proliferation and effector function. In dendritic cells
involved in endosome-to-membrane recycling of major
histocompatibility complex (MHC) class II probably involving
retromer and subsequently allowing antigen sampling, loading and
presentation during T-cell activation (By similarity). Involved in
Arp2/3 complex-dependent actin assembly driving Salmonella
typhimurium invasion independent of ruffling. Involved in the
exocytosis of MMP14 leading to matrix remodeling during invasive
migration and implicating late endosome-to-plasma membrane tubular
connections and cooperation with the exocyst complex
(PubMed:24344185). Involved in negative regulation of autophagy
independently from its role in endosomal sorting by inhibiting
BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By
similarity). {ECO:0000250|UniProtKB:C4AMC7,
ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874,
ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23452853,
ECO:0000305|PubMed:20498093}.
-!- 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 (PubMed:19922875,
PubMed:20498093). Interacts (via WHD1 region) with WASHC2C; the
interaction is direct (PubMed:19922874). Interacts with VPS35;
mediates the association with the retromer CSC complex. Interacts
with FKBP15. Interacts with alpha-tubulin. Interacts with BECN1;
WASHC1 and AMBRA1 can competetively interact with BECN1. Interacts
with BLOC1S2; may associate with the BLOC-1 complex. Interacts
with tubulin gamma chain (TUBG1 or TUBG2) (By similarity).
Interacts with EXOC1, EXOC4, EXOC8; in MMP14-positive endosomes in
breast tumor cells; indicative for an association with the exocyst
complex (PubMed:24344185). {ECO:0000250|UniProtKB:Q8VDD8,
ECO:0000250|UniProtKB:Q9Y4E1, ECO:0000269|PubMed:19922874,
ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
ECO:0000269|PubMed:24344185}.
-!- INTERACTION:
Q14457:BECN1; NbExp=3; IntAct=EBI-6160405, EBI-949378;
Q9NV70:EXOC1; NbExp=2; IntAct=EBI-6160405, EBI-1045313;
Q8IYI6:EXOC8; NbExp=3; IntAct=EBI-6160405, EBI-742102;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:19922874}. Recycling endosome membrane
{ECO:0000250|UniProtKB:Q8VDD8}. Late endosome
{ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:24344185}.
Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}.
Note=Localization to the endosome membrane is mediated via its
interaction with WASHC2 (PubMed:19922874). Localizes to MMP14-
positive late endosomes and transiently to invadipodia
(PubMed:24344185). Localized to Salmonella typhimurium entry sites
(By similarity). {ECO:0000250|UniProtKB:Q8VDD8,
ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:24344185}.
-!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
polymerization by the Arp2/3 complex in vitro.
{ECO:0000250|UniProtKB:C4AMC7}.
-!- PTM: Ubiquitinated at Lys-220 via 'Lys-63'-linked ubiquitin chains
by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to
promote endosomal F-actin assembly. {ECO:0000269|PubMed:23452853}.
-!- MISCELLANEOUS: WASH genes duplicated to multiple chromosomal ends
during primate evolution, with highest copy number reached in
humans, whose WASH repertoires probably vary extensively among
individuals (PubMed:18159949). It is therefore difficult to
determine which gene is functional or not. The telomeric region of
chromosome 9p is paralogous to the pericentromeric regions of
chromosome 9 as well as to 2q. Paralogous regions contain 7
transcriptional units. Duplicated WASH genes are also present in
the Xq/Yq pseudoautosomal region, as well as on chromosome 1 and
15. The chromosome 16 copy seems to be a pseudogene.
{ECO:0000305|PubMed:18159949}.
-!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
-!- CAUTION: To demonstrate the interaction with WASHC2, a WASHC2C
construct with WASHC2A-specific sequence insertions has been used.
In human, WASHC2 has undergone evolutionary duplication giving
rise to highly homologous family members (PubMed:19922874).
{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}.
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EMBL; AK289708; BAF82397.1; -; mRNA.
EMBL; AL928970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS78375.1; -.
RefSeq; NP_878908.4; NM_182905.4.
UniGene; Hs.446466; -.
UniGene; Hs.459573; -.
UniGene; Hs.461200; -.
UniGene; Hs.521961; -.
UniGene; Hs.585931; -.
UniGene; Hs.709408; -.
ProteinModelPortal; A8K0Z3; -.
BioGrid; 938833; 25.
CORUM; A8K0Z3; -.
IntAct; A8K0Z3; 14.
iPTMnet; A8K0Z3; -.
PhosphoSitePlus; A8K0Z3; -.
BioMuta; WASH1; -.
EPD; A8K0Z3; -.
MaxQB; A8K0Z3; -.
PaxDb; A8K0Z3; -.
PRIDE; A8K0Z3; -.
DNASU; 100287171; -.
Ensembl; ENST00000442898; ENSP00000485627; ENSG00000181404.
GeneID; 100287171; -.
KEGG; hsa:100287171; -.
UCSC; uc010mgm.2; human.
