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GTPB2_HUMAN
ID   GTPB2_HUMAN             Reviewed;         602 AA.
AC   Q9BX10; Q5T7E8; Q8ND84; Q8TAH7; Q8WUA5; Q9HCS9; Q9NRU4; Q9NX60;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=GTP-binding protein 2;
GN   Name=GTPBP2 {ECO:0000312|EMBL:CAC36269.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAB12431.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   PubMed=11054535; DOI=10.1016/s0378-1119(00)00346-2;
RA   Watanabe M., Yoshida K., Hida M., Kato H., Uchida K., Yamaguchi R.,
RA   Tateyama S., Sugano S.;
RT   "Cloning, expression analysis, and chromosomal mapping of GTPBP2, a novel
RT   member of the G protein family.";
RL   Gene 256:51-58(2000).
RN   [2] {ECO:0000312|EMBL:CAC36269.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAA91160.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAH64968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon {ECO:0000312|EMBL:AAH20980.2},
RC   Ovary {ECO:0000312|EMBL:AAH28347.2}, and
RC   Skin {ECO:0000312|EMBL:AAH64968.1};
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   [5] {ECO:0000305, ECO:0000312|EMBL:AAF78884.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 41-602 (ISOFORM 1), AND INDUCTION.
RX   PubMed=10833435; DOI=10.1006/bbrc.2000.2763;
RA   Kudo H., Senju S., Mitsuya H., Nishimura Y.;
RT   "Mouse and human GTPBP2, newly identified members of the GP-1 family of
RT   GTPase.";
RL   Biochem. Biophys. Res. Commun. 272:456-465(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-602 (ISOFORM 1).
RC   TISSUE=Testis;
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   [7]
RP   INVOLVEMENT IN JABELS.
RX   PubMed=26675814; DOI=10.1016/j.neurobiolaging.2015.10.034;
RA   Jaberi E., Rohani M., Shahidi G.A., Nafissi S., Arefian E., Soleimani M.,
RA   Rasooli P., Ahmadieh H., Daftarian N., KaramiNejadRanjbar M., Klotzle B.,
RA   Fan J.B., Turk C., Steemers F., Elahi E.;
RT   "Identification of mutation in GTPBP2 in patients of a family with
RT   neurodegeneration accompanied by iron deposition in the brain.";
RL   Neurobiol. Aging 38:216.E11-216.E18(2016).
RN   [8]
RP   INVOLVEMENT IN JABELS, AND VARIANTS JABELS 144-ARG--PHE-602 DEL;
RP   407-GLN--PHE-602 DEL AND 470-ARG--PHE-602 DEL.
RX   PubMed=29449720; DOI=10.1038/s41431-018-0097-3;
RA   Bertoli-Avella A.M., Garcia-Aznar J.M., Brandau O., Al-Hakami F.,
RA   Yueksel Z., Marais A., Gruening N.M., Abbasi Moheb L., Paknia O.,
RA   Alshaikh N., Alameer S., Marafi M.J., Al-Mulla F., Al-Sannaa N., Rolfs A.,
RA   Bauer P.;
RT   "Biallelic inactivating variants in the GTPBP2 gene cause a
RT   neurodevelopmental disorder with severe intellectual disability.";
RL   Eur. J. Hum. Genet. 26:592-598(2018).
CC   -!- INTERACTION:
CC       Q9BX10; P49760: CLK2; NbExp=3; IntAct=EBI-6115579, EBI-750020;
CC       Q9BX10; Q9UHW5: GPN3; NbExp=3; IntAct=EBI-6115579, EBI-395491;
CC       Q9BX10; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-6115579, EBI-6115579;
CC       Q9BX10; O60341: KDM1A; NbExp=2; IntAct=EBI-6115579, EBI-710124;
CC       Q9BX10; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-6115579, EBI-398874;
CC       Q9BX10; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-6115579, EBI-79165;
CC       Q9BX10; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6115579, EBI-742388;
CC       Q9BX10; O14744: PRMT5; NbExp=2; IntAct=EBI-6115579, EBI-351098;
CC       Q9BX10; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-6115579, EBI-912440;
CC       Q9BX10; P20618: PSMB1; NbExp=3; IntAct=EBI-6115579, EBI-372273;
CC       Q9BX10; P08621: SNRNP70; NbExp=3; IntAct=EBI-6115579, EBI-1049228;
CC       Q9BX10; O43463: SUV39H1; NbExp=2; IntAct=EBI-6115579, EBI-349968;
CC       Q9BX10; Q99757: TXN2; NbExp=5; IntAct=EBI-6115579, EBI-2932492;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1 {ECO:0000269|PubMed:10833435};
CC         IsoId=Q9BX10-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:11054535};
CC         IsoId=Q9BX10-2; Sequence=VSP_052154;
CC       Name=3 {ECO:0000269|PubMed:14702039};
CC         IsoId=Q9BX10-3; Sequence=VSP_052154, VSP_052156;
CC       Name=4 {ECO:0000269|PubMed:14574404};
CC         IsoId=Q9BX10-4; Sequence=VSP_052155;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, and
CC       testis. Expressed at lower levels in brain, lung, kidney, and ovary.
