NUP98_RAT
ID NUP98_RAT Reviewed; 1816 AA.
AC P49793; D3ZMW4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nuclear pore complex protein Nup98-Nup96;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup98;
DE AltName: Full=98 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup98;
DE Short=Nup98;
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup96;
DE AltName: Full=96 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup96;
DE Short=Nup96;
GN Name=Nup98;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7736573; DOI=10.1016/0092-8674(95)90331-3;
RA Radu A., Moore M.S., Blobel G.;
RT "The peptide repeat domain of nucleoporin Nup98 functions as a docking site
RT in transport across the nuclear pore complex.";
RL Cell 81:215-222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=10087256; DOI=10.1083/jcb.144.6.1097;
RA Fontoura B.M.A., Blobel G., Matunis M.J.;
RT "A conserved biogenesis pathway for nucleoporins: proteolytic processing of
RT a 186-kilodalton precursor generates Nup98 and the novel nucleoporin,
RT Nup96.";
RL J. Cell Biol. 144:1097-1112(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-653; SER-888 AND
RP SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. Involved in the bidirectional transport across the
CC NPC. May anchor NUP153 and TPR to the NPC.
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. NUP98 and NUP96 are involved in the bidirectional
CC transport across the NPC. May anchor NUP153 and TPR to the NPC. In
CC cooperation with DHX9, plays a role in transcription and alternative
CC splicing activation of a subset of genes. Involved in the localization
CC of DHX9 in discrete intranuclear foci (GLFG-body).
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Interacts directly
CC with NUP96. Part of the Nup160 subcomplex in the nuclear pore which is
CC composed of NUP160, NUP133, NUP107 and NUP96; this complex plays a role
CC in RNA export and in tethering NUP98 and NUP153 to the nucleus.
CC Interacts with RAE1. Does not interact with TPR. Interacts directly
CC with NUP88 and NUP214, subunits of the cytoplasmic filaments of the
CC NPC. Interacts (via N-terminus) with DHX9 (via DRBM, OB-fold and RGG
CC domains); this interaction occurs in a RNA-dependent manner and
CC stimulates DHX9-mediated ATPase activity.
CC {ECO:0000250|UniProtKB:P52948, ECO:0000250|UniProtKB:Q6PFD9}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10087256,
CC ECO:0000269|PubMed:11839768}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10087256}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10087256}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10087256}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10087256}. Note=Localized to the nucleoplasmic side
CC of the nuclear pore complex (NPC), at or near the nucleoplasmic basket
CC (PubMed:10087256). Dissociates from the dissasembled NPC structure
CC early during prophase of mitosis (By similarity). Colocalizes with
CC NUP153 to the nuclear basket of NPC (By similarity). Colocalizes with
CC TPR to the nuclear basket of NPC (PubMed:10087256, PubMed:11839768).
CC Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-
CC body) (By similarity). Remains localized to the nuclear membrane after
CC poliovirus (PV) infection (By similarity).
CC {ECO:0000250|UniProtKB:P52948, ECO:0000269|PubMed:10087256,
CC ECO:0000269|PubMed:11839768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Nup98-Nup96 precursor;
CC IsoId=P49793-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49793-2; Sequence=VSP_040702, VSP_040703;
CC -!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains have a direct
CC role in the transport (By similarity). {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Isoform 1 is autoproteolytically cleaved to yield Nup98 and Nup96
CC or Nup98 only, respectively. Cleaved Nup98 is necessary for the
CC targeting of Nup98 to the nuclear pore and the interaction with Nup96.
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; CH473956; EDM18207.1; -; Genomic_DNA.
DR EMBL; L39991; AAC42054.1; -; mRNA.
DR PIR; A56517; A56517.
DR RefSeq; NP_112336.2; NM_031074.2. [P49793-1]
DR RefSeq; XP_006229954.1; XM_006229892.3. [P49793-1]
DR RefSeq; XP_017445261.1; XM_017589772.1. [P49793-1]
DR AlphaFoldDB; P49793; -.
DR SMR; P49793; -.
DR BioGRID; 249610; 1.
DR CORUM; P49793; -.
DR STRING; 10116.ENSRNOP00000027575; -.
DR MEROPS; S59.001; -.
DR iPTMnet; P49793; -.
DR PhosphoSitePlus; P49793; -.
DR jPOST; P49793; -.
DR PaxDb; P49793; -.
DR PRIDE; P49793; -.
DR Ensembl; ENSRNOT00000027575; ENSRNOP00000027575; ENSRNOG00000020347. [P49793-1]
DR GeneID; 81738; -.
DR KEGG; rno:81738; -.
