SMG5_HUMAN
ID SMG5_HUMAN Reviewed; 1016 AA.
AC Q9UPR3; D3DVB7; Q5QJE7; Q659C7; Q8IXC0; Q8IY09; Q96IJ7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG5 {ECO:0000312|HGNC:HGNC:24644};
DE AltName: Full=EST1-like protein B {ECO:0000303|PubMed:12699629};
DE AltName: Full=LPTS-RP1 {ECO:0000303|Ref.3};
DE AltName: Full=LPTS-interacting protein {ECO:0000303|PubMed:12699629};
DE AltName: Full=SMG-5 homolog {ECO:0000303|PubMed:14636577};
DE Short=hSMG-5 {ECO:0000303|PubMed:14636577};
GN Name=SMG5 {ECO:0000312|HGNC:HGNC:24644};
GN Synonyms=EST1B {ECO:0000312|HGNC:HGNC:24644},
GN KIAA1089 {ECO:0000312|HGNC:HGNC:24644};
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], MUTAGENESIS OF ASP-860, INTERACTION WITH
RP PPP2CA; SMG7 AND SMG1, IDENTIFICATION IN COMPLEXES WITH SMG7; PPP2CA AND
RP PHOSPHORYLATED RENT1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=14636577; DOI=10.1016/s1097-2765(03)00443-x;
RA Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A.,
RA Hachiya T., Hentze M.W., Anderson P., Ohno S.;
RT "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes
RT containing hSMG-5 and hSMG-7.";
RL Mol. Cell 12:1187-1200(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TERT, AND TISSUE SPECIFICITY.
RX PubMed=12699629; DOI=10.1016/s0960-9822(03)00210-0;
RA Snow B.E., Erdmann N., Cruickshank J., Goldman H., Gill R.M.,
RA Robinson M.O., Harrington L.;
RT "Functional conservation of the telomerase protein Est1p in humans.";
RL Curr. Biol. 13:698-704(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Song H., Zhao M., Li T.;
RT "LPTS-RP1, a LPTS interacting protein.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-1004.
RC TISSUE=Muscle, and Testis;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 584-1016.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP ASSOCIATION WITH CYTOPLASMIC MRNA DECAY BODIES.
RX PubMed=15546618; DOI=10.1016/j.molcel.2004.10.013;
RA Unterholzner L., Izaurralde E.;
RT "SMG7 acts as a molecular link between mRNA surveillance and mRNA decay.";
RL Mol. Cell 16:587-596(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 853-1016, AND FUNCTION.
RX PubMed=17053788; DOI=10.1038/sj.emboj.7601377;
RA Glavan F., Behm-Ansmant I., Izaurralde E., Conti E.;
RT "Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within
RT the mRNA surveillance complex.";
RL EMBO J. 25:5117-5125(2006).
CC -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Does not have
CC RNase activity by itself. Promotes dephosphorylation of UPF1. Together
CC with SMG7 is thought to provide a link to the mRNA degradation
CC machinery involving exonucleolytic pathways, and to serve as an adapter
CC for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1
CC dephosphorylation. Necessary for TERT activity.
CC {ECO:0000269|PubMed:17053788}.
CC -!- SUBUNIT: Interacts with TERT, PPP2CA and SMG1. Part of a complex that
CC contains SMG1, SMG5, SMG7, PPP2CA, a short isoform of UPF3A (isoform
CC UPF3AS, but not isoform UPF3AL) and phosphorylated UPF1. Not detected
CC in complexes that contain unphosphorylated UPF1.
CC {ECO:0000269|PubMed:12699629, ECO:0000269|PubMed:14636577}.
CC -!- INTERACTION:
CC Q9UPR3; Q92540: SMG7; NbExp=5; IntAct=EBI-3400861, EBI-719830;
CC Q9UPR3; Q92900-2: UPF1; NbExp=2; IntAct=EBI-3400861, EBI-373492;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14636577}. Nucleus
CC {ECO:0000269|PubMed:14636577}. Note=Predominantly cytoplasmic, and
CC nuclear. Shuttles between nucleus and cytoplasm. Detected in
CC cytoplasmic mRNA decay bodies.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12699629,
CC ECO:0000269|PubMed:14636577}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83041.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB085691; BAC53623.1; -; mRNA.
