PHLP1_MOUSE
ID PHLP1_MOUSE Reviewed; 1687 AA.
AC Q8CHE4; Q6PCN0; Q8QZU8; Q8R5E5; Q99KL6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=PH domain leucine-rich repeat-containing protein phosphatase 1;
DE EC=3.1.3.16;
DE AltName: Full=Pleckstrin homology domain-containing family E member 1;
DE Short=PH domain-containing family E member 1;
DE AltName: Full=Suprachiasmatic nucleus circadian oscillatory protein;
GN Name=Phlpp1; Synonyms=Kiaa0606, Phlpp, Plekhe1, Scop;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1687.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-1687.
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 INDUCTION.
RX PubMed=15542705; DOI=10.1196/annals.1316.012;
RA Yamamoto H., Imai K., Takamatsu Y., Kamegaya E., Hara Y., Shimada K.,
RA Yamamoto T., Shen H.W., Hagino Y., Kobayashi H., Ide S., Sora I., Koga H.,
RA Ikedaa K.;
RT "Changes in expression of the mouse homologues of KIAA genes after
RT subchronic methamphetamine treatment.";
RL Ann. N. Y. Acad. Sci. 1025:92-101(2004).
RN [5]
RP FUNCTION.
RX PubMed=17382888; DOI=10.1016/j.cell.2006.12.047;
RA Shimizu K., Phan T., Mansuy I.M., Storm D.R.;
RT "Proteolytic degradation of SCOP in the hippocampus contributes to
RT activation of MAP kinase and memory.";
RL Cell 128:1219-1229(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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 [7]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
RX PubMed=20089132; DOI=10.1111/j.1471-4159.2010.06609.x;
RA Kanan Y., Matsumoto H., Song H., Sokolov M., Anderson R.E., Rajala R.V.;
RT "Serine/threonine kinase akt activation regulates the activity of retinal
RT serine/threonine phosphatases, PHLPP and PHLPPL.";
RL J. Neurochem. 113:477-488(2010).
RN [8]
RP FUNCTION.
RX PubMed=20080691; DOI=10.1073/pnas.0910292107;
RA Masubuchi S., Gao T., O'Neill A., Eckel-Mahan K., Newton A.C.,
RA Sassone-Corsi P.;
RT "Protein phosphatase PHLPP1 controls the light-induced resetting of the
RT circadian clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1642-1647(2010).
RN [9]
RP FUNCTION.
RX PubMed=21498666; DOI=10.4049/jimmunol.1002126;
RA Patterson S.J., Han J.M., Garcia R., Assi K., Gao T., O'Neill A.,
RA Newton A.C., Levings M.K.;
RT "PHLPP regulates the development, function, and molecular signaling
RT pathways of regulatory T cells.";
RL J. Immunol. 186:5533-5537(2011).
CC -!- FUNCTION: Protein phosphatase involved in regulation of Akt and PKC
CC signaling. Mediates dephosphorylation in the C-terminal domain
CC hydrophobic motif of members of the AGC Ser/Thr protein kinase family;
CC specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and
CC 'Ser-657' of PRKCA (By similarity). Isoform 2 seems to have a major
CC role in regulating Akt signaling in hippocampal neurons (By
CC similarity). Akt regulates the balance between cell survival and
CC apoptosis through a cascade that primarily alters the function of
CC transcription factors that regulate pro- and antiapoptotic genes.
CC Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and
CC suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads
CC to their destabilization and degradation. Dephosphorylates STK4 on
CC 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates
CC RPS6KB1 and is involved in regulation of cap-dependent translation.
CC Inhibits cancer cell proliferation and may act as a tumor suppressor.
CC Dephosphorylates RAF1 inhibiting its kinase activity. May act as a
CC negative regulator of K-Ras signaling in membrane rafts (By
CC similarity). Involved in the hippocampus-dependent long-term memory
CC formation (PubMed:17382888). Involved in circadian control by
CC regulating the consolidation of circadian periodicity after resetting
CC (PubMed:20080691). Involved in development and function of regulatory
CC T-cells (PubMed:21498666). {ECO:0000250|UniProtKB:O60346,
CC ECO:0000250|UniProtKB:Q9WTR8, ECO:0000269|PubMed:17382888,
CC ECO:0000269|PubMed:20080691, ECO:0000269|PubMed:21498666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Insensitive to okadaic acid. Deubiquitination by
CC WDR48-USP12 complex positively regulates PHLPP1 stability.
CC {ECO:0000250|UniProtKB:O60346}.
CC -!- SUBUNIT: Interacts with the nucleotide free form of K-Ras (KRAS) via
CC its LRR repeats (By similarity). Interacts with AKT2, AKT3 and PRKCB.
CC Interacts with WDR48 and USP12 (By similarity).
