CYFP2_HUMAN
ID CYFP2_HUMAN Reviewed; 1278 AA.
AC Q96F07; A6NLT2; D3DQJ3; Q53EN5; Q9NTK4; Q9ULQ2; Q9UN29;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 2;
DE AltName: Full=p53-inducible protein 121;
GN Name=CYFIP2 {ECO:0000312|EMBL:AAH11762.1};
GN Synonyms=KIAA1168, PIR121 {ECO:0000312|EMBL:AAD45723.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD45723.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10449408; DOI=10.1093/emboj/18.16.4424;
RA Saller E., Tom E., Brunori M., Otter M., Estreicher A., Mack D.H., Iggo R.;
RT "Increased apoptosis induction by 121F mutant p53.";
RL EMBO J. 18:4424-4437(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND RNA EDITING OF
RP POSITION 320.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB66484.1}
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND RNA EDITING OF
RP POSITION 320.
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAB66484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAD97324.1};
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7] {ECO:0000305, ECO:0000312|EMBL:CAB66484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH11762.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph {ECO:0000312|EMBL:AAH11762.1};
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 [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAC1, AND TISSUE SPECIFICITY.
RX PubMed=15048733; DOI=10.1002/eji.200324726;
RA Mayne M., Moffatt T., Kong H., McLaren P.J., Fowke K.R., Becker K.G.,
RA Namaka M., Schenck A., Bardoni B., Bernstein C.N., Melanson M.;
RT "CYFIP2 is highly abundant in CD4+ cells from multiple sclerosis patients
RT and is involved in T cell adhesion.";
RL Eur. J. Immunol. 34:1217-1227(2004).
RN [10] {ECO:0000305}
RP RNA EDITING OF POSITION 320.
RX PubMed=15731336; DOI=10.1093/nar/gki239;
RA Levanon E.Y., Hallegger M., Kinar Y., Shemesh R., Djinovic-Carugo K.,
RA Rechavi G., Jantsch M.F., Eisenberg E.;
RT "Evolutionarily conserved human targets of adenosine to inosine RNA
RT editing.";
RL Nucleic Acids Res. 33:1162-1168(2005).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17245118; DOI=10.4161/cc.6.1.3665;
RA Jackson R.S. II, Cho Y.-J., Stein S., Liang P.;
RT "CYFIP2, a direct p53 target, is leptomycin-B sensitive.";
RL Cell Cycle 6:95-103(2007).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1062, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP INTERACTION WITH FMR1.
RX PubMed=24658146; DOI=10.1371/journal.pone.0091465;
RA Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L.,
RA Piekorz R.P., Ahmadian M.R.;
RT "Subcellular fractionation and localization studies reveal a direct
RT interaction of the fragile X mental retardation protein (FMRP) with
RT nucleolin.";
RL PLoS ONE 9:E91465-E91465(2014).
RN [15]
RP INVOLVEMENT IN DEE65, AND VARIANTS DEE65 CYS-87; LEU-87 AND PRO-87.
RX PubMed=29534297; DOI=10.1002/ana.25208;
RA Nakashima M., Kato M., Aoto K., Shiina M., Belal H., Mukaida S., Kumada S.,
RA Sato A., Zerem A., Lerman-Sagie T., Lev D., Leong H.Y., Tsurusaki Y.,
RA Mizuguchi T., Miyatake S., Miyake N., Ogata K., Saitsu H., Matsumoto N.;
RT "De novo hotspot variants in CYFIP2 cause early-onset epileptic
RT encephalopathy.";
RL Ann. Neurol. 83:794-806(2018).
CC -!- FUNCTION: Involved in T-cell adhesion and p53/TP53-dependent induction
CC of apoptosis. Does not bind RNA. As component of the WAVE1 complex,
CC required for BDNF-NTRK2 endocytic trafficking and signaling from early
CC endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6,
CC ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733,
CC ECO:0000269|PubMed:17245118}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP2, BRK1,
CC NCKAP1 and WASF1/WAVE1. Interacts with FMR1, FXR1 and FXR2 (By
CC similarity). Interacts with FMR1 isoform 6; the interaction occurs in a
CC RNA-dependent manner (PubMed:24658146). Interacts with RAC1 (activated
CC form) which causes the complex to dissociate, releasing activated WASF1
CC (PubMed:15048733). The complex can also be activated by NCK1
CC (PubMed:15048733). Interacts with SHANK3; the interaction mediates the
CC association of SHANK3 with the WAVE1 complex (By similarity). Interacts
CC with TMEM108 (via N-terminus); the interaction associates TMEM108 with
CC the WAVE1 complex (By similarity). {ECO:0000250|UniProtKB:Q5SQX6,
CC ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:24658146}.
