ID BI2L1_HUMAN Reviewed; 511 AA. AC Q9UHR4; A4D268; Q75L21; Q75L22; Q96CV4; Q9H5F5; Q9Y2M8; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 05-SEP-2012, entry version 103. DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1; DE Short=BAI1-associated protein 2-like protein 1; DE AltName: Full=Insulin receptor tyrosine kinase substrate; GN Name=BAIAP2L1; Synonyms=IRTKS; 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]. RC TISSUE=Adrenal gland; RX MEDLINE=20402571; PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22616434; PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-511. RC TISSUE=Lung; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND SER-261, AND RP MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP FUNCTION, INTERACTION WITH RAC1 AND F-ACTIN, PHOSPHORYLATION, AND RP MUTAGENESIS OF LYS-141; LYS-142; ARG-145; LYS-146 AND RP 488-GLY--ARG-511. RX PubMed=17430976; DOI=10.1242/jcs.001776; RA Millard T.H., Dawson J., Machesky L.M.; RT "Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator RT with distinct filament bundling properties."; RL J. Cell Sci. 120:1663-1672(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18187866; DOI=10.2116/analsci.24.161; RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; RT "Automated phosphoproteome analysis for cultured cancer cells by two- RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; RL Anal. Sci. 24:161-166(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASS RP SPECTROMETRY. 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., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261; RP SER-281; SER-331; THR-412 AND SER-414, AND MASS SPECTROMETRY. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-261; THR-412; RP SER-414 AND THR-416, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL RT (CD178) by phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-274, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary epithelium; RX PubMed=19534553; DOI=10.1021/pr900044c; RA Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., RA Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., RA Wiley H.S., Qian W.-J.; RT "An extensive survey of tyrosine phosphorylation revealing new sites RT in human mammary epithelial cells."; RL J. Proteome Res. 8:3852-3861(2009). RN [15] RP FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), RP IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI EFFECTOR PROTEIN RP ESPF(U), INTERACTION WITH E.COLI INTIMIN RECEPTOR TIR, AND SUBCELLULAR RP LOCATION. RX PubMed=19366662; DOI=10.1073/pnas.0809131106; RA Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., RA Robbins D., Rosen M.K., Saksela K., Leong J.M.; RT "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 RT actin assembly effectors Tir and EspF(U) during pedestal formation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009). RN [16] 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 [17] RP STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN RP ESPF(U), AND SUBUNIT. RX PubMed=21098279; DOI=10.1073/pnas.1010243107; RA Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M., RA Saksela K., Permi P.; RT "Recognition of tandem PxxP motifs as a unique Src homology 3-binding RT mode triggers pathogen-driven actin assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010). CC -!- FUNCTION: May function as adapter protein. Involved in the CC formation of clusters of actin bundles. Plays a role in the CC reorganization of the actin cytoskeleton in response to bacterial CC infection. CC -!- SUBUNIT: Interacts with RAC1. Binds to F-actin. Interacts with CC FASLG. Interacts (via SH3 domain) with E.coli effector protein CC EspF(U) (via PXXP motifs). Identified in a complex containing at CC least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli CC intimin receptor Tir. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Recruited to CC actin pedestals that are formed upon infection by bacteria at CC bacterial attachment sites. CC -!- DOMAIN: The IMD domain is predicted to have a helical structure. CC It may induce actin bundling and filopodia formation (By CC similarity). CC -!- PTM: Phosphorylated on tyrosine in response to insulin. CC -!- SIMILARITY: Contains 1 IMD (IRSp53/MIM homology) domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAD20937.1; Type=Erroneous gene model prediction; CC Sequence=AAS07549.1; Type=Erroneous initiation; CC Sequence=BAB15671.1; 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; AF119666; AAF17223.2; -; mRNA. DR EMBL; AC004841; AAD20937.