CC {ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q9WTR8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=beta;
CC IsoId=Q8CHE4-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha;
CC IsoId=Q8CHE4-2; Sequence=VSP_057810;
CC -!- TISSUE SPECIFICITY: Isoforms 1 and 2 are expressed in the retina
CC (PubMed:20089132). {ECO:0000269|PubMed:20089132}.
CC -!- INDUCTION: Up-regulated in the hippocampus upon chronic methamphetamine
CC treatment. {ECO:0000269|PubMed:15542705}.
CC -!- DOMAIN: The PH domain is required for interaction with PRKCB and its
CC dephosphorylation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59254.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC101663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB093251; BAC41435.1; -; mRNA.
DR EMBL; BC004581; AAH04581.1; -; mRNA.
DR EMBL; BC022703; AAH22703.1; -; mRNA.
DR EMBL; BC024670; AAH24670.1; -; mRNA.
DR EMBL; BC059254; AAH59254.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48337.1; -. [Q8CHE4-1]
DR RefSeq; NP_598582.3; NM_133821.3. [Q8CHE4-1]
DR AlphaFoldDB; Q8CHE4; -.
DR SMR; Q8CHE4; -.
DR BioGRID; 221058; 35.
DR IntAct; Q8CHE4; 1.
DR STRING; 10090.ENSMUSP00000056530; -.
DR iPTMnet; Q8CHE4; -.
DR PhosphoSitePlus; Q8CHE4; -.
DR EPD; Q8CHE4; -.
DR MaxQB; Q8CHE4; -.
DR PaxDb; Q8CHE4; -.
DR PeptideAtlas; Q8CHE4; -.
DR PRIDE; Q8CHE4; -.
DR ProteomicsDB; 288142; -. [Q8CHE4-1]
DR ProteomicsDB; 288143; -. [Q8CHE4-2]
DR Antibodypedia; 23071; 180 antibodies from 34 providers.
DR DNASU; 98432; -.
DR Ensembl; ENSMUST00000061047; ENSMUSP00000056530; ENSMUSG00000044340. [Q8CHE4-1]
DR GeneID; 98432; -.
DR KEGG; mmu:98432; -.
DR UCSC; uc007cgv.2; mouse. [Q8CHE4-1]
DR CTD; 23239; -.
DR MGI; MGI:2138327; Phlpp1.
DR VEuPathDB; HostDB:ENSMUSG00000044340; -.
DR eggNOG; KOG0618; Eukaryota.
DR GeneTree; ENSGT00940000158137; -.
DR HOGENOM; CLU_003020_0_0_1; -.
DR InParanoid; Q8CHE4; -.
DR OMA; LDICGYF; -.
DR OrthoDB; 172467at2759; -.
DR PhylomeDB; Q8CHE4; -.
DR TreeFam; TF315993; -.
DR Reactome; R-MMU-199418; Negative regulation of the PI3K/AKT network.
DR BioGRID-ORCS; 98432; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Phlpp1; mouse.
DR PRO; PR:Q8CHE4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CHE4; protein.
DR Bgee; ENSMUSG00000044340; Expressed in cerebellar nuclear complex and 244 other tissues.
DR Genevisible; Q8CHE4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0002667; P:regulation of T cell anergy; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51450; LRR; 17.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cytoplasm; Hydrolase;
KW Leucine-rich repeat; Manganese; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..1687
FT /note="PH domain leucine-rich repeat-containing protein
FT phosphatase 1"
FT /id="PRO_0000057782"
FT DOMAIN 492..592
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REPEAT 594..615
FT /note="LRR 1"
FT REPEAT 617..638
FT /note="LRR 2"
FT REPEAT 648..669
FT /note="LRR 3"
FT REPEAT 671..692
FT /note="LRR 4"
FT REPEAT 694..715
FT /note="LRR 5"
FT REPEAT 717..739
FT /note="LRR 6"
FT REPEAT 740..760
FT /note="LRR 7"
FT REPEAT 764..785
FT /note="LRR 8"
FT REPEAT 788..809