DR UCSC; RGD:71033; rat. [P49793-1]
DR CTD; 4928; -.
DR RGD; 71033; Nup98.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00550000074799; -.
DR HOGENOM; CLU_002330_1_0_1; -.
DR InParanoid; P49793; -.
DR OMA; KGFEWPY; -.
DR OrthoDB; 93359at2759; -.
DR PhylomeDB; P49793; -.
DR TreeFam; TF343335; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:P49793; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000020347; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; P49793; baseline and differential.
DR Genevisible; P49793; RN.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR InterPro; IPR021967; Nup98_C.
DR PANTHER; PTHR23198; PTHR23198; 1.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 1.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autocatalytic cleavage;
KW Direct protein sequencing; Hydrolase; Isopeptide bond; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protease;
KW Protein transport; Reference proteome; Repeat; Serine protease;
KW Translocation; Transport; Ubl conjugation.
FT CHAIN 1..880
FT /note="Nuclear pore complex protein Nup98"
FT /id="PRO_0000204890"
FT CHAIN 881..1816
FT /note="Nuclear pore complex protein Nup96"
FT /id="PRO_0000405578"
FT DOMAIN 738..880
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..156
FT /note="FG repeats 1"
FT REGION 157..213
FT /note="GLEBS; interaction with RAE1"
FT /evidence="ECO:0000250"
FT REGION 214..480
FT /note="FG repeats 2"
FT REGION 512..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 881
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT SITE 880..881
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 603
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD9"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD9"
FT MOD_RES 1069
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD9"
FT MOD_RES 1771
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD9"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT CROSSLNK 603
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT CROSSLNK 665
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT VAR_SEQ 930..938
FT /note="PQSQSPEVE -> TSGREGQRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7736573"
FT /id="VSP_040702"
FT VAR_SEQ 939..1816
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7736573"
FT /id="VSP_040703"
FT CONFLICT 11
FT /note="Missing (in Ref. 1; AAC42054)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="N -> S (in Ref. 1; AAC42054)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="F -> L (in Ref. 1; AAC42054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1816 AA; 197283 MW; 70A7D8E23D542B42 CRC64;
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG
GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTANTGTS LFSSQNNAFA QNKPTGFGNF
GTSTSSGGLF GTTNTTSNPF GNTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL
FSSSTTNSAF SYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTPNTGF
SFGNTSTLGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQPNTGFGAV
GSTLFGNNKL TTFGTSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNNSGSSIF
GSKPAAGTLG TGLGTGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTSTAILGFG
APQAPVALTD PNASAAQQAV LQQHLNSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA
QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
VLKNLNNSNL FSPVNHDSED LASPSEYPEN GERFSFLSKP VDENHQQDGD DDSLVSRFYT
NPIAKPIPQT PESAGNKNNS SSNVEDTFIA LNMRAALRNG LEGSSEETSF HDESLQDDRD
EIENSAFQIH PAGIVLTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD
VNLTNLNLDD IVHIRRKEVI VYVDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPPKTT
SKKLKTAPLP PAGQATTFQM TLNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVPD
SVLEESVPED QEPVSASTQI ASSLGINPHV LQIMKASLLV DEEDVDAMEQ RFGHFPSRGD
TAQEICSPRL PISASHSSKS RSIVGGLLQS KFASGTFLSP SASVQECRTP RTSSLMNVPS
TSPWSVPLPL ATVFTVPSPA PEVPLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR
SFRVGWGPNW TLANSGEQLH GSHELENHQV AESMEYGFLP NPVAVKSLSE SPFKVHLEKL
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHGYAD WVKKSPRDLL
ELPIVKHWSL TWTLCEALWG HLKELDSQLD EPSEYIQTLE RRRAFSRWLS HTAAPQIEEE
VSLTRRDSPI EAVFSYLTGS RISEACCLAQ QSGDHRLALL LSQLVGSQSV RELLTMQLAD
WHQLQADSFI HDERLRIFAL LAGKPVWQLS EQKQINVCSQ LDWKRTLAIH LWYLLPPTAS
ISRALSMYEE AFQNTCEGDK YACPPLPSYL EGSGCVVEEE KDPQRPLQDV CFHLLKLYSD
RHYGLNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS YAGQLESEGL
WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK ETFLTQKLCV PAEWIHEAKA
VRAHMESNKH LEALYLFKAG HWNRCHKLVV RHLASDAIIN ENYDYLKGFL EDLAPPERSS
LIQDWETSGL VYLDYIRVIE MLHRIQQVDC SGYELEHLHT KVTSLCNRIE QIPCYNAKDR
LAQSDMAKRV ANLLRVVLSL QHTPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
RGLTQSYLRE LTVGSQ