CTD; 100287171; -.
DisGeNET; 100287171; -.
EuPathDB; HostDB:ENSG00000181404.15; -.
GeneCards; WASHC1; -.
H-InvDB; HIX0034804; -.
HGNC; HGNC:24361; WASHC1.
HPA; HPA002689; -.
MIM; 613632; gene.
neXtProt; NX_A8K0Z3; -.
OpenTargets; ENSG00000181404; -.
PharmGKB; PA162409121; -.
eggNOG; ENOG410IFZ4; Eukaryota.
eggNOG; ENOG410YN2V; LUCA.
GeneTree; ENSGT00390000016717; -.
HOVERGEN; HBG066686; -.
InParanoid; A8K0Z3; -.
KO; K18461; -.
OMA; PNLKGHA; -.
OrthoDB; EOG091G0GKX; -.
PhylomeDB; A8K0Z3; -.
SIGNOR; A8K0Z3; -.
ChiTaRS; WASH1; human.
GenomeRNAi; 100287171; -.
PRO; PR:A8K0Z3; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000181404; -.
CleanEx; HS_WASH1; -.
Genevisible; A8K0Z3; HS.
GO; GO:0005776; C:autophagosome; ISS:ParkinsonsUK-UCL.
GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0071437; C:invadopodium; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
GO; GO:0002468; P:dendritic cell antigen processing and presentation; IEA:Ensembl.
GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
GO; GO:0007032; P:endosome organization; IEA:Ensembl.
GO; GO:0099638; P:endosome to plasma membrane protein transport; IEA:Ensembl.
GO; GO:0006887; P:exocytosis; IMP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0010507; P:negative regulation of autophagy; ISS:ParkinsonsUK-UCL.
GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:1904109; P:positive regulation of cholesterol import; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
GO; GO:0031396; P:regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IMP:UniProtKB.
GO; GO:0090306; P:spindle assembly involved in meiosis; IEA:Ensembl.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
InterPro; IPR028290; WASH1.
InterPro; IPR021854; WASH1_WAHD.
PANTHER; PTHR23331; PTHR23331; 1.
Pfam; PF11945; WASH_WAHD; 1.
1: Evidence at protein level;
Actin-binding; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endosome; Isopeptide bond; Membrane; Protein transport;
Reference proteome; Transport; Ubl conjugation.
CHAIN 1 465 WASH complex subunit 1.
/FTId=PRO_0000329013.
DOMAIN 361 383 WH2.
REGION 1 167 WHD1.
REGION 1 54 Required for WASH complex assembly.
{ECO:0000250|UniProtKB:C4AMC7}.
REGION 349 465 VCA. {ECO:0000250|UniProtKB:C4AMC7}.
COMPBIAS 303 330 Pro-rich.
CROSSLNK 220 220 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23452853}.
MUTAGEN 220 220 K->R: Abolishes ubiquitination by the
TRIM27:MAGEL2 E3 ubiquitin ligase complex
and impairs retrograde transport.
{ECO:0000269|PubMed:23452853}.
MUTAGEN 463 463 W->A: Impairs retrograde transport from
endosome to Golgi apparatus.
{ECO:0000269|PubMed:19922874}.
CONFLICT 19 19 F -> L (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 54 54 Q -> R (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 98 98 G -> E (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 119 119 P -> S (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 141 141 D -> Y (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 245 245 H -> D (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 294 294 V -> A (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 302 302 T -> TAPP (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 321 321 P -> S (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 340 342 SSS -> GSN (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 362 362 W -> R (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 383 383 M -> V (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 391 392 QQ -> KK (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 407 407 H -> D (in Ref. 1; BAF82397).
{ECO:0000305}.
CONFLICT 439 439 V -> A (in Ref. 1; BAF82397).
{ECO:0000305}.
SEQUENCE 465 AA; 50328 MW; DBD5DEAFB7019B3E CRC64;
MTPVRMQHSL AGQTYAVPFI QPDLRREEAV QQMADALQYL QKVSGDIFSR ISQQVEQSRS
QVQAIGEKVS LAQAKIEKIK GSKKAIKVFS SAKYPAPGRL QEYGSIFTGA QDPGLQRRPR
HRIQSKHRPL DERALQEKLK DFPVCVSTKP EPEDDAEEGL GGLPSNISSV SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH VMLGAETEEK LFDAPLSISK REQLEQQVPE NYFYVPDLGQ
VPEIHVPSYL PDLPGIANDL MYSADLGPGI APSAPGTIPE LPTFHTEVAE PLKVDLQDGV
LTPPPPPPPP PPAPEVLASA PPLPPSTAAP VGQGARQDDS SSSASPSVQG APREVVDPSG
GWATLLESIR QAGGIGKAKL RSMKERKLEK QQQKEQEQVR ATSQGGHLMS DLFNKLVMRR
KGISGKGPGA GEGPGGAFVR VSDSIPPLPP PQQPQAEEDE DDWES


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