DR EMBL; AY168922; AAO17582.1; -; mRNA.
DR EMBL; AY336728; AAQ84301.1; -; mRNA.
DR EMBL; AB029012; BAA83041.2; ALT_INIT; mRNA.
DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52973.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52974.1; -; Genomic_DNA.
DR EMBL; BC007453; AAH07453.2; -; mRNA.
DR EMBL; BC038296; AAH38296.1; -; mRNA.
DR EMBL; AL137738; CAH56374.1; -; mRNA.
DR CCDS; CCDS1137.1; -.
DR RefSeq; NP_056142.2; NM_015327.2.
DR PDB; 2HWY; X-ray; 2.75 A; A/B=853-1016.
DR PDBsum; 2HWY; -.
DR AlphaFoldDB; Q9UPR3; -.
DR SMR; Q9UPR3; -.
DR BioGRID; 116957; 74.
DR IntAct; Q9UPR3; 14.
DR MINT; Q9UPR3; -.
DR STRING; 9606.ENSP00000355261; -.
DR iPTMnet; Q9UPR3; -.
DR PhosphoSitePlus; Q9UPR3; -.
DR BioMuta; SMG5; -.
DR DMDM; 84029494; -.
DR EPD; Q9UPR3; -.
DR jPOST; Q9UPR3; -.
DR MassIVE; Q9UPR3; -.
DR MaxQB; Q9UPR3; -.
DR PaxDb; Q9UPR3; -.
DR PeptideAtlas; Q9UPR3; -.
DR PRIDE; Q9UPR3; -.
DR ProteomicsDB; 85426; -.
DR Antibodypedia; 34209; 111 antibodies from 23 providers.
DR DNASU; 23381; -.
DR Ensembl; ENST00000361813.5; ENSP00000355261.5; ENSG00000198952.8.
DR GeneID; 23381; -.
DR KEGG; hsa:23381; -.
DR MANE-Select; ENST00000361813.5; ENSP00000355261.5; NM_015327.3; NP_056142.2.
DR UCSC; uc001foc.5; human.
DR CTD; 23381; -.
DR DisGeNET; 23381; -.
DR GeneCards; SMG5; -.
DR HGNC; HGNC:24644; SMG5.
DR HPA; ENSG00000198952; Low tissue specificity.
DR MIM; 610962; gene.
DR neXtProt; NX_Q9UPR3; -.
DR OpenTargets; ENSG00000198952; -.
DR PharmGKB; PA143485617; -.
DR VEuPathDB; HostDB:ENSG00000198952; -.
DR eggNOG; KOG2162; Eukaryota.
DR GeneTree; ENSGT00940000154566; -.
DR HOGENOM; CLU_011872_0_0_1; -.
DR InParanoid; Q9UPR3; -.
DR OMA; FQIIECC; -.
DR OrthoDB; 184090at2759; -.
DR PhylomeDB; Q9UPR3; -.
DR TreeFam; TF327119; -.
DR PathwayCommons; Q9UPR3; -.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q9UPR3; -.
DR BioGRID-ORCS; 23381; 617 hits in 1093 CRISPR screens.
DR ChiTaRS; SMG5; human.
DR EvolutionaryTrace; Q9UPR3; -.
DR GeneWiki; SMG5; -.
DR GenomeRNAi; 23381; -.
DR Pharos; Q9UPR3; Tbio.
DR PRO; PR:Q9UPR3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UPR3; protein.
DR Bgee; ENSG00000198952; Expressed in apex of heart and 198 other tissues.
DR Genevisible; Q9UPR3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:HGNC-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:HGNC-UCL.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0035303; P:regulation of dephosphorylation; IMP:HGNC-UCL.
DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; TAS:BHF-UCL.
DR DisProt; DP01878; -.
DR Gene3D; 1.25.40.10; -; 1.
