ID   ELMO1_HUMAN             Reviewed;         727 AA.
AC   Q92556; Q29R79; Q96PB0; Q9H0I1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   03-NOV-2009, entry version 93.
DE   RecName: Full=Engulfment and cell motility protein 1;
DE   AltName: Full=CED-12 homolog;
GN   Name=ELMO1; Synonyms=KIAA0281;
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   DOCK1, AND SUBUNIT OF A COMPLEX WITH DOCK1 AND CRK.
RX   MEDLINE=21479119; 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
RT   required for phagocytosis and cell migration.";
RL   Cell 107:27-41(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=97323006; PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RT   "Construction and characterization of human brain cDNA libraries
RT   suitable for analysis of cDNA clones encoding relatively large
RT   proteins.";
RL   DNA Res. 4:53-59(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Lung, and Pancreas;
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   [5]
RP   PHOSPHORYLATION.
RX   MEDLINE=22140354; PubMed=12029088; DOI=10.1074/jbc.M202783200;
RA   Scott M.P., Zappacosta F., Kim E.Y., Annan R.S., Miller W.T.;
RT   "Identification of novel SH3 domain ligands for the Src family kinase
RT   Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein
RT   (WIP), and ELMO1.";
RL   J. Biol. Chem. 277:28238-28246(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH DOCK1, AND SUBUNIT OF A COMPLEX CONTAINING
RP   RAC1 AND DOCK1.
RX   MEDLINE=22144530; PubMed=12134158; DOI=10.1038/ncb824;
RA   Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F.,
RA   Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R.,
RA   Ravichandran K.S.;
RT   "Unconventional Rac-GEF activity is mediated through the Dock180-ELMO
RT   complex.";
RL   Nat. Cell Biol. 4:574-582(2002).
RN   [7]
RP   INTERACTION WITH PLEKHG6.
RX   PubMed=17881735; DOI=10.1091/mbc.E06-12-1144;
RA   D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D.,
RA   Arpin M.;
RT   "Interaction of ezrin with the novel guanine nucleotide exchange
RT   factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton
RT   rearrangements in epithelial cells.";
RL   Mol. Biol. Cell 18:4780-4793(2007).
RN   [8]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-105, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
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).
CC   -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC       phagocytosis of apoptotic cells and cell motility. Acts in
CC       assocation with DOCK1 and CRK. Was initially proposed to be
CC       required in complex with DOCK1 to activate Rac Rho small GTPases.
CC       May enhance the guanine nucleotide exchange factor (GEF) activity
CC       of DOCK1.
CC   -!- SUBUNIT: Interacts with BAI1 (By similarity). Interacts directly
CC       with the SH3-domain of DOCK1 via its SH3-binding site. Part of a
CC       complex with DOCK1 and RAC1. Part of a complex with DOCK1 and CRK
CC       isoform CRK-II. Interacts with PLEKHG6.
CC   -!- INTERACTION:
CC       Q14185:DOCK1; NbExp=2; IntAct=EBI-346417, EBI-446740;
CC       P08631:HCK; NbExp=4; IntAct=EBI-346417, EBI-346340;
CC       P84095:RHOG; NbExp=2; IntAct=EBI-346417, EBI-446579;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocation
CC       to plasma membrane seems to be mediated by DOCK1 and CRK.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92556-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92556-2; Sequence=VSP_007480;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in
CC       the spleen and placenta.
CC   -!- PTM: Phosphorylated by HCK (Probable).
CC   -!- SIMILARITY: Contains 1 ELMO domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AF398885; AAL14466.1; -; mRNA.
DR   EMBL; D87457; BAA13397.2; ALT_INIT; mRNA.
DR   EMBL; AL136787; CAB66721.1; -; mRNA.
DR   EMBL; BC003051; AAH03051.1; -; mRNA.
DR   EMBL; BC064635; AAH64635.1; -; mRNA.
DR   EMBL; BC077074; AAH77074.1; -; mRNA.
DR   EMBL; BC114341; AAI14342.1; -; mRNA.
DR   IPI; IPI00219532; -.
DR   IPI; IPI00745455; -.
DR   RefSeq; NP_001034548.1; -.
