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   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.
DR   Genevisible; Q8BHL5; MM.
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
//