ID EIF3L_HUMAN Reviewed; 564 AA. AC Q9Y262; B2RDG6; B4DYB2; G8JLH4; Q53HQ1; Q53HT4; Q5QTR1; Q5TI15; AC Q6ICD2; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 03-APR-2013, entry version 107. DE RecName: Full=Eukaryotic translation initiation factor 3 subunit L; DE Short=eIF3l; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6-interacting protein; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit E-interacting protein; GN Name=EIF3L; Synonyms=EIF3EIP, EIF3S6IP; GN ORFNames=HSPC021, HSPC025, MSTP005; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Aorta; RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y., RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J., RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Cervix, and Colon; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH EIF3E. RX PubMed=11590142; DOI=10.1074/jbc.M104966200; RA Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.; RT "The human protein HSPC021 interacts with Int-6 and is associated with RT eukaryotic translation initiation factor 3."; RL J. Biol. Chem. 276:45988-45995(2001). RN [10] RP INTERACTION WITH RRN3. RX PubMed=12393749; DOI=10.1093/embo-reports/kvf212; RA Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.; RT "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) RT subunits regulate preinitiation complex assembly at the ribosomal gene RT promoter."; RL EMBO Rep. 3:1082-1087(2002). RN [11] RP CHARACTERIZATION OF THE EIF-3 COMPLEX. RX PubMed=15703437; DOI=10.1261/rna.7215305; RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., RA Pestova T.V.; RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits RT and its role in ribosomal dissociation and anti-association."; RL RNA 11:470-486(2005). RN [12] RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16766523; DOI=10.1074/jbc.M605418200; RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., RA Bradley C.A., Hershey J.W.B., Rhoads R.E.; RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e RT subunit."; RL J. Biol. Chem. 281:22917-22932(2006). RN [13] RP CHARACTERIZATION OF THE EIF-3 COMPLEX. RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765; RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.; RT "Reconstitution reveals the functional core of mammalian eIF3."; RL EMBO J. 26:3373-3383(2007). RN [14] RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND RP MASS SPECTROMETRY. RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200; RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.; RT "Structural characterization of the human eukaryotic initiation factor RT 3 protein complex by mass spectrometry."; RL Mol. Cell. Proteomics 6:1135-1146(2007). RN [15] RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 RP COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B. RX PubMed=18599441; DOI=10.1073/pnas.0801313105; RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., RA Doudna J.A., Robinson C.V.; RT "Mass spectrometry reveals modularity and a complete subunit RT interaction map of the eukaryotic translation factor eIF3."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-549, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [17] 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., RA Buerckstuemmer T., 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 [18] RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY. RX PubMed=16322461; DOI=10.1126/science.1118977; RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.; RT "Structural roles for human translation factor eIF3 in initiation of RT protein synthesis."; RL Science 310:1513-1515(2005). CC -!- FUNCTION: Component of the eukaryotic translation initiation CC factor 3 (eIF-3) complex, which is required for several steps in CC the initiation of protein synthesis. The eIF-3 complex associates CC with the 40S ribosome and facilitates the recruitment of eIF-1, CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA CC recruitment to the 43S PIC and scanning of the mRNA for AUG CC recognition. The eIF-3 complex is also required for disassembly CC and recycling of post-termination ribosomal complexes and CC subsequently prevents premature joining of the 40S and 60S CC ribosomal subunits prior to initiation. CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module CC C binds EIF3B of module A and EIF3H of module B, thereby linking CC the three modules. EIF3J is a labile subunit that binds to the CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 CC under conditions of nutrient depletion. Mitogenic stimulation CC leads to binding and activation of a complex composed of MTOR and CC RPTOR, leading to phosphorylation and release of RPS6KB1 and CC binding of EIF4B to eIF-3. Interacts with RRN3 (By similarity). CC -!