N4BP1_HUMAN
ID N4BP1_HUMAN Reviewed; 896 AA.
AC O75113; A7MD49; Q2YDX1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=NEDD4-binding protein 1 {ECO:0000250|UniProtKB:Q6A037};
DE Short=N4BP1 {ECO:0000250|UniProtKB:Q6A037};
DE EC=3.1.-.- {ECO:0000269|PubMed:31133753};
GN Name=N4BP1 {ECO:0000312|HGNC:HGNC:29850};
GN Synonyms=KIAA0615 {ECO:0000303|PubMed:9734811};
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 [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-300, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242 AND SER-300, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, 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 [10]
RP DOMAIN, UBIQUITINATION, AND MUTAGENESIS OF PRO-866.
RX PubMed=31319543; DOI=10.3390/biom9070284;
RA Nepravishta R., Ferrentino F., Mandaliti W., Mattioni A., Weber J.,
RA Polo S., Castagnoli L., Cesareni G., Paci M., Santonico E.;
RT "CoCUN, a novel ubiquitin binding domain identified in N4BP1.";
RL Biomolecules 9:0-0(2019).
RN [11]
RP ERRATUM OF PUBMED:31319543.
RX PubMed=31795258; DOI=10.3390/biom9120803;
RA Nepravishta R., Ferrentino F., Mandaliti W., Mattioni A., Weber J.,
RA Polo S., Castagnoli L., Cesareni G., Paci M., Santonico E.;
RL Biomolecules 9:0-0(2019).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PROTEOLYTIC CLEAVAGE,
RP INDUCTION, AND MUTAGENESIS OF ARG-509 AND ASP-623.
RX PubMed=31133753; DOI=10.1038/s41564-019-0460-3;
RA Yamasoba D., Sato K., Ichinose T., Imamura T., Koepke L., Joas S.,
RA Reith E., Hotter D., Misawa N., Akaki K., Uehata T., Mino T., Miyamoto S.,
RA Noda T., Yamashita A., Standley D.M., Kirchhoff F., Sauter D., Koyanagi Y.,
RA Takeuchi O.;
RT "N4BP1 restricts HIV-1 and its inactivation by MALT1 promotes viral
RT reactivation.";
RL Nat. Microbiol. 4:1532-1544(2019).
RN [13] {ECO:0007744|PDB:6Q3V}
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 8-193.
RA Garg A., Heinemann U.;
RT "Crystal structure of Human N4BP1 KH domains.";
RL Submitted (DEC-2018) to the PDB data bank.
CC -!- FUNCTION: Potent suppressor of cytokine production that acts as a
CC regulator of innate immune signaling and inflammation. Acts as a key
CC negative regulator of select cytokine and chemokine responses elicited
CC by TRIF-independent Toll-like receptors (TLRs), thereby limiting
CC inflammatory cytokine responses to minor insults. In response to more
CC threatening pathogens, cleaved by CASP8 downstream of TLR3 or TLR4,
CC leading to its inactivation, thereby allowing production of
CC inflammatory cytokines (By similarity). Acts as a restriction factor
CC against some viruses, such as HIV-1: restricts HIV-1 replication by
CC binding to HIV-1 mRNAs and mediating their degradation via its
CC ribonuclease activity (PubMed:31133753). Also acts as an inhibitor of
CC the E3 ubiquitin-protein ligase ITCH: acts by interacting with the
CC second WW domain of ITCH, leading to compete with ITCH's substrates and
CC impairing ubiquitination of substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q6A037, ECO:0000269|PubMed:31133753}.
CC -!- ACTIVITY REGULATION: Proteolytic cleavage by CASP8 or MALT1 leads to
CC its inactivation. {ECO:0000269|PubMed:31133753}.
CC -!- SUBUNIT: Interacts with NEDD4. Interacts with ITCH (via WW domain 2).
CC {ECO:0000250|UniProtKB:Q6A037}.
CC -!- INTERACTION:
CC O75113; Q96J02: ITCH; NbExp=3; IntAct=EBI-5278391, EBI-1564678;
CC O75113; Q99732: LITAF; NbExp=3; IntAct=EBI-5278391, EBI-725647;
CC O75113; O15344: MID1; NbExp=3; IntAct=EBI-5278391, EBI-2340316;
CC O75113; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-5278391, EBI-6115874;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6A037}. Nucleus {ECO:0000250|UniProtKB:Q6A037}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6A037}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q6A037}. Note=Primarily localizes to the
CC nucleolus. Also localizes to the PML nuclear bodies, when desumoylated.
