NUFP2_MOUSE
ID NUFP2_MOUSE Reviewed; 692 AA.
AC Q5F2E7; Q3TCE2; Q3V195; Q80TF1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=FMR1-interacting protein NUFIP2 {ECO:0000305|PubMed:12837692};
DE AltName: Full=82 kDa FMRP-interacting protein;
DE Short=82-FIP;
DE AltName: Full=FMRP-interacting protein 2;
GN Name=Nufip2; Synonyms=Kiaa1321;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Dendritic cell, Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FMR1.
RX PubMed=12837692; DOI=10.1093/hmg/ddg181;
RA Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F.,
RA Pastore A., Khandjian E.W., Mandel J.-L.;
RT "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting
RT protein, shows a cell cycle-dependent intracellular localization.";
RL Hum. Mol. Genet. 12:1689-1698(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-215 AND SER-649, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-213; SER-215;
RP SER-570; SER-626; SER-649 AND SER-652, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Binds RNA. {ECO:0000250|UniProtKB:Q7Z417}.
CC -!- SUBUNIT: Interacts with FMR1 (via N-terminus) (PubMed:12837692).
CC Interacts with DDX6 (By similarity). {ECO:0000250|UniProtKB:Q7Z417,
CC ECO:0000269|PubMed:12837692}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837692}. Cytoplasm
CC {ECO:0000269|PubMed:12837692}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q7Z417}. Note=Localized in both nucleus and
CC cytoplasm in most neurons. In the cortex, distributed in a diffuse way
CC in the nucleus and in the cytoplasm. Localized in the cytoplasm in
CC neurons of the dentate gyrus in the olfactive bulb, in the ependymal
CC epithelium and in the granular layer of the cerebellum. In Purkinje
CC cells, distributed in both cell compartments and in nuclear dots
CC adjacent to the nucleolus (PubMed:12837692).
CC {ECO:0000250|UniProtKB:Q7Z417, ECO:0000269|PubMed:12837692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5F2E7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F2E7-2; Sequence=VSP_019729;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122494; BAC65776.1; ALT_INIT; mRNA.
DR EMBL; AK132603; BAE21256.1; -; mRNA.
DR EMBL; AK152336; BAE31134.1; -; mRNA.
DR EMBL; AK160601; BAE35905.1; -; mRNA.
DR EMBL; AK170764; BAE42015.1; -; mRNA.
DR EMBL; AL591136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25083.1; -. [Q5F2E7-1]
DR RefSeq; NP_001019376.1; NM_001024205.2. [Q5F2E7-1]
DR RefSeq; XP_006534125.1; XM_006534062.3. [Q5F2E7-1]
DR AlphaFoldDB; Q5F2E7; -.
DR BioGRID; 212929; 32.
DR IntAct; Q5F2E7; 4.
DR MINT; Q5F2E7; -.
DR STRING; 10090.ENSMUSP00000098365; -.
DR iPTMnet; Q5F2E7; -.
DR PhosphoSitePlus; Q5F2E7; -.
DR EPD; Q5F2E7; -.
DR jPOST; Q5F2E7; -.
DR MaxQB; Q5F2E7; -.
DR PaxDb; Q5F2E7; -.
DR PeptideAtlas; Q5F2E7; -.
DR PRIDE; Q5F2E7; -.
DR ProteomicsDB; 287855; -. [Q5F2E7-1]
DR ProteomicsDB; 287856; -. [Q5F2E7-2]
DR Antibodypedia; 2837; 97 antibodies from 23 providers.
DR DNASU; 68564; -.
DR Ensembl; ENSMUST00000100802; ENSMUSP00000098365; ENSMUSG00000037857. [Q5F2E7-1]
DR Ensembl; ENSMUST00000181023; ENSMUSP00000137922; ENSMUSG00000037857. [Q5F2E7-2]
DR GeneID; 68564; -.
DR KEGG; mmu:68564; -.
DR UCSC; uc007khd.2; mouse. [Q5F2E7-1]
DR CTD; 57532; -.
DR MGI; MGI:1915814; Nufip2.
DR VEuPathDB; HostDB:ENSMUSG00000037857; -.
DR eggNOG; ENOG502QPMD; Eukaryota.
DR GeneTree; ENSGT00440000038328; -.
DR HOGENOM; CLU_020745_0_0_1; -.
DR InParanoid; Q5F2E7; -.
DR OMA; NEQKGNR; -.
DR OrthoDB; 331657at2759; -.
DR PhylomeDB; Q5F2E7; -.
DR TreeFam; TF332832; -.
DR BioGRID-ORCS; 68564; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Nufip2; mouse.
DR PRO; PR:Q5F2E7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5F2E7; protein.
DR Bgee; ENSMUSG00000037857; Expressed in manus and 218 other tissues.
DR Genevisible; Q5F2E7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC.
DR GO; GO:0042788; C:polysomal ribosome; ISS:HGNC.
DR GO; GO:0003723; F:RNA binding; ISS:HGNC.
DR InterPro; IPR032747; NUFIP2.
DR PANTHER; PTHR28333; PTHR28333; 1.
DR Pfam; PF15293; NUFIP2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..692
FT /note="FMR1-interacting protein NUFIP2"
FT /id="PRO_0000245522"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..56
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT VAR_SEQ 676..692
FT /note="DPKRIITYNEAMDSPDQ -> VFCLCVYMYTYVHHVMSLHGRERTLDPLELA
FT LHWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019729"
FT CONFLICT 52
FT /note="Missing (in Ref. 2; BAE42015)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="Q -> R (in Ref. 2; BAE42015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 75657 MW; 3E295AC111814564 CRC64;
MEEKPGQPQP QHHHSHHHPH HHPQQQQQQQ SHHHHHYYFY NHSHNHHHHH HHQQPHQYLQ
HGAEGSPKAQ PKPLKHEQKH TLQQHQETPK KKTGYGEING NAGEREISLK SLSSDEATNP
ISRVLNGNQQ VVETSLKQTV KTSTFGKAGI KTKNFIQKNS MDKKNGKSYE NKSGETQAVD
KTDTIAIPNG VITSSSGYIT NGYMSKGADN DGSGSESGYT TPKKRKARRN SAKGCENLNL
VQDKIMQETS VPALKQGLET LKPDYSEQKG MRVDGSKPIW KYETGPGGTS RGKPAMGDVL
RKSSDIKPGL SSKKFDDRPK GKHASAAASK EDSWTLFKPP PVFPVDNSSA KIVPKISYAS
KVKENLNKTV QNSSVSPSSS SSSSSTGETQ TQSSSRLSQV PMSALKSVTS ASFSNGPVLA
GTDGSVYPSG GQPLLTTAAN TLTPISTGTD SVLQDMSLAS AAVEQIKSSL FIYPSNMQTV
LLSAQVDLPS QTDQQNLGDI FQNQWGLSFI NEPSAGPETV IGKSSDHKVM EVTFQGEYPA
TLVSQGAEII PSGTEHPVFP KAYELEKRTS PQVLGHILKP GTTESGALSL DPSHIGDLQK
ADTSSQGALV FLSKDYEIEN QNPLASPTNT LLGSAKEQRY QRGLERNDSW GSFDLRAAIV
YHTKEMESIW NLQKQDPKRI ITYNEAMDSP DQ
