EH1L1_HUMAN
ID EH1L1_HUMAN Reviewed; 1523 AA.
AC Q8N3D4; Q8TB89; Q9H7M7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=EH domain-binding protein 1-like protein 1;
GN Name=EHBP1L1;
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-1523, AND VARIANTS LEU-133 AND
RP VAL-569.
RC TISSUE=Melanoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1523, AND VARIANTS LEU-133;
RP GLN-307; GLY-538 AND VAL-569.
RC TISSUE=Spleen;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1281-1523.
RC TISSUE=Muscle;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-1257, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-173; SER-191;
RP SER-285 AND SER-1168, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP IDENTIFICATION BY 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-1273, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-367; SER-430;
RP SER-964; SER-1168 AND SER-1257, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-1273, AND
RP IDENTIFICATION BY 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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=26833786; DOI=10.1083/jcb.201508086;
RA Nakajo A., Yoshimura S., Togawa H., Kunii M., Iwano T., Izumi A.,
RA Noguchi Y., Watanabe A., Goto A., Sato T., Harada A.;
RT "EHBP1L1 coordinates Rab8 and Bin1 to regulate apical-directed transport in
RT polarized epithelial cells.";
RL J. Cell Biol. 212:297-306(2016).
RN [14]
RP INTERACTION WITH RAB8A; RAB10; RAB13 AND RAB15, DOMAIN, FUNCTION,
RP ISOPRENYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
CC -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC trafficking. {ECO:0000305|PubMed:27552051}.
CC -!- SUBUNIT: Interacts with RAB8A, RAB10, RAB13 and RAB15 (in their GTP-
CC bound forms); at least in case of RAB8A can bind 2 molecules of RAB8A
CC simultaneously; ternary complex formation of RAB8A, RAB13 and EHBP1L1
CC is possible. {ECO:0000269|PubMed:27552051}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000305|PubMed:27552051}.
CC -!- DOMAIN: The CAAX motif is a signal for prenylation and required for
CC endosomal colocalization with Rab8 and Rab10.
CC {ECO:0000269|PubMed:27552051}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound
CC forms). {ECO:0000269|PubMed:27552051}.
CC -!- PTM: Prenylated (Probable). Farnelysation (predominant) and
CC geranylgeranylation has been observed in vitro.
CC {ECO:0000269|PubMed:27552051}.
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DR EMBL; AP001362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834433; CAD39093.1; -; mRNA.
DR EMBL; AK024451; BAB15741.1; -; mRNA.
DR EMBL; BC024207; AAH24207.2; -; mRNA.
DR CCDS; CCDS44649.1; -.
DR RefSeq; NP_001092879.1; NM_001099409.1.
DR AlphaFoldDB; Q8N3D4; -.
DR SMR; Q8N3D4; -.
DR BioGRID; 129015; 46.
DR IntAct; Q8N3D4; 5.
DR MINT; Q8N3D4; -.
DR STRING; 9606.ENSP00000312671; -.
DR iPTMnet; Q8N3D4; -.
DR PhosphoSitePlus; Q8N3D4; -.
DR BioMuta; EHBP1L1; -.
DR DMDM; 146286137; -.
DR EPD; Q8N3D4; -.
DR jPOST; Q8N3D4; -.
DR MassIVE; Q8N3D4; -.
DR MaxQB; Q8N3D4; -.
DR PaxDb; Q8N3D4; -.
DR PeptideAtlas; Q8N3D4; -.
DR PRIDE; Q8N3D4; -.
DR ProteomicsDB; 71793; -.
DR Antibodypedia; 51069; 13 antibodies from 7 providers.
DR DNASU; 254102; -.
DR Ensembl; ENST00000309295.9; ENSP00000312671.4; ENSG00000173442.13.
DR GeneID; 254102; -.
DR KEGG; hsa:254102; -.
DR MANE-Select; ENST00000309295.9; ENSP00000312671.4; NM_001099409.3; NP_001092879.1.
DR UCSC; uc001oeo.5; human.
DR CTD; 254102; -.
DR DisGeNET; 254102; -.
DR GeneCards; EHBP1L1; -.
DR HGNC; HGNC:30682; EHBP1L1.
DR HPA; ENSG00000173442; Tissue enhanced (skeletal).
DR MIM; 619583; gene.
DR neXtProt; NX_Q8N3D4; -.
DR OpenTargets; ENSG00000173442; -.
DR PharmGKB; PA134871712; -.
DR VEuPathDB; HostDB:ENSG00000173442; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000161027; -.
DR HOGENOM; CLU_004178_0_0_1; -.
DR InParanoid; Q8N3D4; -.
DR OMA; SGAPEMD; -.
DR OrthoDB; 165311at2759; -.
DR PhylomeDB; Q8N3D4; -.
DR TreeFam; TF105382; -.
DR PathwayCommons; Q8N3D4; -.
DR SignaLink; Q8N3D4; -.
DR BioGRID-ORCS; 254102; 40 hits in 1075 CRISPR screens.
DR ChiTaRS; EHBP1L1; human.
DR GenomeRNAi; 254102; -.
DR Pharos; Q8N3D4; Tdark.
DR PRO; PR:Q8N3D4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N3D4; protein.
DR Bgee; ENSG00000173442; Expressed in granulocyte and 153 other tissues.
DR ExpressionAtlas; Q8N3D4; baseline and differential.
