NUP88_HUMAN
ID NUP88_HUMAN Reviewed; 741 AA.
AC Q99567; D3DTM2; Q9BWE5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nuclear pore complex protein Nup88;
DE AltName: Full=88 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup88;
GN Name=NUP88;
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], AND INTERACTION WITH NUP214/CAN.
RC TISSUE=Placenta;
RX PubMed=9049309; DOI=10.1093/emboj/16.4.807;
RA Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D.,
RA Murti K.G., Fransen J., Grosveld G.;
RT "The human homologue of yeast CRM1 is in a dynamic subcomplex with
RT CAN/Nup214 and the novel nuclear pore component Nup88.";
RL EMBO J. 16:807-816(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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-517, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; SER-517 AND
RP THR-525, AND 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; THR-525 AND SER-540, AND
RP IDENTIFICATION BY 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; SER-379; SER-437;
RP SER-442; SER-517 AND THR-525, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP IDENTIFICATION BY 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 [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP62; NUP98 AND NUP214,
RP INVOLVEMENT IN FADS4, VARIANTS FADS4 TYR-434; 509-ARG--PHE-741 DEL AND
RP GLU-634 DEL, AND CHARACTERIZATION OF VARIANTS FADS4 TYR-434;
RP 509-ARG--PHE-741 DEL AND GLU-634 DEL.
RX PubMed=30543681; DOI=10.1371/journal.pgen.1007845;
RA Bonnin E., Cabochette P., Filosa A., Juehlen R., Komatsuzaki S.,
RA Hezwani M., Dickmanns A., Martinelli V., Vermeersch M., Supply L.,
RA Martins N., Pirenne L., Ravenscroft G., Lombard M., Port S., Spillner C.,
RA Janssens S., Roets E., Van Dorpe J., Lammens M., Kehlenbach R.H.,
RA Ficner R., Laing N.G., Hoffmann K., Vanhollebeke B., Fahrenkrog B.;
RT "Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia
RT deformation sequence.";
RL PLoS Genet. 14:E1007845-E1007845(2018).
CC -!- FUNCTION: Component of nuclear pore complex.
CC {ECO:0000269|PubMed:30543681}.
CC -!- SUBUNIT: Interacts with NUP214/CAN (PubMed:9049309, PubMed:30543681).
CC Interacts with NUP62 and NUP98 (PubMed:30543681).
CC {ECO:0000269|PubMed:30543681, ECO:0000269|PubMed:9049309}.
CC -!- INTERACTION:
CC Q99567; P37198: NUP62; NbExp=6; IntAct=EBI-726178, EBI-347978;
CC Q99567; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-726178, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:30543681}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Fetal akinesia deformation sequence 4 (FADS4) [MIM:618393]: A
CC clinically and genetically heterogeneous group of disorders with
CC congenital malformations related to impaired fetal movement. Clinical
CC features include fetal akinesia, intrauterine growth retardation,
CC polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial
CC abnormalities, and cryptorchidism. FADS4 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:30543681}. Note=The disease is caused by
CC variants affecting the gene represented in this entry. Disease
CC mechanism likely includes impaired formation of the neuromuscular
CC junction. NUP88 silencing in vitro results in reduced levels of rapsyn,
CC a key player in clustering of nicotinic acetylcholine receptors
CC (nAChRs) at the neuromuscular junction. Decreased rapsyn levels have
CC also been observed in a patient muscle biopsy.
CC {ECO:0000269|PubMed:30543681}.
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DR EMBL; Y08612; CAA69904.1; -; mRNA.
DR EMBL; CH471108; EAW90340.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90342.1; -; Genomic_DNA.
DR EMBL; BC000335; AAH00335.1; -; mRNA.
DR CCDS; CCDS11070.1; -.
DR RefSeq; NP_001307582.1; NM_001320653.1.
DR RefSeq; NP_002523.2; NM_002532.5.
DR AlphaFoldDB; Q99567; -.
DR SMR; Q99567; -.
DR BioGRID; 110981; 101.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q99567; 50.
DR MINT; Q99567; -.
DR STRING; 9606.ENSP00000458954; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q99567; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99567; -.
DR PhosphoSitePlus; Q99567; -.
DR BioMuta; NUP88; -.
DR DMDM; 25008854; -.
DR EPD; Q99567; -.
DR jPOST; Q99567; -.
DR MassIVE; Q99567; -.
DR MaxQB; Q99567; -.
DR PaxDb; Q99567; -.
DR PeptideAtlas; Q99567; -.
DR PRIDE; Q99567; -.
DR ProteomicsDB; 78327; -.
DR Antibodypedia; 3693; 194 antibodies from 29 providers.
DR DNASU; 4927; -.
DR Ensembl; ENST00000573584.6; ENSP00000458954.1; ENSG00000108559.12.
DR GeneID; 4927; -.
DR KEGG; hsa:4927; -.
DR MANE-Select; ENST00000573584.6; ENSP00000458954.1; NM_002532.6; NP_002523.2.
DR UCSC; uc002gbo.3; human.
DR CTD; 4927; -.
DR DisGeNET; 4927; -.
