EFL1_HUMAN
ID EFL1_HUMAN Reviewed; 1120 AA.
AC Q7Z2Z2; A6NKY5; B7Z6I0; Q9H8Z6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Elongation factor-like GTPase 1;
DE AltName: Full=Elongation factor Tu GTP-binding domain-containing protein 1;
DE AltName: Full=Elongation factor-like 1;
DE AltName: Full=Protein FAM42A;
GN Name=EFL1 {ECO:0000312|HGNC:HGNC:25789}; Synonyms=EFTUD1, FAM42A;
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 1), AND VARIANT ASP-478.
RC TISSUE=Placenta;
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 MRNA] (ISOFORM 2), AND VARIANT ASP-478.
RC TISSUE=Fetal 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 [3]
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-528, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
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 [6]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF THR-33 AND HIS-96.
RX PubMed=21536732; DOI=10.1101/gad.623011;
RA Finch A.J., Hilcenko C., Basse N., Drynan L.F., Goyenechea B., Menne T.F.,
RA Gonzalez Fernandez A., Simpson P., D'Santos C.S., Arends M.J., Donadieu J.,
RA Bellanne-Chantelot C., Costanzo M., Boone C., McKenzie A.N., Freund S.M.,
RA Warren A.J.;
RT "Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causes
RT Shwachman-Diamond syndrome.";
RL Genes Dev. 25:917-929(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=25015090; DOI=10.1093/neuonc/nou132;
RA Saito K., Iizuka Y., Ohta S., Takahashi S., Nakamura K., Saya H.,
RA Yoshida K., Kawakami Y., Toda M.;
RT "Functional analysis of a novel glioma antigen, EFTUD1.";
RL Neuro-oncol. 16:1618-1629(2014).
RN [9]
RP INTERACTION WITH SBDS; GTP AND GDP.
RX PubMed=25991726; DOI=10.1074/jbc.m114.626275;
RA Garcia-Marquez A., Gijsbers A., de la Mora E., Sanchez-Puig N.;
RT "Defective guanine nucleotide exchange in the elongation factor-like 1
RT (EFL1) GTPase by mutations in the Shwachman-Diamond syndrome protein.";
RL J. Biol. Chem. 290:17669-17678(2015).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), AND IDENTIFICATION IN A
RP COMPLEX WITH SBDS; 60S RIBOSOMAL SUBUNIT AND EFL1.
RX PubMed=26479198; DOI=10.1038/nsmb.3112;
RA Weis F., Giudice E., Churcher M., Jin L., Hilcenko C., Wong C.C.,
RA Traynor D., Kay R.R., Warren A.J.;
RT "Mechanism of eIF6 release from the nascent 60S ribosomal subunit.";
RL Nat. Struct. Mol. Biol. 22:914-919(2015).
RN [11]
RP INVOLVEMENT IN SDS2, AND VARIANTS SDS2 LYS-882 AND GLN-1095.
RX PubMed=28331068; DOI=10.1136/jmedgenet-2016-104366;
RA Stepensky P., Chacon-Flores M., Kim K.H., Abuzaitoun O.,
RA Bautista-Santos A., Simanovsky N., Siliqi D., Altamura D., Mendez-Godoy A.,
RA Gijsbers A., Naser Eddin A., Dor T., Charrow J., Sanchez-Puig N.,
RA Elpeleg O.;
RT "Mutations in EFL1, an SBDS partner, are associated with infantile
RT pancytopenia, exocrine pancreatic insufficiency and skeletal anomalies in a
RT Shwachman-Diamond like syndrome.";
RL J. Med. Genet. 54:558-566(2017).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit and
CC translational activation of ribosomes. Together with SBDS, triggers the
CC GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm,
CC thereby activating ribosomes for translation competence by allowing 80S
CC ribosome assembly and facilitating EIF6 recycling to the nucleus, where
CC it is required for 60S rRNA processing and nuclear export. Has low
CC intrinsic GTPase activity. GTPase activity is increased by contact with
CC 60S ribosome subunits. {ECO:0000269|PubMed:21536732}.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit (PubMed:21536732).
CC Found in a complex consisting of the 60S ribosomal subunit, SBDS and
CC EFL1 (PubMed:22814378). Interacts with SBDS and binds to GTP and GDP;
CC the interaction with SBDS decreases EFL1 affinity for GDP and
CC facilitates GDP release (PubMed:25991726).
CC {ECO:0000269|PubMed:21536732, ECO:0000269|PubMed:25991726}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z2Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2Z2-2; Sequence=VSP_030152;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in brain. Expression is
CC highly increased in glioma tissues. {ECO:0000269|PubMed:25015090}.
