TBD2B_HUMAN
ID TBD2B_HUMAN Reviewed; 963 AA.
AC Q9UPU7; A7MD42; Q8N1F9; Q9NXM0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=TBC1 domain family member 2B;
GN Name=TBC1D2B; Synonyms=KIAA1055;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-914 (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-924 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-963 (ISOFORM 1).
RC TISSUE=Duodenum;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-317; SER-473 AND
RP SER-957, AND IDENTIFICATION BY MASS 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN NEDSGO, VARIANTS NEDSGO
RP 494-GLN--THR-963 DEL; 765-TYR--THR-963 DEL AND 793-LEU--THR-963 DEL, AND
RP CHARACTERIZATION OF VARIANT NEDSGO 793-LEU--THR-963 DEL.
RX PubMed=32623794; DOI=10.1002/humu.24071;
RA Harms F.L., Parthasarathy P., Zorndt D., Alawi M., Fuchs S., Halliday B.J.,
RA McKeown C., Sampaio H., Radhakrishnan N., Radhakrishnan S.K., Gorce M.,
RA Navet B., Ziegler A., Sachdev R., Robertson S.P., Nampoothiri S.,
RA Kutsche K.;
RT "Biallelic loss-of-function variants in TBC1D2B cause a neurodevelopmental
RT disorder with seizures and gingival overgrowth.";
RL Hum. Mutat. 41:1645-1661(2020).
CC -!- FUNCTION: GTPase-activating protein that plays a role in the early
CC steps of endocytosis (PubMed:32623794). {ECO:0000269|PubMed:32623794}.
CC -!- INTERACTION:
CC Q9UPU7; O95166: GABARAP; NbExp=2; IntAct=EBI-2947180, EBI-712001;
CC Q9UPU7; Q9H0R8: GABARAPL1; NbExp=5; IntAct=EBI-2947180, EBI-746969;
CC Q9UPU7; P60520: GABARAPL2; NbExp=3; IntAct=EBI-2947180, EBI-720116;
CC Q9UPU7; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-2947180, EBI-373144;
CC Q9UPU7; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-2947180, EBI-2603996;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:32623794}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPU7-2; Sequence=VSP_030669;
CC Name=3;
CC IsoId=Q9UPU7-3; Sequence=VSP_030666, VSP_030667, VSP_030668;
CC -!- DISEASE: Neurodevelopmental disorder with seizures and gingival
CC overgrowth (NEDSGO) [MIM:619323]: An autosomal recessive disorder with
CC variable clinical manifestations including delayed development,
CC hypotonia, seizures, gingival hypertrophy associated with a prominent
CC mandible or cherubism in the first years of life. Some patients have
CC early normal development followed by developmental regression.
CC Additional variable features are coarse facial features, optic atrophy,
CC sensorineural hearing loss, and ataxia. Brain imaging may show
CC cerebellar or cerebral atrophy and enlarged ventricles.
CC {ECO:0000269|PubMed:32623794}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI52466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW99190.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000173; BAA90990.1; -; mRNA.
DR EMBL; AC104758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99188.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99190.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB028978; BAA83007.1; -; mRNA.
DR EMBL; BC033712; AAH33712.1; ALT_INIT; mRNA.
DR EMBL; BC152465; AAI52466.1; ALT_INIT; mRNA.
DR CCDS; CCDS32301.2; -. [Q9UPU7-2]
DR CCDS; CCDS45314.1; -. [Q9UPU7-1]
DR RefSeq; NP_055894.6; NM_015079.5. [Q9UPU7-2]
DR RefSeq; NP_653173.1; NM_144572.1. [Q9UPU7-1]
DR AlphaFoldDB; Q9UPU7; -.
DR SMR; Q9UPU7; -.
DR BioGRID; 116729; 86.
DR IntAct; Q9UPU7; 22.
DR STRING; 9606.ENSP00000300584; -.
DR iPTMnet; Q9UPU7; -.
DR PhosphoSitePlus; Q9UPU7; -.
DR BioMuta; TBC1D2B; -.
DR DMDM; 166227884; -.
DR EPD; Q9UPU7; -.
DR jPOST; Q9UPU7; -.
DR MassIVE; Q9UPU7; -.
DR MaxQB; Q9UPU7; -.
DR PaxDb; Q9UPU7; -.
DR PeptideAtlas; Q9UPU7; -.
DR PRIDE; Q9UPU7; -.
DR ProteomicsDB; 85447; -. [Q9UPU7-1]
DR ProteomicsDB; 85448; -. [Q9UPU7-2]
DR ProteomicsDB; 85449; -. [Q9UPU7-3]
DR Antibodypedia; 56232; 37 antibodies from 11 providers.
DR DNASU; 23102; -.
DR Ensembl; ENST00000300584.8; ENSP00000300584.3; ENSG00000167202.12. [Q9UPU7-1]
DR Ensembl; ENST00000409931.7; ENSP00000387165.3; ENSG00000167202.12. [Q9UPU7-2]
DR GeneID; 23102; -.
DR KEGG; hsa:23102; -.
DR MANE-Select; ENST00000300584.8; ENSP00000300584.3; NM_144572.2; NP_653173.1.