DR GeneCards; NUP88; -.
DR HGNC; HGNC:8067; NUP88.
DR HPA; ENSG00000108559; Low tissue specificity.
DR MalaCards; NUP88; -.
DR MIM; 602552; gene.
DR MIM; 618393; phenotype.
DR neXtProt; NX_Q99567; -.
DR OpenTargets; ENSG00000108559; -.
DR Orphanet; 994; Fetal akinesia deformation sequence.
DR PharmGKB; PA31855; -.
DR VEuPathDB; HostDB:ENSG00000108559; -.
DR eggNOG; KOG4460; Eukaryota.
DR GeneTree; ENSGT00390000015063; -.
DR InParanoid; Q99567; -.
DR OMA; HINQIQL; -.
DR OrthoDB; 1149034at2759; -.
DR PhylomeDB; Q99567; -.
DR TreeFam; TF105307; -.
DR PathwayCommons; Q99567; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q99567; -.
DR SIGNOR; Q99567; -.
DR BioGRID-ORCS; 4927; 698 hits in 1091 CRISPR screens.
DR ChiTaRS; NUP88; human.
DR GeneWiki; NUP88; -.
DR GenomeRNAi; 4927; -.
DR Pharos; Q99567; Tbio.
DR PRO; PR:Q99567; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99567; protein.
DR Bgee; ENSG00000108559; Expressed in right testis and 198 other tissues.
DR ExpressionAtlas; Q99567; baseline and differential.
DR Genevisible; Q99567; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0017056; F:structural constituent of nuclear pore; TAS:ProtInc.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR InterPro; IPR019321; Nucleoporin_Nup88.
DR InterPro; IPR037700; NUP88/NUP82.
DR PANTHER; PTHR13257; PTHR13257; 1.
DR Pfam; PF10168; Nup88; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Disease variant; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..741
FT /note="Nuclear pore complex protein Nup88"
FT /id="PRO_0000204887"
FT COILED 585..651
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CEC0"
FT VARIANT 289
FT /note="N -> S (in dbSNP:rs1806245)"
FT /id="VAR_029340"
FT VARIANT 434
FT /note="D -> Y (in FADS4; no effect on localization to the
FT nuclear pore complex; no effect on interaction with NUP214
FT and NUP62; dbSNP:rs1567568217)"
FT /evidence="ECO:0000269|PubMed:30543681"
FT /id="VAR_082159"
FT VARIANT 509..741
FT /note="Missing (in FADS4; decreased localization to the
FT nuclear pore complex; decreased interaction with NUP214 and
FT NUP62)"
FT /evidence="ECO:0000269|PubMed:30543681"
FT /id="VAR_082160"
FT VARIANT 634
FT /note="Missing (in FADS4; decreased localization to the
FT nuclear pore complex; decreased interaction with NUP214 and
FT NUP62)"
FT /evidence="ECO:0000269|PubMed:30543681"
FT /id="VAR_082161"
FT CONFLICT 247
FT /note="A -> D (in Ref. 1; CAA69904)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..301
FT /note="GKLLGPLPMHP -> WKAVGSIAHAS (in Ref. 1; CAA69904)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="K -> R (in Ref. 1; CAA69904)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="P -> S (in Ref. 1; CAA69904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 83542 MW; 954A8E2E203BC20B CRC64;
MAAAEGPVGD GELWQTWLPN HVVFLRLREG LKNQSPTEAE KPASSSLPSS PPPQLLTRNV
VFGLGGELFL WDGEDSSFLV VRLRGPSGGG EEPALSQYQR LLCINPPLFE IYQVLLSPTQ
HHVALIGIKG LMVLELPKRW GKNSEFEGGK STVNCSTTPV AERFFTSSTS LTLKHAAWYP
SEILDPHVVL LTSDNVIRIY SLREPQTPTN VIILSEAEEE SLVLNKGRAY TASLGETAVA
FDFGPLAAVP KTLFGQNGKD EVVAYPLYIL YENGETFLTY ISLLHSPGNI GKLLGPLPMH
PAAEDNYGYD ACAVLCLPCV PNILVIATES GMLYHCVVLE GEEEDDHTSE KSWDSRIDLI
PSLYVFECVE LELALKLASG EDDPFDSDFS CPVKLHRDPK CPSRYHCTHE AGVHSVGLTW
IHKLHKFLGS DEEDKDSLQE LSTEQKCFVE HILCTKPLPC RQPAPIRGFW IVPDILGPTM
ICITSTYECL IWPLLSTVHP ASPPLLCTRE DVEVAESPLR VLAETPDSFE KHIRSILQRS
VANPAFLKAS EKDIAPPPEE CLQLLSRATQ VFREQYILKQ DLAKEEIQRR VKLLCDQKKK
QLEDLSYCRE ERKSLREMAE RLADKYEEAK EKQEDIMNRM KKLLHSFHSE LPVLSDSERD
MKKELQLIPD QLRHLGNAIK QVTMKKDYQQ QKMEKVLSLP KPTIILSAYQ RKCIQSILKE
EGEHIREMVK QINDIRNHVN F
