ID ELMO2_MOUSE Reviewed; 732 AA.
AC Q8BHL5; A2A5A6; Q5GMG3; Q8BHL9; Q8BQG1; Q8CBM8; Q8CC50; Q8CH98; Q91ZU2;
AC Q9CT75;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 166.
DE RecName: Full=Engulfment and cell motility protein 2;
DE AltName: Full=Protein ced-12 homolog A;
GN Name=Elmo2; Synonyms=Kiaa1834;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C3H/HeJ;
RX PubMed=11595183; DOI=10.1016/s0092-8674(01)00520-7;
RA Gumienny T.L., Brugnera E., Tosello-Trampont A.-C., Kinchen J.M.,
RA Haney L.B., Nishiwaki K., Walk S.F., Nemergut M.E., Macara I.G.,
RA Francis R., Schedl T., Qin Y., Van Aelst L., Hengartner M.O.,
RA Ravichandran K.S.;
RT "CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required
RT for phagocytosis and cell migration.";
RL Cell 107:27-41(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, Cerebellum, Diencephalon, Embryo, Eye, Hypothalamus,
RC Medulla oblongata, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-732.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48 AND TYR-729, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH AUTS2 AND DOCK1.
RX PubMed=25533347; DOI=10.1016/j.celrep.2014.11.045;
RA Hori K., Nagai T., Shan W., Sakamoto A., Taya S., Hashimoto R., Hayashi T.,
RA Abe M., Yamazaki M., Nakao K., Nishioka T., Sakimura K., Yamada K.,
RA Kaibuchi K., Hoshino M.;
RT "Cytoskeletal regulation by AUTS2 in neuronal migration and
RT neuritogenesis.";
RL Cell Rep. 9:2166-2179(2014).
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Acts in association
CC with DOCK1 and CRK. Was initially proposed to be required in complex
CC with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine
CC nucleotide exchange factor (GEF) activity of DOCK1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts directly with the SH3-domain of DOCK1 via its SH3-
CC binding site (PubMed:25533347). Probably forms a heterotrimeric complex
CC with DOCK1 and RAC1. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates
CC activation of RAC1 by EPHA2 (By similarity). Interacts with ADGRB3 (By
CC similarity). Interacts with AUTS2; the interaction is direct
CC (PubMed:25533347). {ECO:0000250|UniProtKB:Q96JJ3,
CC ECO:0000269|PubMed:25533347}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96JJ3}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96JJ3}. Membrane
CC {ECO:0000250|UniProtKB:Q96JJ3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BHL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHL5-2; Sequence=VSP_007488;
CC Name=3;
CC IsoId=Q8BHL5-3; Sequence=VSP_007488, VSP_007489;
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DR EMBL; AF398884; AAL14465.1; -; mRNA.
DR EMBL; AK004448; BAB23307.1; -; mRNA.
DR EMBL; AK032033; BAC27662.1; -; mRNA.
DR EMBL; AK033918; BAC28514.1; -; mRNA.
DR EMBL; AK035710; BAC29162.1; -; mRNA.
DR EMBL; AK038455; BAC30007.1; -; mRNA.
DR EMBL; AK045428; BAC32361.1; -; mRNA.
DR EMBL; AK047040; BAC32945.1; -; mRNA.
DR EMBL; AK050823; BAC34424.1; -; mRNA.
DR EMBL; AK053574; BAC35433.1; -; mRNA.
DR EMBL; AL591430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023954; AAH23954.1; -; mRNA.
DR EMBL; AB093301; BAC41483.3; -; Transcribed_RNA.
DR CCDS; CCDS17075.1; -. [Q8BHL5-2]
DR CCDS; CCDS17076.1; -. [Q8BHL5-1]
DR RefSeq; NP_001289681.1; NM_001302752.1. [Q8BHL5-2]
DR RefSeq; NP_001289683.1; NM_001302754.1.
DR RefSeq; NP_525026.2; NM_080287.2. [Q8BHL5-2]
DR RefSeq; NP_997589.1; NM_207706.1. [Q8BHL5-1]
DR RefSeq; XP_011237586.1; XM_011239284.1. [Q8BHL5-1]
DR RefSeq; XP_011237587.1; XM_011239285.1. [Q8BHL5-1]
DR RefSeq; XP_011237588.1; XM_011239286.2. [Q8BHL5-2]
DR RefSeq; XP_017170976.1; XM_017315487.1. [Q8BHL5-1]
DR PDB; 6UKA; X-ray; 2.40 A; B=1-80.
DR PDBsum; 6UKA; -.
DR AlphaFoldDB; Q8BHL5; -.
DR SMR; Q8BHL5; -.
DR BioGRID; 228287; 1.
DR IntAct; Q8BHL5; 2.
DR STRING; 10090.ENSMUSP00000073691; -.
DR iPTMnet; Q8BHL5; -.
DR PhosphoSitePlus; Q8BHL5; -.
DR EPD; Q8BHL5; -.
DR MaxQB; Q8BHL5; -.
DR PaxDb; 10090-ENSMUSP00000071619; -.
DR PeptideAtlas; Q8BHL5; -.
DR ProteomicsDB; 275598; -. [Q8BHL5-1]
DR ProteomicsDB; 275599; -. [Q8BHL5-2]
DR ProteomicsDB; 275600; -. [Q8BHL5-3]
DR Pumba; Q8BHL5; -.
DR Antibodypedia; 13191; 275 antibodies from 32 providers.