CC       {ECO:0000269|PubMed:11054535}.
CC   -!- INDUCTION: Up-regulated by IFNG/IFN-gamma in human monocytic cell line
CC       THP-1. {ECO:0000269|PubMed:10833435}.
CC   -!- DISEASE: Jaberi-Elahi syndrome (JABELS) [MIM:617988]: An autosomal
CC       recessive disorder characterized by developmental delay and
CC       intellectual disability. Additional variable features include ataxic
CC       gait and abnormal movements, visual impairment, microcephaly, abnormal
CC       foot or hand posturing, kyphoscoliosis, dysmorphic facial features or
CC       seizures. Brain imaging typically shows cerebellar atrophy and
CC       hypoplasia of the corpus callosum. {ECO:0000269|PubMed:26675814,
CC       ECO:0000269|PubMed:29449720}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. GTPBP1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD38999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB024574; BAB12431.1; -; mRNA.
DR   EMBL; AL353602; CAC36269.1; -; Genomic_DNA.
DR   EMBL; AL353602; CAI12785.1; -; Genomic_DNA.
DR   EMBL; AK000430; BAA91160.1; -; mRNA.
DR   EMBL; BC020980; AAH20980.2; -; mRNA.
DR   EMBL; BC028347; AAH28347.2; -; mRNA.
DR   EMBL; BC064968; AAH64968.1; -; mRNA.
DR   EMBL; AF168990; AAF78884.1; -; mRNA.
DR   EMBL; AL834331; CAD38999.1; ALT_INIT; mRNA.
DR   CCDS; CCDS4903.1; -. [Q9BX10-1]
DR   CCDS; CCDS69124.1; -. [Q9BX10-2]
DR   PIR; PC7084; PC7084.
DR   RefSeq; NP_001273145.1; NM_001286216.1. [Q9BX10-2]
DR   RefSeq; NP_061969.3; NM_019096.4. [Q9BX10-1]
DR   AlphaFoldDB; Q9BX10; -.
DR   SMR; Q9BX10; -.
DR   BioGRID; 120097; 54.
DR   IntAct; Q9BX10; 33.
DR   MINT; Q9BX10; -.
DR   STRING; 9606.ENSP00000303997; -.
DR   iPTMnet; Q9BX10; -.
DR   PhosphoSitePlus; Q9BX10; -.
DR   BioMuta; GTPBP2; -.
DR   DMDM; 74752415; -.
DR   EPD; Q9BX10; -.
DR   jPOST; Q9BX10; -.
DR   MassIVE; Q9BX10; -.
DR   MaxQB; Q9BX10; -.
DR   PaxDb; Q9BX10; -.
DR   PeptideAtlas; Q9BX10; -.
DR   PRIDE; Q9BX10; -.
DR   ProteomicsDB; 79339; -. [Q9BX10-1]
DR   ProteomicsDB; 79340; -. [Q9BX10-2]
DR   ProteomicsDB; 79341; -. [Q9BX10-3]
DR   ProteomicsDB; 79342; -. [Q9BX10-4]
DR   Antibodypedia; 30525; 187 antibodies from 27 providers.
DR   DNASU; 54676; -.
DR   Ensembl; ENST00000307114.11; ENSP00000304893.7; ENSG00000172432.19. [Q9BX10-2]
DR   Ensembl; ENST00000307126.10; ENSP00000303997.5; ENSG00000172432.19. [Q9BX10-1]
DR   GeneID; 54676; -.
DR   KEGG; hsa:54676; -.
DR   MANE-Select; ENST00000307126.10; ENSP00000303997.5; NM_019096.5; NP_061969.3.