CC {ECO:0000250|UniProtKB:Q6A037}.
CC -!- TISSUE SPECIFICITY: Detected in heart, lung, brain, liver, skeletal
CC muscle, pancreas, kidney, spleen, testis and ovary.
CC {ECO:0000269|PubMed:9734811}.
CC -!- INDUCTION: Up-regulated in response to interferon alpha (IFN-alpha)
CC stimulation (at protein level). {ECO:0000269|PubMed:31133753}.
CC -!- DOMAIN: The CoCUN region mediates binding to ubiquitin
CC (PubMed:31319543). Does not interact with NEDD8 (PubMed:31319543).
CC {ECO:0000269|PubMed:31319543}.
CC -!- PTM: Proteolytically cleaved by CASP8 downstream of TLR3 or TLR4,
CC leading to its inactivation. Mainly cleaved at Asp-490 by CASP8 (By
CC similarity). Cleaved by caspase-like protein MALT1 in T-cells following
CC TCR-mediated activation, leading to its inactivation and subsequent
CC viral reactivation during HIV-1 infection (PubMed:31133753).
CC {ECO:0000250|UniProtKB:Q6A037, ECO:0000269|PubMed:31133753}.
CC -!- PTM: Mono- and polyubiquitinated on the CoCUN region (PubMed:31319543).
CC Monoubiquitinated by NEDD4 (By similarity). Polyubiquitinated, leading
CC to its degradation by the proteasome (By similarity). Sumoylated with
CC SUMO1, abrogating polyubiquitination and subsequent degradation (By
CC similarity). Desumoylated by SENP1, leading to accumulation in PML
CC nuclear bodies (By similarity). {ECO:0000250|UniProtKB:Q6A037,
CC ECO:0000269|PubMed:31319543}.
CC -!- SIMILARITY: Belongs to the N4BP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31590.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014515; BAA31590.2; ALT_INIT; mRNA.
DR EMBL; AC023813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108288; AAI08289.1; -; mRNA.
DR EMBL; BC152472; AAI52473.1; -; mRNA.
DR CCDS; CCDS45479.1; -.
DR PIR; T00389; T00389.
DR RefSeq; NP_694574.3; NM_153029.3.
DR PDB; 6Q3V; X-ray; 1.88 A; A=8-193.
DR PDBsum; 6Q3V; -.
DR AlphaFoldDB; O75113; -.
DR SMR; O75113; -.
DR BioGRID; 115036; 35.
DR DIP; DIP-41205N; -.
DR IntAct; O75113; 11.
DR MINT; O75113; -.
DR STRING; 9606.ENSP00000262384; -.
DR GlyGen; O75113; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; O75113; -.
DR MetOSite; O75113; -.
DR PhosphoSitePlus; O75113; -.
DR BioMuta; N4BP1; -.
DR EPD; O75113; -.
DR jPOST; O75113; -.
DR MassIVE; O75113; -.
DR MaxQB; O75113; -.
DR PaxDb; O75113; -.
DR PeptideAtlas; O75113; -.
DR PRIDE; O75113; -.
DR ProteomicsDB; 49772; -.
DR Antibodypedia; 49389; 137 antibodies from 28 providers.
DR DNASU; 9683; -.
DR Ensembl; ENST00000262384.4; ENSP00000262384.3; ENSG00000102921.8.
DR GeneID; 9683; -.
DR KEGG; hsa:9683; -.
DR MANE-Select; ENST00000262384.4; ENSP00000262384.3; NM_153029.4; NP_694574.3.
DR UCSC; uc002efp.3; human.
DR CTD; 9683; -.
DR DisGeNET; 9683; -.
DR GeneCards; N4BP1; -.
DR HGNC; HGNC:29850; N4BP1.
DR HPA; ENSG00000102921; Low tissue specificity.
DR MIM; 619138; gene.
DR neXtProt; NX_O75113; -.
DR OpenTargets; ENSG00000102921; -.
DR PharmGKB; PA162396561; -.
DR VEuPathDB; HostDB:ENSG00000102921; -.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000158682; -.
DR HOGENOM; CLU_014137_1_0_1; -.
DR InParanoid; O75113; -.
DR OMA; KIPYKLE; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; O75113; -.
DR TreeFam; TF315783; -.