CC -!- DISEASE: Shwachman-Diamond syndrome 2 (SDS2) [MIM:617941]: A form of
CC Shwachman-Diamond syndrome, a disorder characterized by hematopoietic
CC abnormalities, exocrine pancreatic dysfunction, and skeletal dysplasia.
CC Intermittent or chronic neutropenia is the most common hematological
CC manifestation, followed by anemia and thrombocytopenia. Some patients
CC progress to bone marrow failure, myelodysplastic syndrome and malignant
CC transformation, with acute myelogenous leukemia being the most common.
CC Exocrine pancreatic dysfunction is generally the first presenting
CC symptom in infancy. Short stature and metaphyseal dysplasia are the
CC most frequent skeletal manifestations. SDS2 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:28331068}. Note=The disease may be
CC caused by 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.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14450.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK023181; BAB14450.1; ALT_INIT; mRNA.
DR EMBL; AK300348; BAH13266.1; -; mRNA.
DR EMBL; BX538332; CAD98101.1; -; mRNA.
DR EMBL; AC026624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS42070.1; -. [Q7Z2Z2-2]
DR CCDS; CCDS42071.1; -. [Q7Z2Z2-1]
DR RefSeq; NP_001035700.1; NM_001040610.2. [Q7Z2Z2-2]
DR RefSeq; NP_001309774.1; NM_001322845.1. [Q7Z2Z2-1]
DR RefSeq; NP_078856.4; NM_024580.5. [Q7Z2Z2-1]
DR PDB; 5ANB; EM; 4.10 A; K=1-1120.
DR PDB; 5ANC; EM; 4.20 A; K=1-1120.
DR PDBsum; 5ANB; -.
DR PDBsum; 5ANC; -.
DR AlphaFoldDB; Q7Z2Z2; -.
DR SMR; Q7Z2Z2; -.
DR BioGRID; 122761; 49.
DR IntAct; Q7Z2Z2; 19.
DR MINT; Q7Z2Z2; -.
DR STRING; 9606.ENSP00000268206; -.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB02750; S-(Methylmercury)-L-Cysteine.
DR GlyGen; Q7Z2Z2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z2Z2; -.
DR MetOSite; Q7Z2Z2; -.
DR PhosphoSitePlus; Q7Z2Z2; -.
DR BioMuta; EFL1; -.
DR DMDM; 166232397; -.
DR EPD; Q7Z2Z2; -.
DR jPOST; Q7Z2Z2; -.
DR MassIVE; Q7Z2Z2; -.
DR MaxQB; Q7Z2Z2; -.
DR PaxDb; Q7Z2Z2; -.
DR PeptideAtlas; Q7Z2Z2; -.
DR PRIDE; Q7Z2Z2; -.
DR ProteomicsDB; 68991; -. [Q7Z2Z2-1]
DR ProteomicsDB; 68992; -. [Q7Z2Z2-2]
DR Antibodypedia; 55408; 89 antibodies from 18 providers.
DR DNASU; 79631; -.
DR Ensembl; ENST00000268206.12; ENSP00000268206.7; ENSG00000140598.15. [Q7Z2Z2-1]
DR Ensembl; ENST00000359445.7; ENSP00000352418.3; ENSG00000140598.15. [Q7Z2Z2-2]
DR GeneID; 79631; -.
DR KEGG; hsa:79631; -.
DR MANE-Select; ENST00000268206.12; ENSP00000268206.7; NM_024580.6; NP_078856.4.
DR UCSC; uc002bgt.2; human. [Q7Z2Z2-1]
DR CTD; 79631; -.
DR DisGeNET; 79631; -.
DR GeneCards; EFL1; -.
DR HGNC; HGNC:25789; EFL1.
DR HPA; ENSG00000140598; Low tissue specificity.
DR MalaCards; EFL1; -.
DR MIM; 617538; gene.
DR MIM; 617941; phenotype.
DR neXtProt; NX_Q7Z2Z2; -.
DR OpenTargets; ENSG00000140598; -.
DR Orphanet; 811; Shwachman-Diamond syndrome.
DR PharmGKB; PA134902221; -.
DR VEuPathDB; HostDB:ENSG00000140598; -.
DR eggNOG; KOG0467; Eukaryota.
DR GeneTree; ENSGT00550000074806; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR InParanoid; Q7Z2Z2; -.
DR OMA; ERFARCE; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; Q7Z2Z2; -.
DR TreeFam; TF105909; -.
DR BRENDA; 3.6.5.3; 2681.