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC093169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093799; AAS07549.1; ALT_INIT; Genomic_DNA. DR EMBL; AC093799; AAS07550.1; -; Genomic_DNA. DR EMBL; CH236956; EAL23890.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76706.1; -; Genomic_DNA. DR EMBL; BC013888; AAH13888.1; -; mRNA. DR EMBL; AK027142; BAB15671.1; ALT_INIT; mRNA. DR IPI; IPI00179326; -. DR RefSeq; NP_061330.2; NM_018842.4. DR UniGene; Hs.656063; -. DR PDB; 2KXC; NMR; -; A=339-402. DR PDBsum; 2KXC; -. DR ProteinModelPortal; Q9UHR4; -. DR SMR; Q9UHR4; 1-247, 339-402. DR DIP; DIP-53820N; -. DR IntAct; Q9UHR4; 5. DR STRING; Q9UHR4; -. DR PhosphoSite; Q9UHR4; -. DR DMDM; 74735022; -. DR PeptideAtlas; Q9UHR4; -. DR PRIDE; Q9UHR4; -. DR DNASU; 55971; -. DR Ensembl; ENST00000005260; ENSP00000005260; ENSG00000006453. DR GeneID; 55971; -. DR KEGG; hsa:55971; -. DR UCSC; uc003upj.3; human. DR CTD; 55971; -. DR GeneCards; GC07M097920; -. DR H-InvDB; HIX0167837; -. DR HGNC; HGNC:21649; BAIAP2L1. DR HPA; HPA019484; -. DR HPA; HPA021257; -. DR HPA; HPA023874; -. DR HPA; HPA029503; -. DR MIM; 611877; gene. DR neXtProt; NX_Q9UHR4; -. DR PharmGKB; PA142672562; -. DR eggNOG; NOG71665; -. DR GeneTree; ENSGT00390000005995; -. DR HOVERGEN; HBG054462; -. DR InParanoid; Q9UHR4; -. DR OMA; HCSFANH; -. DR OrthoDB; EOG4GXFMT; -. DR PhylomeDB; Q9UHR4; -. DR GenomeRNAi; 55971; -. DR NextBio; 61407; -. DR ArrayExpress; Q9UHR4; -. DR Bgee; Q9UHR4; -. DR CleanEx; HS_BAIAP2L1; -. DR Genevestigator; Q9UHR4; -. DR GermOnline; ENSG00000006453; Homo sapiens. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0046847; P:filopodium assembly; IEA:InterPro. DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1. DR InterPro; IPR013606; IRSp53/MIM_homology_IMD. DR InterPro; IPR011511; SH3_2. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF08397; IMD; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3; 1. DR PROSITE; PS51338; IMD; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Coiled coil; Complete proteome; KW Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism; KW Reference proteome; SH3 domain. FT CHAIN 1 511 Brain-specific angiogenesis inhibitor 1- FT associated protein 2-like protein 1. FT /FTId=PRO_0000247854. FT DOMAIN 1 249 IMD. FT DOMAIN 339 402 SH3. FT REGION 483 511 Binds F-actin. FT COILED 115 154 Potential. FT MOD_RES 248 248 Phosphothreonine. FT MOD_RES 257 257 Phosphothreonine. FT MOD_RES 261 261 Phosphoserine. FT MOD_RES 274 274 Phosphotyrosine. FT MOD_RES 281 281 Phosphoserine. FT MOD_RES 329 329 Phosphoserine (By similarity). FT MOD_RES 331 331 Phosphoserine. FT MOD_RES 412 412 Phosphothreonine. FT MOD_RES 414 414 Phosphoserine. FT MOD_RES 416 416 Phosphothreonine. FT VARIANT 460 460 S -> T (in dbSNP:rs2269966). FT /FTId=VAR_033515. FT MUTAGEN 141 141 K->E: Loss ability to induce the FT formation of actin clusters; when FT associated with K-142; R-145 and K-146. FT MUTAGEN 142 142 K->E: Loss ability to induce the FT formation of actin clusters; when FT associated with K-141; R-145 and K-146. FT MUTAGEN 145 145 R->E: Loss ability to induce the FT formation of actin clusters; when FT associated with K-141; K-142 and K-146. FT MUTAGEN 146 146 K->E: Loss ability to induce the FT formation of actin clusters; when FT associated with K-141; K-142 and R-145. FT MUTAGEN 488 511 Missing: Loss ability to induce the FT formation of actin clusters; induce the FT formation of long filopodia. FT CONFLICT 456 456 A -> V (in Ref. 6; BAB15671). FT CONFLICT 460 460 S -> F (in Ref. 6; BAB15671). FT CONFLICT 464 464 A -> V (in Ref. 6; BAB15671). FT CONFLICT 466 466 A -> V (in Ref. 6; BAB15671). FT CONFLICT 467 467 S -> F (in Ref. 6; BAB15671). FT STRAND 343 348 FT STRAND 356 358 FT STRAND 366 373 FT STRAND 378 386 FT STRAND 389 393 FT HELIX 394 396 FT STRAND 397 400 SQ SEQUENCE 511 AA; 56883 MW; C2304C4444B02F02 CRC64; MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI IHELEKKIEL DVKYMNATLK RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS RNALKYEHKE IEYVETVTSR QSEIQKFIAD GCKEALLEEK RRFCFLVDKH CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM NMIEEIKTPA STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH TAGSNKTLLS FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL EENETEAVTV PTPSPTPVRS ISTVNLSENS SVVIPPPDYL ECLSMGAAAD RRADSARTTS TFKAPASKPE TAAPNDANGT AKPPFLSGEN PFATVKLRPT VTNDRSAPII R //