DR Genevisible; Q8N3D4; HS.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR029928; Ehbp1l1.
DR InterPro; IPR019448; NT-C2.
DR PANTHER; PTHR23167:SF42; PTHR23167:SF42; 2.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF10358; NT-C2; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS51840; C2_NT; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..1523
FT /note="EH domain-binding protein 1-like protein 1"
FT /id="PRO_0000285204"
FT DOMAIN 8..157
FT /note="C2 NT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01186"
FT DOMAIN 1037..1142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1349..1501
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195,
FT ECO:0000305|PubMed:27552051"
FT REGION 179..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1363..1515
FT /evidence="ECO:0000255"
FT MOTIF 1520..1523
FT /note="CAAX motif"
FT /evidence="ECO:0000305|PubMed:27552051"
FT COMPBIAS 209..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99MS7"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MS7"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 133
FT /note="V -> L (in dbSNP:rs1194100)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_061645"
FT VARIANT 307
FT /note="R -> Q (in dbSNP:rs3741380)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031993"
FT VARIANT 538
FT /note="V -> G (in dbSNP:rs6591182)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031994"
FT VARIANT 569
FT /note="D -> V (in dbSNP:rs1194099)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031995"
FT VARIANT 599
FT /note="T -> I (in dbSNP:rs7931052)"
FT /id="VAR_031996"
FT VARIANT 648
FT /note="T -> I (in dbSNP:rs7931269)"
FT /id="VAR_031997"
FT CONFLICT 1235
FT /note="P -> L (in Ref. 2; CAD39093)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378
FT /note="D -> E (in Ref. 2; CAD39093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1523 AA; 161854 MW; 5F0DD06B15131597 CRC64;
MTSVWKRLQR VGKRAAKFQF VACYHELVLE CTKKWQPDKL VVVWTRRNRR ICSKAHSWQP
GIQNPYRGTV VWMVPENVDI SVTLYRDPHV DQYEAKEWTF IIENESKGQR KVLATAEVDL
ARHAGPVPVQ VPVRLRLKPK SVKVVQAELS LTLSGVLLRE GRATDDDMQS LASLMSVKPS
DVGNLDDFAE SDEDEAHGPG APEARARVPQ PDPSRELKTL CEEEEEGQGR PQQAVASPSN
AEDTSPAPVS APAPPARTSR GQGSERANEA GGQVGPEAPR PPETSPEMRS SRQPAQDTAP
TPAPRLRKGS DALRPPVPQG EDEVPKASGA PPAGLGSARE TQAQACPQEG TEAHGARLGP
SIEDKGSGDP FGRQRLKAEE MDTEDRPEAS GVDTEPRSGG REANTKRSGV RAGEAEESSA
VCQVDAEQRS KVRHVDTKGP EATGVMPEAR CRGTPEAPPR GSQGRLGVRT RDEAPSGLSL
PPAEPAGHSG QLGDLEGARA AAGQEREGAE VRGGAPGIEG TGLEQGPSVG AISTRPQVSS
WQGALLSTAQ GAISRGLGGW EAEAGGSGDL ETETEVVGLE VLGTQEKEVE GSGFPETRTL
EIEILGALEK EAARSRVLES EVAGTAQCEG LETQETEVGV IETPGTETEV LGTQKTEAGG
SGVLQTRTTI AETEVLVTQE ISGDLGPLKI EDTIQSEMLG TQETEVEASR VPESEAEGTE
AKILGTQEIT ARDSGVREIE AEIAESDILV AQEIEVGLLG VLGIETGAAE GAILGTQEIA
SRDSGVPGLE ADTTGIQVKE VGGSEVPEIA TGTAETEILG TQEIASRSSG VPGLESEVAG
AQETEVGGSG ISGPEAGMAE ARVLMTRKTE IIVPEAEKEE AQTSGVQEAE TRVGSALKYE
ALRAPVTQPR VLGSQEAKAE ISGVQGSETQ VLRVQEAEAG VWGMSEGKSG AWGAQEAEMK
VLESPENKSG TFKAQEAEAG VLGNEKGKEA EGSLTEASLP EAQVASGAGA GAPRASSPEK
AEEDRRLPGS QAPPALVSSS QSLLEWCQEV TTGYRGVRIT NFTTSWRNGL AFCAILHRFY
PDKIDYASLD PLNIKQNNKQ AFDGFAALGV SRLLEPADMV LLSVPDKLIV MTYLCQIRAF
CTGQELQLVQ LEGGGGAGTY RVGSAQPSPP DDLDAGGLAQ RLRGHGAEGP QEPKEAADRA
DGAAPGVASR NAVAGRASKD GGAEAPRESR PAEVPAEGLV NGAGAPGGGG VRLRRPSVNG
EPGSVPPPRA HGSFSHVRDA DLLKKRRSRL RNSSSFSMDD PDAGAMGAAA AEGQAPDPSP
APGPPTAADS QQPPGGSSPS EEPPPSPGEE AGLQRFQDTS QYVCAELQAL EQEQRQIDGR
AAEVEMQLRS LMESGANKLQ EEVLIQEWFT LVNKKNALIR RQDQLQLLME EQDLERRFEL
LSRELRAMLA IEDWQKTSAQ QHREQLLLEE LVSLVNQRDE LVRDLDHKER IALEEDERLE
RGLEQRRRKL SRQLSRRERC VLS