DR PathwayCommons; O75113; -.
DR SignaLink; O75113; -.
DR BioGRID-ORCS; 9683; 16 hits in 1088 CRISPR screens.
DR ChiTaRS; N4BP1; human.
DR GenomeRNAi; 9683; -.
DR Pharos; O75113; Tbio.
DR PRO; PR:O75113; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75113; protein.
DR Bgee; ENSG00000102921; Expressed in amniotic fluid and 196 other tissues.
DR ExpressionAtlas; O75113; baseline and differential.
DR Genevisible; O75113; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Immunity; Innate immunity; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..896
FT /note="NEDD4-binding protein 1"
FT /id="PRO_0000096680"
FT DOMAIN 59..143
FT /note="KH-like"
FT /evidence="ECO:0000255"
FT DOMAIN 617..769
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT REGION 403..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..896
FT /note="CoCUN"
FT /evidence="ECO:0000305|PubMed:31319543"
FT SITE 200..201
FT /note="Cleavage; by CASP8"
FT /evidence="ECO:0000250|UniProtKB:Q6A037"
FT SITE 326..327
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q6A037"
FT SITE 490..491
FT /note="Cleavage; by CASP8"
FT /evidence="ECO:0000250|UniProtKB:Q6A037"
FT SITE 509..510
FT /note="Cleavage; by MALT1"
FT /evidence="ECO:0000269|PubMed:31133753"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A037"
FT MUTAGEN 509
FT /note="R->A: Abolished cleavage by MALT1."
FT /evidence="ECO:0000269|PubMed:31133753"
FT MUTAGEN 623
FT /note="D->N: Abolihsed ability to degrade HIV-1 mRNAs."
FT /evidence="ECO:0000269|PubMed:31133753"
FT MUTAGEN 866
FT /note="P->A: Abolished ability to interact with ubiquitin."
FT /evidence="ECO:0000269|PubMed:31319543"
FT CONFLICT 62
FT /note="V -> E (in Ref. 1; BAA31590 and 3; AAI52473)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="L -> P (in Ref. 3; AAI08289)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6Q3V"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:6Q3V"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:6Q3V"
SQ SEQUENCE 896 AA; 100379 MW; 171EDCC9D3BCF3D3 CRC64;
MAARAVLDEF TAPAEKAELL EQSRGRIEGL FGVSLAVLGA LGAEEPLPAR IWLQLCGAQE
AVHSAKEYIK GICEPELEER ECYPKDMHCI FVGAESLFLK SLIQDTCADL CILDIGLLGI
RGSAEAVVMA RSHIQQFVKL FENKENLPSS QKESEVKREF KQFVEAHADN YTMDLLILPT
SLKKELLTLT QGEENLFETG DDEVIEMRDS QQTEFTQNAA TGLNISRDET VLQEEARNKA
GTPVSELTKQ MDTVLSSSPD VLFDPINGLT PDEEALSNER ICQKRRFSDS EERHTKKQFS
LENVQEGEIL HDAKTLAGNV IADLSDSSAD SENLSPDIKE TTEEMEYNIL VNFFKTMGYS
QEIVEKVIKV YGPSTEPLLL LEEIEKENKR FQEDREFSAG TVYPETNKTK NKGVYSSTNE
LTTDSTPKKT QAHTQQNMVE KFSQLPFKVE AKPCTSNCRI NTFRTVPIEQ KHEVWGSNQN
YICNTDPETD GLSPSVASPS PKEVNFVSRG ASSHQPRVPL FPENGLHQQP EPLLPNNMKS
ACEKRLGCCS SPHSKPNCST LSPPMPLPQL LPSVTDARSA GPSDHIDSSV TGVQRFRDTL
KIPYKLELKN EPGRTDLKHI VIDGSNVAIT HGLKKFFSCR GIAIAVEYFW KLGNRNITVF
VPQWRTRRDP NVTEQHFLTQ LQELGILSLT PARMVFGERI ASHDDRFLLH LADKTGGIIV
TNDNFREFVN ESVSWREIIT KRLLQYTFVG DIFMVPDDPL GRSGPRLEEF LQKEVCLRDM
QPLLSALPNV GMFDPSFRVP GTQAASTSHQ PPTRIQGAPS SHWLPQQPHF PLLPALPSLQ
QNLPMPAQRS SAETNELREA LLKIFPDSEQ RLKIDQILVA HPYMKDLNAL SAMVLD