DR UCSC; uc002bcy.4; human. [Q9UPU7-1]
DR CTD; 23102; -.
DR DisGeNET; 23102; -.
DR GeneCards; TBC1D2B; -.
DR HGNC; HGNC:29183; TBC1D2B.
DR HPA; ENSG00000167202; Low tissue specificity.
DR MIM; 619152; gene.
DR MIM; 619323; phenotype.
DR neXtProt; NX_Q9UPU7; -.
DR OpenTargets; ENSG00000167202; -.
DR PharmGKB; PA142670832; -.
DR VEuPathDB; HostDB:ENSG00000167202; -.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000157737; -.
DR HOGENOM; CLU_011278_0_0_1; -.
DR InParanoid; Q9UPU7; -.
DR OMA; EQAFFKP; -.
DR PhylomeDB; Q9UPU7; -.
DR TreeFam; TF317336; -.
DR PathwayCommons; Q9UPU7; -.
DR SignaLink; Q9UPU7; -.
DR BioGRID-ORCS; 23102; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; TBC1D2B; human.
DR GenomeRNAi; 23102; -.
DR Pharos; Q9UPU7; Tdark.
DR PRO; PR:Q9UPU7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UPU7; protein.
DR Bgee; ENSG00000167202; Expressed in decidua and 190 other tissues.
DR ExpressionAtlas; Q9UPU7; baseline and differential.
DR Genevisible; Q9UPU7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Endosome;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..963
FT /note="TBC1 domain family member 2B"
FT /id="PRO_0000315713"
FT DOMAIN 34..139
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 662..856
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 337..535
FT /evidence="ECO:0000255"
FT COMPBIAS 314..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030666"
FT VAR_SEQ 860
FT /note="I -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030667"
FT VAR_SEQ 861..963
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030668"
FT VAR_SEQ 900..963
FT /note="KLISISFGDLNPFPLRQIRNRRAYHLEKVRLELTELEAIREDFLRERDTSPD
FT KGELVSDEEEDT -> SGTDAPTTWRKSGWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030669"
FT VARIANT 494..963
FT /note="Missing (in NEDSGO)"
FT /evidence="ECO:0000269|PubMed:32623794"
FT /id="VAR_085821"
FT VARIANT 765..963
FT /note="Missing (in NEDSGO)"
FT /evidence="ECO:0000269|PubMed:32623794"
FT /id="VAR_085822"
FT VARIANT 793..963
FT /note="Missing (in NEDSGO; severely reduced protein
FT abundance due to nonsense-mediated decay of mutant
FT transcripts in homozygous patient cells)"
FT /evidence="ECO:0000269|PubMed:32623794"
FT /id="VAR_085823"
SQ SEQUENCE 963 AA; 109880 MW; 1BC9B8FCA5BC2EEF CRC64;
MPGAGARAEE GGGGGEGAAQ GAAAEPGAGP AREPARLCGY LQKLSGKGPL RGYRSRWFVF
DARRCYLYYF KSPQDALPLG HLDIADACFS YQGPDEAAEP GTEPPAHFQV HSAGAVTVLK
APNRQLMTYW LQELQQKRWE YCNSLDMVKW DSRTSPTPGD FPKGLVARDN TDLIYPHPNA
SAEKARNVLA VETVPGELVG EQAANQPAPG HPNSINFYSL KQWGNELKNS MSSFRPGRGH
NDSRRTVFYT NEEWELLDPT PKDLEESIVQ EEKKKLTPEG NKGVTGSGFP FDFGRNPYKG
KRPLKDIIGS YKNRHSSGDP SSEGTSGSGS VSIRKPASEM QLQVQSQQEE LEQLKKDLSS
QKELVRLLQQ TVRSSQYDKY FTSSRLCEGV PKDTLELLHQ KDDQILGLTS QLERFSLEKE
SLQQEVRTLK SKVGELNEQL GMLMETIQAK DEVIIKLSEG EGNGPPPTVA PSSPSVVPVA
RDQLELDRLK DNLQGYKTQN KFLNKEILEL SALRRNAERR ERDLMAKYSS LEAKLCQIES
KYLILLQEMK TPVCSEDQGP TREVIAQLLE DALQVESQEQ PEQAFVKPHL VSEYDIYGFR
TVPEDDEEEK LVAKVRALDL KTLYLTENQE VSTGVKWENY FASTVNREMM CSPELKNLIR
AGIPHEHRSK VWKWCVDRHT RKFKDNTEPG HFQTLLQKAL EKQNPASKQI ELDLLRTLPN
NKHYSCPTSE GIQKLRNVLL AFSWRNPDIG YCQGLNRLVA VALLYLEQED AFWCLVTIVE
VFMPRDYYTK TLLGSQVDQR VFRDLMSEKL PRLHGHFEQY KVDYTLITFN WFLVVFVDSV
VSDILFKIWD SFLYEGPKVI FRFALALFKY KEEEILKLQD SMSIFKYLRY FTRTILDARK
LISISFGDLN PFPLRQIRNR RAYHLEKVRL ELTELEAIRE DFLRERDTSP DKGELVSDEE
EDT