CC -!- INTERACTION:
CC Q96F07; Q06787: FMR1; NbExp=2; IntAct=EBI-2433893, EBI-366305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10449408,
CC ECO:0000269|PubMed:17245118}. Nucleus {ECO:0000269|PubMed:17245118}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5SQX6}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q5SQX6}. Note=Highly expressed in
CC the perinuclear regionand enriched in synaptosomes (By similarity).
CC Treatment with leptomycin-B triggers translocation to the nucleus
CC (PubMed:17245118). {ECO:0000250|UniProtKB:Q5SQX6,
CC ECO:0000269|PubMed:17245118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96F07-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10449408};
CC IsoId=Q96F07-2; Sequence=VSP_052349;
CC -!- TISSUE SPECIFICITY: Expressed in T-cells. Increased expression is
CC observed in CD4(+) T-lymphocytes from patients with multiple sclerosis
CC (at protein level). {ECO:0000269|PubMed:15048733}.
CC -!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:17245118}.
CC -!- RNA EDITING: Modified_positions=320 {ECO:0000269|PubMed:10574461,
CC ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:15731336};
CC Note=Partially edited. Editing appears to be brain-specific.
CC {ECO:0000269|PubMed:15731336};
CC -!- DISEASE: Developmental and epileptic encephalopathy 65 (DEE65)
CC [MIM:618008]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE65 is an autosomal dominant form characterized by
CC onset of intractable seizures usually in the first 6 months of life and
CC severe to profound psychomotor developmental delay.
CC {ECO:0000269|PubMed:29534297}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86482.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD97324.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF160973; AAD45723.1; -; mRNA.
DR EMBL; AB032994; BAA86482.2; ALT_INIT; mRNA.
DR EMBL; AL136549; CAB66484.1; -; mRNA.
DR EMBL; AK223604; BAD97324.1; ALT_INIT; mRNA.
DR EMBL; AC008676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61604.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61605.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61606.1; -; Genomic_DNA.
DR EMBL; BC011762; AAH11762.1; -; mRNA.
DR CCDS; CCDS75364.1; -. [Q96F07-2]
DR CCDS; CCDS78077.1; -. [Q96F07-1]
DR PIR; T46248; T46248.
DR RefSeq; NP_001032410.1; NM_001037333.2. [Q96F07-2]
DR RefSeq; NP_001278650.1; NM_001291721.1.
DR RefSeq; NP_001278651.1; NM_001291722.1. [Q96F07-1]
DR RefSeq; NP_055191.2; NM_014376.3. [Q96F07-2]
DR RefSeq; XP_011532818.1; XM_011534516.2. [Q96F07-2]
DR RefSeq; XP_016864830.1; XM_017009341.1. [Q96F07-2]
DR AlphaFoldDB; Q96F07; -.
DR SMR; Q96F07; -.
DR BioGRID; 117945; 129.
DR IntAct; Q96F07; 47.
DR MINT; Q96F07; -.
DR STRING; 9606.ENSP00000444645; -.
DR GlyGen; Q96F07; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96F07; -.
DR MetOSite; Q96F07; -.
DR PhosphoSitePlus; Q96F07; -.
DR SwissPalm; Q96F07; -.
DR BioMuta; CYFIP2; -.
DR DMDM; 134034199; -.
DR EPD; Q96F07; -.
DR jPOST; Q96F07; -.
DR MassIVE; Q96F07; -.
DR MaxQB; Q96F07; -.
DR PaxDb; Q96F07; -.
DR PeptideAtlas; Q96F07; -.
DR PRIDE; Q96F07; -.
DR ProteomicsDB; 76481; -. [Q96F07-1]
DR ProteomicsDB; 76482; -. [Q96F07-2]
DR Antibodypedia; 28408; 150 antibodies from 27 providers.
DR DNASU; 26999; -.
DR Ensembl; ENST00000616178.4; ENSP00000479719.1; ENSG00000055163.20. [Q96F07-1]
DR Ensembl; ENST00000618329.4; ENSP00000484819.1; ENSG00000055163.20. [Q96F07-2]
DR Ensembl; ENST00000620254.5; ENSP00000479968.1; ENSG00000055163.20. [Q96F07-2]
DR GeneID; 26999; -.
DR KEGG; hsa:26999; -.
DR MANE-Select; ENST00000620254.5; ENSP00000479968.1; NM_001037333.3; NP_001032410.1. [Q96F07-2]
DR UCSC; uc003lwt.5; human. [Q96F07-1]
DR CTD; 26999; -.
DR DisGeNET; 26999; -.
DR GeneCards; CYFIP2; -.
DR HGNC; HGNC:13760; CYFIP2.
DR HPA; ENSG00000055163; Tissue enhanced (brain, kidney, lymphoid tissue).
DR MalaCards; CYFIP2; -.
