SYNJ2_HUMAN
ID SYNJ2_HUMAN Reviewed; 1496 AA.
AC O15056; Q5TA13; Q5TA16; Q5TA19; Q86XK0; Q8IZA8; Q9H226;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Synaptojanin-2;
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q9D2G5};
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2;
GN Name=SYNJ2; Synonyms=KIAA0348;
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 [MRNA] (ISOFORM 2A).
RA Jeong S.-Y., Youle R.J.;
RT "cDNA cloning of human SH3 domain-containing proteins, synaptojanin 2A.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B2), AND SUBCELLULAR LOCATION.
RX PubMed=11084340; DOI=10.1016/s0960-9822(00)00778-8;
RA Malecz N., McCabe P.C., Spaargaren C., Qiu R.-G., Chuang Y.-Y., Symons M.;
RT "Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated
RT endocytosis.";
RL Curr. Biol. 10:1383-1386(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-1496 (ISOFORM 2B2).
RC TISSUE=Brain;
RX PubMed=11498538; DOI=10.1074/jbc.m106404200;
RA Nemoto Y., Wenk M.R., Watanabe M., Daniell L., Murakami T., Ringstad N.,
RA Yamada H., Takei K., De Camilli P.;
RT "Identification and characterization of a synaptojanin 2 splice isoform
RT predominantly expressed in nerve terminals.";
RL J. Biol. Chem. 276:41133-41142(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-1496 (ISOFORM 2B2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-1496 (ISOFORM 2B2), AND
RP VARIANT GLY-1468.
RC TISSUE=Testis;
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 [7]
RP IDENTIFICATION BY 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1124 AND SER-1191, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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-1191, 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 STRUCTURE BY NMR OF 819-969.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNP domain in synaptojanin 2.";
RL Submitted (DEC-2003) to the PDB data bank.
CC -!- FUNCTION: Inositol 5-phosphatase which may be involved in distinct
CC membrane trafficking and signal transduction pathways. May mediate the
CC inhibitory effect of Rac1 on endocytosis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000250|UniProtKB:Q9D2G5};
CC -!- SUBUNIT: Binds to GRB2. Isoform 2A binds to SYNJ2BP/OMP25. Isoform 2B2
CC C-terminal proline-rich region binds to a variety of SH3 domain-
CC containing proteins including SH3GL1, SH3GL2, SH3GL3 and GRB2.
CC -!- INTERACTION:
CC O15056; P62993: GRB2; NbExp=2; IntAct=EBI-310513, EBI-401755;
CC O15056; P16333: NCK1; NbExp=3; IntAct=EBI-310513, EBI-389883;
CC O15056; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-310513, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11084340}. Cell
CC membrane {ECO:0000269|PubMed:11084340}. Membrane raft
CC {ECO:0000269|PubMed:11084340}. Presynapse
CC {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O55207}. Note=Localizes at presynapse terminals
CC in brain and at bundles of microtubules surrounding the nucleus in the
CC elongating spermatids corresponding to the manchette (By similarity).
CC Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent
CC manner (PubMed:11084340). {ECO:0000269|PubMed:11084340}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=2B2;
CC IsoId=O15056-1; Sequence=Displayed;
CC Name=2B1;
CC IsoId=O15056-2; Sequence=VSP_012911;
CC Name=2A;
CC IsoId=O15056-3; Sequence=VSP_012912, VSP_012913;
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43277.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY152396; AAN73051.1; -; mRNA.
DR EMBL; AF318616; AAG46036.1; -; mRNA.
DR EMBL; AL139330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF039945; AAD02178.1; -; mRNA.
DR EMBL; AB002346; BAA20805.2; -; mRNA.
DR EMBL; BC043277; AAH43277.1; ALT_INIT; mRNA.
DR CCDS; CCDS5254.1; -. [O15056-1]
DR RefSeq; NP_001171559.1; NM_001178088.1.
DR RefSeq; NP_003889.1; NM_003898.3. [O15056-1]
DR RefSeq; XP_006715655.1; XM_006715592.3. [O15056-3]
DR RefSeq; XP_011534527.1; XM_011536225.1.
DR PDB; 1UFW; NMR; -; A=882-963.
DR PDBsum; 1UFW; -.
DR AlphaFoldDB; O15056; -.
DR SMR; O15056; -.