DR IDEAL; IID00107; -.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR019458; Est1_N.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 2.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1016
FT /note="Nonsense-mediated mRNA decay factor SMG5"
FT /id="PRO_0000076322"
FT DOMAIN 872..995
FT /note="PINc"
FT REGION 408..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 798..841
FT /evidence="ECO:0000255"
FT COMPBIAS 418..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPY2"
FT VARIANT 1004
FT /note="N -> D (in dbSNP:rs17853821)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030828"
FT MUTAGEN 860
FT /note="D->A: Abolishes stimulation of RENT1
FT dephosphorylation."
FT /evidence="ECO:0000269|PubMed:14636577"
FT CONFLICT 372
FT /note="A -> S (in Ref. 3; AAQ84301)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="T -> A (in Ref. 3; AAQ84301)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="G -> R (in Ref. 3; AAQ84301)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="K -> KK (in Ref. 9; CAH56374)"
FT /evidence="ECO:0000305"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 861..866
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 868..877
FT /evidence="ECO:0007829|PDB:2HWY"
FT STRAND 878..884
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 886..895
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 900..915
FT /evidence="ECO:0007829|PDB:2HWY"
FT STRAND 918..922
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 946..955
FT /evidence="ECO:0007829|PDB:2HWY"
FT STRAND 977..980
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 992..996
FT /evidence="ECO:0007829|PDB:2HWY"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:2HWY"
FT HELIX 1005..1011
FT /evidence="ECO:0007829|PDB:2HWY"
SQ SEQUENCE 1016 AA; 113928 MW; B6F8F9B53CF42195 CRC64;
MSQGPPTGES SEPEAKVLHT KRLYRAVVEA VHRLDLILCN KTAYQEVFKP ENISLRNKLR
ELCVKLMFLH PVDYGRKAEE LLWRKVYYEV IQLIKTNKKH IHSRSTLECA YRTHLVAGIG
FYQHLLLYIQ SHYQLELQCC IDWTHVTDPL IGCKKPVSAS GKEMDWAQMA CHRCLVYLGD
LSRYQNELAG VDTELLAERF YYQALSVAPQ IGMPFNQLGT LAGSKYYNVE AMYCYLRCIQ
SEVSFEGAYG NLKRLYDKAA KMYHQLKKCE TRKLSPGKKR CKDIKRLLVN FMYLQSLLQP
KSSSVDSELT SLCQSVLEDF NLCLFYLPSS PNLSLASEDE EEYESGYAFL PDLLIFQMVI
ICLMCVHSLE RAGSKQYSAA IAFTLALFSH LVNHVNIRLQ AELEEGENPV PAFQSDGTDE
PESKEPVEKE EEPDPEPPPV TPQVGEGRKS RKFSRLSCLR RRRHPPKVGD DSDLSEGFES
DSSHDSARAS EGSDSGSDKS LEGGGTAFDA ETDSEMNSQE SRSDLEDMEE EEGTRSPTLE
PPRGRSEAPD SLNGPLGPSE ASIASNLQAM STQMFQTKRC FRLAPTFSNL LLQPTTNPHT
SASHRPCVNG DVDKPSEPAS EEGSESEGSE SSGRSCRNER SIQEKLQVLM AEGLLPAVKV
FLDWLRTNPD LIIVCAQSSQ SLWNRLSVLL NLLPAAGELQ ESGLALCPEV QDLLEGCELP
DLPSSLLLPE DMALRNLPPL RAAHRRFNFD TDRPLLSTLE ESVVRICCIR SFGHFIARLQ
GSILQFNPEV GIFVSIAQSE QESLLQQAQA QFRMAQEEAR RNRLMRDMAQ LRLQLEVSQL
EGSLQQPKAQ SAMSPYLVPD TQALCHHLPV IRQLATSGRF IVIIPRTVID GLDLLKKEHP
GARDGIRYLE AEFKKGNRYI RCQKEVGKSF ERHKLKRQDA DAWTLYKILD SCKQLTLAQG
AGEEDPSGMV TIITGLPLDN PSVLSGPMQA ALQAAAHASV DIKNVLDFYK QWKEIG