DR   UCSC; uc003ovs.5; human. [Q9BX10-1]
DR   CTD; 54676; -.
DR   DisGeNET; 54676; -.
DR   GeneCards; GTPBP2; -.
DR   HGNC; HGNC:4670; GTPBP2.
DR   HPA; ENSG00000172432; Low tissue specificity.
DR   MalaCards; GTPBP2; -.
DR   MIM; 607434; gene.
DR   MIM; 617988; phenotype.
DR   neXtProt; NX_Q9BX10; -.
DR   OpenTargets; ENSG00000172432; -.
DR   PharmGKB; PA29058; -.
DR   VEuPathDB; HostDB:ENSG00000172432; -.
DR   eggNOG; KOG1143; Eukaryota.
DR   GeneTree; ENSGT00940000155636; -.
DR   HOGENOM; CLU_012821_1_1_1; -.
DR   InParanoid; Q9BX10; -.
DR   OMA; DYACLVI; -.
DR   PhylomeDB; Q9BX10; -.
DR   TreeFam; TF350446; -.
DR   PathwayCommons; Q9BX10; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   SignaLink; Q9BX10; -.
DR   BioGRID-ORCS; 54676; 30 hits in 1084 CRISPR screens.
DR   ChiTaRS; GTPBP2; human.
DR   GenomeRNAi; 54676; -.
DR   Pharos; Q9BX10; Tbio.
DR   PRO; PR:Q9BX10; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9BX10; protein.
DR   Bgee; ENSG00000172432; Expressed in lower esophagus mucosa and 169 other tissues.
DR   ExpressionAtlas; Q9BX10; baseline and differential.
DR   Genevisible; Q9BX10; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd04165; GTPBP1_like; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR035531; GTPBP1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; GTP-binding;
KW   Intellectual disability; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..602
FT                   /note="GTP-binding protein 2"
FT                   /id="PRO_0000248500"
FT   DOMAIN          170..398
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          16..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O00178"
FT   BINDING         260..264
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O00178"
FT   BINDING         316..319
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O00178"
FT   VAR_SEQ         1..88
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11054535,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_052154"
FT   VAR_SEQ         72..79
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14574404"
FT                   /id="VSP_052155"
FT   VAR_SEQ         101..370
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_052156"
FT   VARIANT         144..602
FT                   /note="Missing (in JABELS; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:29449720"
FT                   /id="VAR_080975"
FT   VARIANT         407..602
FT                   /note="Missing (in JABELS; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:29449720"
FT                   /id="VAR_080976"
FT   VARIANT         470..602
FT                   /note="Missing (in JABELS; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:29449720"
FT                   /id="VAR_080977"
FT   CONFLICT        42..43
FT                   /note="KK -> TR (in Ref. 5; AAF78884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="G -> E (in Ref. 1; BAB12431)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   602 AA;  65768 MW;  BA9CA08F3797A7B1 CRC64;
     MDSRVSELFG GCCRPGGGPA VGGTLKARGA GSSSGCGGPK GKKKNGRNRG GKANNPPYLP
     PEAEDGNIEY KLKLVNPSQY RFEHLVTQMK WRLQEGRGEA VYQIGVEDNG LLVGLAEEEM
     RASLKTLHRM AEKVGADITV LREREVDYDS DMPRKITEVL VRKVPDNQQF LDLRVAVLGN
     VDSGKSTLLG VLTQGELDNG RGRARLNLFR HLHEIQSGRT SSISFEILGF NSKGEVVNYS
     DSRTAEEICE SSSKMITFID LAGHHKYLHT TIFGLTSYCP DCALLLVSAN TGIAGTTREH
     LGLALALKVP FFIVVSKIDL CAKTTVERTV RQLERVLKQP GCHKVPMLVT SEDDAVTAAQ
     QFAQSPNVTP IFTLSSVSGE SLDLLKVFLN ILPPLTNSKE QEELMQQLTE FQVDEIYTVP
     EVGTVVGGTL SSGICREGDQ LVVGPTDDGC FLELRVCSIQ RNRSACRVLR AGQAATLALG
     DFDRALLRKG MVMVSPEMNP TICSVFEAEI VLLFHATTFR RGFQVTVHVG NVRQTAVVEK
     IHAKDKLRTG EKAVVRFRFL KHPEYLKVGA KLLFREGVTK GIGHVTDVQA ITAGEAQANM
     GF
 
 
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