FT /note="LRR 9"
FT REPEAT 829..850
FT /note="LRR 10"
FT REPEAT 851..872
FT /note="LRR 11"
FT REPEAT 874..895
FT /note="LRR 12"
FT REPEAT 897..918
FT /note="LRR 13"
FT REPEAT 919..940
FT /note="LRR 14"
FT REPEAT 943..964
FT /note="LRR 15"
FT REPEAT 969..989
FT /note="LRR 16"
FT REPEAT 993..1014
FT /note="LRR 17"
FT REPEAT 1017..1038
FT /note="LRR 18"
FT REPEAT 1040..1061
FT /note="LRR 19"
FT REPEAT 1062..1083
FT /note="LRR 20"
FT REPEAT 1085..1106
FT /note="LRR 21"
FT DOMAIN 1131..1378
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1685..1687
FT /note="PDZ-binding"
FT COMPBIAS 314..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 1166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 1167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 1330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 1369
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60346"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60346"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60346"
FT VAR_SEQ 1..468
FT /note="Missing (in isoform 2)"
FT /id="VSP_057810"
FT CONFLICT 724
FT /note="S -> F (in Ref. 3; AAH59254)"
FT /evidence="ECO:0000305"
FT CONFLICT 1506
FT /note="E -> K (in Ref. 3; AAH22703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1687 AA; 182367 MW; 32B0809AAB3D2412 CRC64;
MEPAAAAPAQ RLADPTGEDQ ALAAAAAEGG RCPDPALSAA APSGGNGGAA REEAPCEAPP
GPLPGRAGGT GRRRRRGAPQ PAAGGAAPVP AAGGGANSLL LKRGRLKRNL SAAAAASSSS
SPSSASSAAG GLPASCSASA SLCTRSLDRK TLLLKHRQLL QLQPSDRDWV RHQLQRGCVH
VFDRHMASSY LRPVLCTLDT TAAEVAARLL QLGHKGGGVV KVLGYGPPPA AAPAASDQTL
DGEHGRDVEP PPSSGTVGAV RGPARAPPAD LPLPGGAWTR CAPRISPAPS DSSPGELFAG
GPGSPPRAPR PASDTESFSL SPSAESVSDR LDPYSSGGGG SSSSSEELEA DPAMPHRPGR
PAQPRPPSPK TSALLQPKAP TGVDSTGVIA GEGPGDDKAM AAAAPDVPLS TSGRIRETVQ
KTSPPSLYVQ LHGETTRRLE ADEKPLQIQN DYLFQLGFGE LWRVQEEGMD SEIGCLIRFY
AGKPHSTGSS ERIQLSGMYN VRKGKMQLPV NRWTRRQVIL CGTCLIVSSV KDSVSGKMHV
LPLIGGKVEE VKKHQHCLAF SSSGPQSQTY YICFDTFTEY LRWLRQVSKV ASQRISSVDL
SCCSLEHLPA NLFYSQDLTH LNLKQNFLRQ TPTLPAARGL GELQRFTKLK SLNLSNNHLG
AFPSAVCSIP TLAELNVSCN ALREVPAAVG DMQNLQTFLL DGNFLQSLPA ELESMHQLSY
LGLSFNEFTD IPEVLEKLTA VDKLCMAGNC VETLRLQALR RMPHIKHVDL RLNILRKLMA
DEVDFVQHVT QLDLRDNKLG DLDAMIFNNI EVLHCERNQL VTLNVCGYFL KALYASSNEL
AQLDVYPVPN YLSYMDVSRN CLESVPEWVC ESRKLEVLDI GHNQICELPA RLFCNSSLRK
LLAGHNRLAR LPERLERTSV EVLDVQHNQI TELPPNLLMK ADSLRFLNAS ANKLETLPPA
TLSEETSSIL QELYLTNNCL TDKCVPLLTG HPRLKILHMA YNRLQSFPAS KMAKLEELEE
IDISGNKLKA IPTTIMNCRR MHTVIAHSNC IEVFPEVMQL PEVKCVDLSC NELSEITLPE
NLPPKLQELD LTGNPRLALD HKSLELLNNI RCFKIDQPSA GDASGAPAVW SHGYTEASGV
KNKLCVAALS VNNFRDNREA LYGVFDGDRN VEVPYLLQCT MSDILAEELQ KTKNEEEYMV
NTFIVMQRKL GTAGQKLGGA AVLCHIKPDP VDLGGSFTLT SANVGKCQTV LCRNGKPLSL
SRSYIMSCEE ERKRIKQHKA IITEDGKVNG VTESTRILGY TFLHPSVVPR PHVQSVLLTP
QDEFFILGSK GLWDSLSIDE AVEAVRNVPD ALAAAKKLCT LAQSYGCHDS ISAVVVQLSV
TEDSFCCCEL SAGGSMPPPS PGIFPPSVNM VIKDRPSDGL GVPSSSSGMA SEISSELSTS
EMSSEVGSTA SDEPPSGVLN ESSPAYPNEQ RCMLHPVCLS NSFQRQLSSA TFSSAFSDNG
LDSDDEEPIE GVFSNGSRVE VEVDIHCSRA KEKERQQHLL QVPAEASDEG IVISANEDES
GLSKKADFSA VGTIGRRRAN GSVAPQERSH NVIEVAADAP LRKPGGYFAA PAQPDPDDQF
IIPPELEEEV KEIMKHHQEQ QQQQQQQQLP PPPQPPQPQP QPQPQPQPQP QRHFQMDHLP
DCYDTPL