DR   RefSeq; NP_055615.8; -.
DR   RefSeq; NP_569709.1; -.
DR   UniGene; Hs.656638; -.
DR   PDB; 2VSZ; X-ray; 2.30 A; A/B=532-675.
DR   PDBsum; 2VSZ; -.
DR   IntAct; Q92556; 4.
DR   STRING; Q92556; -.
DR   PhosphoSite; Q92556; -.
DR   PeptideAtlas; Q92556; -.
DR   PRIDE; Q92556; -.
DR   Ensembl; ENST00000310758; ENSP00000312185; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000341056; ENSP00000342142; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000361912; ENSP00000355266; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000396040; ENSP00000379355; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000396042; ENSP00000379357; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000396045; ENSP00000379360; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000420636; ENSP00000396465; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000424212; ENSP00000395933; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000433246; ENSP00000413108; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000442504; ENSP00000406952; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000442573; ENSP00000406330; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000445322; ENSP00000397857; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000448602; ENSP00000394458; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000453399; ENSP00000391734; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000455119; ENSP00000406610; ENSG00000155849; Homo sapiens.
DR   Ensembl; ENST00000455879; ENSP00000416090; ENSG00000155849; Homo sapiens.
DR   GeneID; 9844; -.
DR   KEGG; hsa:9844; -.
DR   UCSC; uc003tfi.1; human.
DR   UCSC; uc003tfk.1; human.
DR   CTD; 9844; -.
DR   GeneCards; GC07M036860; -.
DR   H-InvDB; HIX0020858; -.
DR   HGNC; HGNC:16286; ELMO1.
DR   MIM; 606420; gene.
DR   PharmGKB; PA27754; -.
DR   HOGENOM; Q92556; -.
DR   HOVERGEN; Q92556; -.
DR   OMA; FPKLMEI; -.
DR   Pathway_Interaction_DB; trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
DR   Reactome; REACT_6185; HIV Infection.
DR   NextBio; 37098; -.
DR   ArrayExpress; Q92556; -.
DR   Bgee; Q92556; -.
DR   CleanEx; HS_ELMO1; -.
DR   Genevestigator; Q92556; -.
DR   GermOnline; ENSG00000155849; Homo sapiens.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; NAS:UniProtKB.
DR   GO; GO:0006928; P:cell motion; IGI:UniProtKB.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IGI:UniProtKB.
DR   GO; GO:0016601; P:Rac protein signal transduction; IGI:UniProtKB.
DR   InterPro; IPR006816; Engulfment_cell_motility_ELMO.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF04727; ELMO_CED12; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS51335; ELMO; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   Cell membrane; Complete proteome; Cytoplasm; Membrane; Phagocytosis;
KW   Phosphoprotein; SH3-binding.
FT   CHAIN         1    727       Engulfment and cell motility protein 1.
FT                                /FTId=PRO_0000153712.
FT   DOMAIN      319    492       ELMO.
FT   DOMAIN      555    676       PH.
FT   MOTIF       707    714       SH3-binding.
FT   MOD_RES     100    100       N6-acetyllysine.
FT   MOD_RES     105    105       N6-acetyllysine.
FT   VAR_SEQ       1    480       Missing (in isoform 2).
FT                                /FTId=VSP_007480.
FT   CONFLICT    716    716       E -> A (in Ref. 3; CAB66721).
FT   HELIX       532    534
FT   HELIX       535    538
FT   HELIX       540    557
FT   STRAND      561    563
FT   STRAND      569    571
FT   STRAND      574    576
FT   STRAND      583    588
FT   STRAND      591    593
FT   STRAND      604    609
FT   HELIX       610    612
FT   STRAND      613    617
FT   HELIX       623    625
FT   HELIX       635    638
FT   STRAND      641    646
FT   TURN        647    649
FT   STRAND      650    655
FT   HELIX       659    666
FT   TURN        670    672
SQ   SEQUENCE   727 AA;  83829 MW;  053DCA73D2B0A4C6 CRC64;
     MPPPADIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY
     ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF
     INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF
     IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGSDQEIQ
     TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL
     TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG
     FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL
     TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV
     MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI
     QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP
     HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH
     EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY
     DFVYDCN
//