DR DNASU; 140579; -.
DR Ensembl; ENSMUST00000071699.11; ENSMUSP00000071619.5; ENSMUSG00000017670.17. [Q8BHL5-3]
DR Ensembl; ENSMUST00000074046.13; ENSMUSP00000073691.7; ENSMUSG00000017670.17. [Q8BHL5-1]
DR Ensembl; ENSMUST00000094329.11; ENSMUSP00000091887.5; ENSMUSG00000017670.17. [Q8BHL5-2]
DR Ensembl; ENSMUST00000103088.10; ENSMUSP00000099377.4; ENSMUSG00000017670.17. [Q8BHL5-3]
DR Ensembl; ENSMUST00000103091.9; ENSMUSP00000099380.3; ENSMUSG00000017670.17. [Q8BHL5-2]
DR GeneID; 140579; -.
DR KEGG; mmu:140579; -.
DR UCSC; uc008nxj.1; mouse. [Q8BHL5-2]
DR UCSC; uc008nxk.1; mouse. [Q8BHL5-1]
DR UCSC; uc008nxm.2; mouse. [Q8BHL5-3]
DR AGR; MGI:2153045; -.
DR CTD; 63916; -.
DR MGI; MGI:2153045; Elmo2.
DR VEuPathDB; HostDB:ENSMUSG00000017670; -.
DR eggNOG; KOG2999; Eukaryota.
DR GeneTree; ENSGT00940000159236; -.
DR HOGENOM; CLU_023887_0_0_1; -.
DR InParanoid; Q8BHL5; -.
DR OMA; XDMANAF; -.
DR OrthoDB; 4872856at2759; -.
DR PhylomeDB; Q8BHL5; -.
DR TreeFam; TF312966; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 140579; 8 hits in 78 CRISPR screens.
DR ChiTaRS; Elmo2; mouse.
DR PRO; PR:Q8BHL5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BHL5; Protein.
DR Bgee; ENSMUSG00000017670; Expressed in dentate gyrus of hippocampal formation granule cell and 292 other cell types or tissues.
DR ExpressionAtlas; Q8BHL5; baseline and differential.
DR Genevisible; Q8BHL5; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR CDD; cd13359; PH_ELMO1_CED-12; 1.
DR Gene3D; 6.10.250.810; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12771; ENGULFMENT AND CELL MOTILITY; 1.
DR PANTHER; PTHR12771:SF8; ENGULFMENT AND CELL MOTILITY PROTEIN 2; 1.
DR Pfam; PF11841; ELMO_ARM; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Membrane;
KW Phagocytosis; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..732
FT /note="Engulfment and cell motility protein 2"
FT /id="PRO_0000153715"
FT DOMAIN 323..497
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT DOMAIN 565..686
FT /note="PH"
FT MOTIF 712..719
FT /note="SH3-binding"
FT MOD_RES 48
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JJ3"
FT MOD_RES 729
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT VAR_SEQ 253..264
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11595183,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007488"
FT VAR_SEQ 667..732
FT /note="YCIWIDGLSALLGKDMSSELTKSDLDTLLSMEMKLRLLDLENIQIPEAPPPV
FT PKEPSSYDFVYHYG -> VSSVPHCLEHQCPHCEEVSVPHCLEHQCSHCEEVWPAQRYP
FT HKPGSQNGSLSLWTFYHWAGLPTSHRGLSSSAFRGLGLELCATTPNLSLCALEQLAWHR
FT EGFPLCNLAVTFPRRVESQLPGANLVRLWSQMDLPLLTRDSQFT (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007489"
FT CONFLICT 102
FT /note="D -> G (in Ref. 2; BAC28514)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="Missing (in Ref. 1; AAL14465)"
FT /evidence="ECO:0000305"
FT CONFLICT 519..523
FT /note="ILRLR -> NSAVA (in Ref. 2; BAC29162)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="I -> V (in Ref. 5; BAC41483)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="M -> I (in Ref. 2; BAC34424)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6UKA"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6UKA"
SQ SEQUENCE 732 AA; 83887 MW; 087A80728DC43A23 CRC64;
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
VTEQTRNDIK NGTILQLAVS PSRAARQLME RTQSSSMETR LDAMKELAKL SADVTFATEF
INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSV TFIKQIAGYV
SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
ALFLKAPEDK RQDKHLNPLD LPVTDMANAF AQKHLRSIIL NHVIRGNRPI KTEMAHQLYV
LQVLTFNLLE ERMMTKMDPN DQAQRDIIFE LRRIAFDAES DPSNVPGSGT EKRKAMYTKD
YKMLGFTNHI NPALDFTQTP PGMLALDNML YLAKVHQDTY IRIVLENSSR EDKHECPFGR
SAIELTKMLC EILQVGELPN EGRNDYHPMF FTHDRAFEEL FGICIQLLNK TWKEMRATAE
DFNKVMQVVR EQITRALPSK PNSLDQFKSK LRSLSYSEIL RLRQSERMSQ DDFQSPPIVE
LREKIQPEIL ELIKQQRLNR LCEGSSFRKI GNRRRQERFW HCRLALNHKV LHYGDLDDNP
QGEVTFESLQ EKIPVADIKA IVTGKDCPHM KEKSALKQNK EVLELAFSIL YDPDETLNFI
APNKYEYCIW IDGLSALLGK DMSSELTKSD LDTLLSMEMK LRLLDLENIQ IPEAPPPVPK
EPSSYDFVYH YG
//