DR PathwayCommons; Q7Z2Z2; -.
DR SignaLink; Q7Z2Z2; -.
DR SIGNOR; Q7Z2Z2; -.
DR BioGRID-ORCS; 79631; 689 hits in 1058 CRISPR screens.
DR ChiTaRS; EFL1; human.
DR GenomeRNAi; 79631; -.
DR Pharos; Q7Z2Z2; Tbio.
DR PRO; PR:Q7Z2Z2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7Z2Z2; protein.
DR Bgee; ENSG00000140598; Expressed in secondary oocyte and 164 other tissues.
DR ExpressionAtlas; Q7Z2Z2; baseline and differential.
DR Genevisible; Q7Z2Z2; HS.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IMP:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Ribosome biogenesis.
FT CHAIN 1..1120
FT /note="Elongation factor-like GTPase 1"
FT /id="PRO_0000313805"
FT DOMAIN 17..272
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 430..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 528
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 32..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030152"
FT VARIANT 478
FT /note="E -> D (in dbSNP:rs2292189)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_037746"
FT VARIANT 617
FT /note="I -> V (in dbSNP:rs1128431)"
FT /id="VAR_037747"
FT VARIANT 711
FT /note="K -> R (in dbSNP:rs2292071)"
FT /id="VAR_037748"
FT VARIANT 882
FT /note="M -> K (in SDS2; unknown pathological significance;
FT dbSNP:rs1316615934)"
FT /evidence="ECO:0000269|PubMed:28331068"
FT /id="VAR_080513"
FT VARIANT 1095
FT /note="R -> Q (in SDS2; unknown pathological significance;
FT dbSNP:rs376095522)"
FT /evidence="ECO:0000269|PubMed:28331068"
FT /id="VAR_080514"
FT MUTAGEN 33
FT /note="T->A: Loss of GTPase activity. Abolishes
FT dissociation of EIF6 from 60S pre-ribosome subunits."
FT /evidence="ECO:0000269|PubMed:21536732"
FT MUTAGEN 96
FT /note="H->A: Loss of GTPase activity. Abolishes
FT dissociation of EIF6 from 60S pre-ribosome subunits."
FT /evidence="ECO:0000269|PubMed:21536732"
FT CONFLICT 456
FT /note="A -> V (in Ref. 2; CAD98101)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="Q -> R (in Ref. 1; BAB14450)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="I -> T (in Ref. 2; CAD98101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1120 AA; 125430 MW; CCD765953015F109 CRC64;
MVLNSLDKMI QLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR
EDEQIRGITM KSSAISLHYA TGNEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV
EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFTPQ EAYSHLKNIL EQINALTGTL
FTSKVLEERA ERETESQVNP NSEQGEQVYD WSTGLEDTDD SHLYFSPEQG NVVFTSAIDG
WGFGIEHFAR IYSQKIGIKK EVLMKTLWGD YYINMKAKKI MKGDQAKGKK PLFVQLILEN
IWSLYDAVLK KDKDKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP ISHAVLAMVC
QKLPSPLDIT AERVERLMCT GSQTFDSFPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV
DAKALPQNKP RPLTQEEIAQ RRERARQRHA EKLAAAQGQA PLEPTQDGSA IETCPKGEEP
RGDEQQVESM TPKPVLQEEN NQESFIAFAR VFSGVARRGK KIFVLGPKYS PLEFLRRVPL
GFSAPPDGLP QVPHMAYCAL ENLYLLMGRE LEYLEEVPPG NVLGIGGLQD FVLKSATLCS
LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQIL IQETGEHVLV
TAGEVHLQRC LDDLKERFAK IHISVSEPII PFRETITKPP KVDMVNEEIG KQQKVAVIHQ
MKEDQSKIPE GIQVDSDGLI TITTPNKLAT LSVRAMPLPE EVTQILEENS DLIRSMEQLT
SSLNEGENTH MIHQKTQEKI WEFKGKLEQH LTGRRWRNIV DQIWSFGPRK CGPNILVNKS
EDFQNSVWTG PADKASKEAS RYRDLGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWDLS
KFEEQGASDL AKEGQEENET CSGGNENQEL QDGCSEAFEK RTSQKGESPL TDCYGPFSGQ
LIATMKEACR YALQVKPQRL MAAMYTCDIM ATGDVLGRVY AVLSKREGRV LQEEMKEGTD
MFIIKAVLPV AESFGFADEI RKRTSGLASP QLVFSHWEII PSDPFWVPTT EEEYLHFGEK
ADSENQARKY MNAVRKRKGL YVEEKIVEHA EKQRTLSKNK
