ELMO1_HUMAN
ID ELMO1_HUMAN Reviewed; 727 AA.
AC Q92556; A4D1X6; Q29R79; Q6ZTJ0; Q96PB0; Q9H0I1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Engulfment and cell motility protein 1;
DE AltName: Full=Protein ced-12 homolog;
GN Name=ELMO1; Synonyms=KIAA0281;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DOCK1,
RP AND SUBUNIT OF A COMPLEX WITH DOCK1 AND CRK.
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] (ISOFORM 2).
RC TISSUE=Brain;
RX 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 suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Urinary bladder;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX 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., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., 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., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION.
RX 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 Hck.
RT Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP),
RT and ELMO1.";
RL J. Biol. Chem. 277:28238-28246(2002).
RN [9]
RP FUNCTION, INTERACTION WITH DOCK1, AND SUBUNIT OF A COMPLEX CONTAINING RAC1
RP AND DOCK1.
RX 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 [10]
RP INTERACTION WITH HCK, AND PHOSPHORYLATION AT TYR-18; TYR-216; TYR-395;
RP TYR-511 AND TYR-720.
RX PubMed=15952790; DOI=10.1021/bi0500832;
RA Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S.,
RA Ravichandran K.S., Miller W.T.;
RT "Identification of tyrosine residues on ELMO1 that are phosphorylated by
RT the Src-family kinase Hck.";
RL Biochemistry 44:8841-8849(2005).
RN [11]
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., Arpin M.;
RT "Interaction of ezrin with the novel guanine nucleotide exchange factor
RT PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in
RT epithelial cells.";
RL Mol. Biol. Cell 18:4780-4793(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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).
RN [14]
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., Buerckstuemmer T.,
RA 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INTERACTION WITH ADGRB3.
RX PubMed=24567399; DOI=10.1073/pnas.1313886111;
RA Hamoud N., Tran V., Croteau L.P., Kania A., Cote J.F.;
RT "G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3745-3750(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP VARIANT SER-362.
RX PubMed=20869035; DOI=10.1016/j.ajhg.2010.08.015;
RA Funari V.A., Krakow D., Nevarez L., Chen Z., Funari T.L., Vatanavicharn N.,
RA Wilcox W.R., Rimoin D.L., Nelson S.F., Cohn D.H.;
RT "BMPER mutation in diaphanospondylodysostosis identified by ancestral
RT autozygosity mapping and targeted high-throughput sequencing.";
RL Am. J. Hum. Genet. 87:532-537(2010).
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.
CC {ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:12134158}.
CC -!- SUBUNIT: Interacts with ADGRB1 (By similarity). Interacts directly with
CC the SH3-domain of DOCK1 via its SH3-binding site. Part of a complex
CC with DOCK1 and RAC1. Part of a complex with DOCK1 and CRK isoform CRK-
CC II. Interacts with PLEKHG6. Interacts with HCK (via SH3 domain).
CC Interacts with ADGRB3 (PubMed:24567399). {ECO:0000250|UniProtKB:Q8BPU7,
CC ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:12134158,
CC ECO:0000269|PubMed:15952790, ECO:0000269|PubMed:17881735,
CC ECO:0000269|PubMed:24567399}.
CC -!- INTERACTION:
CC Q92556; Q14185: DOCK1; NbExp=17; IntAct=EBI-346417, EBI-446740;
CC Q92556; P08631: HCK; NbExp=4; IntAct=EBI-346417, EBI-346340;
CC Q92556; P84095: RHOG; NbExp=3; IntAct=EBI-346417, EBI-446579;
CC Q92556; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-346417, EBI-2130429;
CC Q92556; Q8TD17: ZNF398; NbExp=5; IntAct=EBI-346417, EBI-8643207;
CC Q92556-1; O14514: ADGRB1; NbExp=2; IntAct=EBI-15668002, EBI-1995178;
CC Q92556-1; Q3UHD1: Adgrb1; Xeno; NbExp=9; IntAct=EBI-15668002, EBI-911280;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocation to
CC plasma membrane seems to be mediated by DOCK1 and CRK.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92556-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92556-2; Sequence=VSP_007480;
CC Name=3;
CC IsoId=Q92556-3; Sequence=VSP_038550, VSP_038551;
CC -!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in the
CC spleen and placenta.
CC -!- PTM: Phosphorylated by HCK. {ECO:0000305|PubMed:12029088,
CC ECO:0000305|PubMed:15952790}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13397.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF398885; AAL14466.1; -; mRNA.
DR EMBL; D87457; BAA13397.2; ALT_INIT; mRNA.
DR EMBL; AL136787; CAB66721.1; -; mRNA.
DR EMBL; AK126565; BAC86597.1; -; mRNA.
DR EMBL; CH236951; EAL23979.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94076.1; -; Genomic_DNA.
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 CCDS; CCDS5449.1; -. [Q92556-1]
DR CCDS; CCDS5450.1; -. [Q92556-2]
DR RefSeq; NP_001034548.1; NM_001039459.2. [Q92556-2]
DR RefSeq; NP_001193409.1; NM_001206480.2. [Q92556-1]
DR RefSeq; NP_001193411.1; NM_001206482.1. [Q92556-1]
DR RefSeq; NP_055615.8; NM_014800.10. [Q92556-1]
DR RefSeq; NP_569709.1; NM_130442.3. [Q92556-2]
DR RefSeq; XP_005249976.1; XM_005249919.2. [Q92556-1]
DR RefSeq; XP_006715868.1; XM_006715805.1. [Q92556-1]
DR RefSeq; XP_011513956.1; XM_011515654.1. [Q92556-1]
DR RefSeq; XP_016868327.1; XM_017012838.1.