DR BioGRID; 114391; 35.
DR IntAct; O15056; 18.
DR MINT; O15056; -.
DR STRING; 9606.ENSP00000347792; -.
DR ChEMBL; CHEMBL4523129; -.
DR DEPOD; SYNJ2; -.
DR iPTMnet; O15056; -.
DR PhosphoSitePlus; O15056; -.
DR BioMuta; SYNJ2; -.
DR EPD; O15056; -.
DR jPOST; O15056; -.
DR MassIVE; O15056; -.
DR MaxQB; O15056; -.
DR PaxDb; O15056; -.
DR PeptideAtlas; O15056; -.
DR PRIDE; O15056; -.
DR ProteomicsDB; 48407; -. [O15056-1]
DR ProteomicsDB; 48408; -. [O15056-2]
DR ProteomicsDB; 48409; -. [O15056-3]
DR Antibodypedia; 33432; 203 antibodies from 27 providers.
DR DNASU; 8871; -.
DR Ensembl; ENST00000355585.9; ENSP00000347792.4; ENSG00000078269.15. [O15056-1]
DR Ensembl; ENST00000640338.1; ENSP00000492532.1; ENSG00000078269.15. [O15056-3]
DR GeneID; 8871; -.
DR KEGG; hsa:8871; -.
DR MANE-Select; ENST00000355585.9; ENSP00000347792.4; NM_003898.4; NP_003889.1.
DR UCSC; uc003qqx.3; human. [O15056-1]
DR CTD; 8871; -.
DR DisGeNET; 8871; -.
DR GeneCards; SYNJ2; -.
DR HGNC; HGNC:11504; SYNJ2.
DR HPA; ENSG00000078269; Tissue enriched (brain).
DR MIM; 609410; gene.
DR neXtProt; NX_O15056; -.
DR OpenTargets; ENSG00000078269; -.
DR PharmGKB; PA36286; -.
DR VEuPathDB; HostDB:ENSG00000078269; -.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000160715; -.
DR HOGENOM; CLU_003016_5_2_1; -.
DR InParanoid; O15056; -.
DR OMA; RVLWWRR; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; O15056; -.
DR TreeFam; TF354311; -.
DR BioCyc; MetaCyc:HS01279-MON; -.
DR PathwayCommons; O15056; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O15056; -.
DR BioGRID-ORCS; 8871; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; SYNJ2; human.
DR EvolutionaryTrace; O15056; -.
DR GenomeRNAi; 8871; -.
DR Pharos; O15056; Tchem.
DR PRO; PR:O15056; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15056; protein.
DR Bgee; ENSG00000078269; Expressed in inferior vagus X ganglion and 204 other tissues.
DR ExpressionAtlas; O15056; baseline and differential.
DR Genevisible; O15056; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0034596; F:phosphatidylinositol phosphate 4-phosphatase activity; TAS:Reactome.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; TAS:Reactome.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; TAS:Reactome.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; TAS:Reactome.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd12720; RRM_SYNJ2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034974; SYNJ2.
DR InterPro; IPR034973; SYNJ2_RRM.
DR PANTHER; PTHR11200:SF148; PTHR11200:SF148; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Hydrolase; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; RNA-binding; Synapse.
FT CHAIN 1..1496
FT /note="Synaptojanin-2"
FT /id="PRO_0000209733"
FT DOMAIN 120..444
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 889..968
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 450..?