- INTERACTION: CC Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-373519, EBI-6248094; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y262-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y262-2; Sequence=VSP_045881; CC Note=No experimental confirmation available; CC -!- MASS SPECTROMETRY: Mass=66637.9; Method=Unknown; Range=1-564; CC Source=PubMed:17322308; CC -!- MASS SPECTROMETRY: Mass=66640.2; Mass_error=0.5; Method=MALDI; CC Range=1-564; Source=PubMed:18599441; CC -!- SIMILARITY: Belongs to the eIF-3 subunit L family. CC -!- SEQUENCE CAUTION: CC Sequence=CAG30322.1; Type=Erroneous initiation; CC Sequence=CAX14899.1; Type=Erroneous initiation; 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; AF077207; AAD27002.1; -; mRNA. DR EMBL; AF083243; AAD39841.1; -; mRNA. DR EMBL; AF109359; AAQ13507.1; -; mRNA. DR EMBL; CR456436; CAG30322.1; ALT_INIT; mRNA. DR EMBL; AK302346; BAG63674.1; -; mRNA. DR EMBL; AK315533; BAG37913.1; -; mRNA. DR EMBL; AK222496; BAD96216.1; -; mRNA. DR EMBL; AK222529; BAD96249.1; -; mRNA. DR EMBL; Z97630; CAX14899.1; ALT_INIT; Genomic_DNA. DR EMBL; AL022311; CAX14899.1; JOINED; Genomic_DNA. DR EMBL; CH471095; EAW60198.1; -; Genomic_DNA. DR EMBL; BC001101; AAH01101.1; -; mRNA. DR EMBL; BC007510; AAH07510.1; -; mRNA. DR EMBL; BC029265; AAH29265.1; -; mRNA. DR IPI; IPI00745266; -. DR IPI; IPI00910422; -. DR RefSeq; NP_001229852.1; NM_001242923.1. DR RefSeq; NP_057175.1; NM_016091.3. DR UniGene; Hs.446852; -. DR ProteinModelPortal; Q9Y262; -. DR DIP; DIP-31172N; -. DR IntAct; Q9Y262; 10. DR MINT; MINT-216779; -. DR STRING; 9606.ENSP00000416892; -. DR PhosphoSite; Q9Y262; -. DR DMDM; 23396631; -. DR PaxDb; Q9Y262; -. DR PRIDE; Q9Y262; -. DR DNASU; 51386; -. DR Ensembl; ENST00000381683; ENSP00000371099; ENSG00000100129. DR Ensembl; ENST00000412331; ENSP00000416892; ENSG00000100129. DR GeneID; 51386; -. DR KEGG; hsa:51386; -. DR UCSC; uc003auf.3; human. DR CTD; 51386; -. DR GeneCards; GC22P038244; -. DR HGNC; HGNC:18138; EIF3L. DR HPA; HPA003028; -. DR neXtProt; NX_Q9Y262; -. DR PharmGKB; PA27706; -. DR eggNOG; NOG251364; -. DR HOVERGEN; HBG001289; -. DR InParanoid; Q9Y262; -. DR KO; K15029; -. DR OrthoDB; EOG4T4CV3; -. DR PhylomeDB; Q9Y262; -. DR ChiTaRS; EIF3L; human. DR GenomeRNAi; 51386; -. DR NextBio; 54905; -. DR ArrayExpress; Q9Y262; -. DR Bgee; Q9Y262; -. DR Genevestigator; Q9Y262; -. DR GermOnline; ENSG00000100129; Homo sapiens. DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; IEA:Compara. DR GO; GO:0005654; C:nucleoplasm; IEA:Compara. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB. DR HAMAP; MF_03011; eIF3l; 1; -. DR InterPro; IPR019382; TIF3_suL. DR Pfam; PF10255; Paf67; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Initiation factor; Polymorphism; Protein biosynthesis; KW Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 564 Eukaryotic translation initiation factor FT 3 subunit L. FT /FTId=PRO_0000084162. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 465 465 N6-acetyllysine. FT MOD_RES 549 549 N6-acetyllysine. FT VAR_SEQ 146 193 Missing (in isoform 2). FT /FTId=VSP_045881. FT VARIANT 239 239 N -> S (in dbSNP:rs11551387). FT /FTId=VAR_053937. FT CONFLICT 353 353 T -> I (in Ref. 2; AAQ13507). FT CONFLICT 377 377 M -> V (in Ref. 5; BAD96249). FT CONFLICT 432 432 H -> Y (in Ref. 5; BAD96216). FT CONFLICT 434 434 N -> D (in Ref. 5; BAD96249). FT CONFLICT 513 513 F -> L (in Ref. 4; BAG63674). FT CONFLICT 528 528 I -> T (in Ref. 4; BAG63674). FT CONFLICT 558 558 K -> R (in Ref. 4; BAG63674). SQ SEQUENCE 564 AA; 66727 MW; ECBD32192D96E3FE CRC64; MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAEAIAP QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN QWLWDIIDEF IYQFQSFSQY RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDPQVYE ELFSYSCPKF LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG DFFIRQIHKF EELNRTLKKM GQRP //