DR MIM; 606323; gene.
DR MIM; 618008; phenotype.
DR neXtProt; NX_Q96F07; -.
DR OpenTargets; ENSG00000055163; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA38368; -.
DR VEuPathDB; HostDB:ENSG00000055163; -.
DR eggNOG; KOG3534; Eukaryota.
DR GeneTree; ENSGT00500000044831; -.
DR HOGENOM; CLU_002688_2_1_1; -.
DR InParanoid; Q96F07; -.
DR OMA; MPKVCKL; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; Q96F07; -.
DR PathwayCommons; Q96F07; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q96F07; -.
DR BioGRID-ORCS; 26999; 13 hits in 286 CRISPR screens.
DR ChiTaRS; CYFIP2; human.
DR GeneWiki; CYFIP2; -.
DR GenomeRNAi; 26999; -.
DR Pharos; Q96F07; Tbio.
DR PRO; PR:Q96F07; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96F07; protein.
DR Bgee; ENSG00000055163; Expressed in renal medulla and 207 other tissues.
DR ExpressionAtlas; Q96F07; baseline and differential.
DR Genevisible; Q96F07; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 2.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cell adhesion; Cytoplasm;
KW Disease variant; Epilepsy; Nucleus; Reference proteome; RNA editing;
KW Synapse; Synaptosome.
FT CHAIN 1..1278
FT /note="Cytoplasmic FMR1-interacting protein 2"
FT /id="PRO_0000279709"
FT MOD_RES 1062
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 558..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10449408,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:15489334"
FT /id="VSP_052349"
FT VARIANT 87
FT /note="R -> C (in DEE65; dbSNP:rs1131692231)"
FT /evidence="ECO:0000269|PubMed:29534297"
FT /id="VAR_080817"
FT VARIANT 87
FT /note="R -> L (in DEE65; dbSNP:rs1554108163)"
FT /evidence="ECO:0000269|PubMed:29534297"
FT /id="VAR_080818"
FT VARIANT 87
FT /note="R -> P (in DEE65; dbSNP:rs1554108163)"
FT /evidence="ECO:0000269|PubMed:29534297"
FT /id="VAR_080819"
FT VARIANT 320
FT /note="K -> E (in RNA edited version; dbSNP:rs3207362)"
FT /evidence="ECO:0000269|PubMed:15731336"
FT /id="VAR_030953"
FT CONFLICT 796
FT /note="I -> T (in Ref. 8; AAH11762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1278 AA; 148399 MW; D6562B1204DC2463 CRC64;
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGHEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMKFMYFQR KAIERFCSEV KRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD
IVNICVDYYE NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS KWTCTQSSIS PQYNICEQMV QIRDDHIRFI
SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL SKWSAHVMEV YSWKLVHPTD
KFCNKDCPGT AEEYERATRY NYTSEEKFAF VEVIAMIKGL QVLMGRMESV FNQAIRNTIY
AALQDFAQVT LREPLRQAVR KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG
GFDIKVPRRA VGPSSTQACQ WSPRALFHPT GGTQGRRGCR SLLYMVRTML ESLIADKSGS
KKTLRSSLDG PIVLAIEDFH KQSFFFTHLL NISEALQQCC DLSQLWFREF FLELTMGRRI
QFPIEMSMPW ILTDHILETK EPSMMEYVLY PLDLYNDSAY YALTKFKKQF LYDEIEAEVN
LCFDQFVYKL ADQIFAYYKA MAGSVLLDKR FRAECKNYGV IIPYPPSNRY ETLLKQRHVQ
LLGRSIDLNR LITQRISAAM YKSLDQAISR FESEDLTSIV ELEWLLEINR LTHRLLCKHM
TLDSFDAMFR EANHNVSAPY GRITLHVFWE LNFDFLPNYC YNGSTNRFVR TAIPFTQEPQ
RDKPANVQPY YLYGSKPLNI AYSHIYSSYR NFVGPPHFKT ICRLLGYQGI AVVMEELLKI
VKSLLQGTIL QYVKTLIEVM PKICRLPRHE YGSPGILEFF HHQLKDIIEY AELKTDVFQS
LREVGNAILF CLLIEQALSQ EEVCDLLHAA PFQNILPRVY IKEGERLEVR MKRLEAKYAP
LHLVPLIERL GTPQQIAIAR EGDLLTKERL CCGLSMFEVI LTRIRSYLQD PIWRGPPPTN
GVMHVDECVE FHRLWSAMQF VYCIPVGTNE FTAEQCFGDG LNWAGCSIIV LLGQQRRFDL
FDFCYHLLKV QRQDGKDEII KNVPLKKMAD RIRKYQILNN EVFAILNKYM KSVETDSSTV
EHVRCFQPPI HQSLATTC