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 1027..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1070..1114
FT /note="Missing (in isoform 2B1)"
FT /evidence="ECO:0000305"
FT /id="VSP_012911"
FT VAR_SEQ 1249..1288
FT /note="PLSPEEQFEQQTVHFTIGPPETSVEAPPVVTAPRVPPVPK -> IVFCSRSQ
FT ASQPCLLLQRHEFVRTVAAQRLASVDTSGSSV (in isoform 2A)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012912"
FT VAR_SEQ 1289..1496
FT /note="Missing (in isoform 2A)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012913"
FT VARIANT 1468
FT /note="E -> G (in dbSNP:rs2502601)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024507"
FT STRAND 891..898
FT /evidence="ECO:0007829|PDB:1UFW"
FT HELIX 901..905
FT /evidence="ECO:0007829|PDB:1UFW"
FT HELIX 909..922
FT /evidence="ECO:0007829|PDB:1UFW"
FT STRAND 926..931
FT /evidence="ECO:0007829|PDB:1UFW"
FT STRAND 934..938
FT /evidence="ECO:0007829|PDB:1UFW"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:1UFW"
FT HELIX 951..953
FT /evidence="ECO:0007829|PDB:1UFW"
FT STRAND 954..956
FT /evidence="ECO:0007829|PDB:1UFW"
FT STRAND 959..963
FT /evidence="ECO:0007829|PDB:1UFW"
SQ SEQUENCE 1496 AA; 165538 MW; 7CC9E368585ACF21 CRC64;
MALSKGLRLL GRLGAEGDCS VLLEARGRDD CLLFEAGTVA TLAPEEKEVI KGQYGKLTDA
YGCLGELRLK SGGTSLSFLV LVTGCTSVGR IPDAEIYKIT ATDFYPLQEE AKEEERLIAL
KKILSSGVFY FSWPNDGSRF DLTVRTQKQG DDSSEWGNSF FWNQLLHVPL RQHQVSCCDW
LLKIICGVVT IRTVYASHKQ AKACLVSRVS CERTGTRFHT RGVNDDGHVS NFVETEQMIY
MDDGVSSFVQ IRGSVPLFWE QPGLQVGSHH LRLHRGLEAN APAFDRHMVL LKEQYGQQVV
VNLLGSRGGE EVLNRAFKKL LWASCHAGDT PMINFDFHQF AKGGKLEKLE TLLRPQLKLH
WEDFDVFTKG ENVSPRFQKG TLRMNCLDCL DRTNTVQSFI ALEVLHLQLK TLGLSSKPIV
DRFVESFKAM WSLNGHSLSK VFTGSRALEG KAKVGKLKDG ARSMSRTIQS NFFDGVKQEA
IKLLLVGDVY GEEVADKGGM LLDSTALLVT PRILKAMTER QSEFTNFKRI RIAMGTWNVN
GGKQFRSNVL RTAELTDWLL DSPQLSGATD SQDDSSPADI FAVGFEEMVE LSAGNIVNAS
TTNKKMWGEQ LQKAISRSHR YILLTSAQLV GVCLYIFVRP YHVPFIRDVA IDTVKTGMGG
KAGNKGAVGI RFQFHSTSFC FICSHLTAGQ SQVKERNEDY KEITQKLCFP MGRNVFSHDY
VFWCGDFNYR IDLTYEEVFY FVKRQDWKKL LEFDQLQLQK SSGKIFKDFH EGAINFGPTY
KYDVGSAAYD TSDKCRTPAW TDRVLWWRKK HPFDKTAGEL NLLDSDLDVD TKVRHTWSPG
ALQYYGRAEL QASDHRPVLA IVEVEVQEVD VGARERVFQE VSSFQGPLDA TVVVNLQSPT
LEEKNEFPED LRTELMQTLG SYGTIVLVRI NQGQMLVTFA DSHSALSVLD VDGMKVKGRA
VKIRPKTKDW LKGLREEIIR KRDSMAPVSP TANSCLLEEN FDFTSLDYES EGDILEDDED
YLVDEFNQPG VSDSELGGDD LSDVPGPTAL APPSKSPALT KKKQHPTYKD DADLVELKRE
LEAVGEFRHR SPSRSLSVPN RPRPPQPPQR PPPPTGLMVK KSASDASISS GTHGQYSILQ
TARLLPGAPQ QPPKARTGIS KPYNVKQIKT TNAQEAEAAI RCLLEARGGA SEEALSAVAP
RDLEASSEPE PTPGAAKPET PQAPPLLPRR PPPRVPAIKK PTLRRTGKPL SPEEQFEQQT
VHFTIGPPET SVEAPPVVTA PRVPPVPKPR TFQPGKAAER PSHRKPASDE APPGAGASVP
PPLEAPPLVP KVPPRRKKSA PAAFHLQVLQ SNSQLLQGLT YNSSDSPSGH PPAAGTVFPQ
GDFLSTSSAT SPDSDGTKAM KPEAAPLLGD YQDPFWNLLH HPKLLNNTWL SKSSDPLDSG
TRSPKRDPID PVSAGASAAK AELPPDHEHK TLGHWVTISD QEKRTALQVF DPLAKT