DR RefSeq; XP_016868328.1; XM_017012839.1. [Q92556-1]
DR PDB; 2RQR; NMR; -; A=697-722.
DR PDB; 2VSZ; X-ray; 2.30 A; A/B=532-675.
DR PDB; 3A98; X-ray; 2.10 A; B/D=532-727.
DR PDB; 6JPP; NMR; -; A=1-113.
DR PDB; 6TGB; EM; 5.50 A; B=1-727.
DR PDB; 6TGC; EM; 4.10 A; B/E=1-727.
DR PDB; 7DPA; EM; 3.80 A; C/F=1-727.
DR PDBsum; 2RQR; -.
DR PDBsum; 2VSZ; -.
DR PDBsum; 3A98; -.
DR PDBsum; 6JPP; -.
DR PDBsum; 6TGB; -.
DR PDBsum; 6TGC; -.
DR PDBsum; 7DPA; -.
DR AlphaFoldDB; Q92556; -.
DR SMR; Q92556; -.
DR BioGRID; 115180; 32.
DR CORUM; Q92556; -.
DR DIP; DIP-31095N; -.
DR IntAct; Q92556; 21.
DR MINT; Q92556; -.
DR STRING; 9606.ENSP00000312185; -.
DR iPTMnet; Q92556; -.
DR MetOSite; Q92556; -.
DR PhosphoSitePlus; Q92556; -.
DR BioMuta; ELMO1; -.
DR DMDM; 30923321; -.
DR CPTAC; CPTAC-1759; -.
DR EPD; Q92556; -.
DR jPOST; Q92556; -.
DR MassIVE; Q92556; -.
DR MaxQB; Q92556; -.
DR PaxDb; Q92556; -.
DR PeptideAtlas; Q92556; -.
DR PRIDE; Q92556; -.
DR ProteomicsDB; 75312; -. [Q92556-1]
DR ProteomicsDB; 75313; -. [Q92556-2]
DR ProteomicsDB; 75314; -. [Q92556-3]
DR Antibodypedia; 12940; 232 antibodies from 34 providers.
DR DNASU; 9844; -.
DR Ensembl; ENST00000310758.9; ENSP00000312185.4; ENSG00000155849.16. [Q92556-1]
DR Ensembl; ENST00000396040.6; ENSP00000379355.2; ENSG00000155849.16. [Q92556-2]
DR Ensembl; ENST00000396045.7; ENSP00000379360.3; ENSG00000155849.16. [Q92556-2]
DR Ensembl; ENST00000442504.5; ENSP00000406952.1; ENSG00000155849.16. [Q92556-1]
DR Ensembl; ENST00000448602.5; ENSP00000394458.1; ENSG00000155849.16. [Q92556-1]
DR GeneID; 9844; -.
DR KEGG; hsa:9844; -.
DR MANE-Select; ENST00000310758.9; ENSP00000312185.4; NM_014800.11; NP_055615.8.
DR UCSC; uc003tfi.3; human. [Q92556-1]
DR CTD; 9844; -.
DR DisGeNET; 9844; -.
DR GeneCards; ELMO1; -.
DR HGNC; HGNC:16286; ELMO1.
DR HPA; ENSG00000155849; Tissue enhanced (brain).
DR MIM; 606420; gene.
DR neXtProt; NX_Q92556; -.
DR OpenTargets; ENSG00000155849; -.
DR PharmGKB; PA27754; -.
DR VEuPathDB; HostDB:ENSG00000155849; -.
DR eggNOG; KOG2999; Eukaryota.
DR GeneTree; ENSGT00940000155994; -.
DR HOGENOM; CLU_097960_0_0_1; -.
DR InParanoid; Q92556; -.
DR OMA; WESHARP; -.
DR PhylomeDB; Q92556; -.
DR TreeFam; TF312966; -.
DR PathwayCommons; Q92556; -.
DR Reactome; R-HSA-164944; Nef and signal transduction.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q92556; -.
DR SIGNOR; Q92556; -.
DR BioGRID-ORCS; 9844; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; ELMO1; human.
DR EvolutionaryTrace; Q92556; -.
DR GeneWiki; ELMO1; -.
DR GenomeRNAi; 9844; -.
DR Pharos; Q92556; Tbio.
DR PRO; PR:Q92556; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q92556; protein.
DR Bgee; ENSG00000155849; Expressed in prefrontal cortex and 168 other tissues.
DR ExpressionAtlas; Q92556; baseline and differential.
DR Genevisible; Q92556; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:WormBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030029; P:actin filament-based process; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; IGI:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IGI:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IGI:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR030715; ELMO1.
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:SF23; PTHR12771:SF23; 1.
DR Pfam; PF11841; DUF3361; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane;
KW Cytoplasm; Membrane; Phagocytosis; Phosphoprotein; Reference proteome;
KW SH3-binding.
FT CHAIN 1..727
FT /note="Engulfment and cell motility protein 1"
FT /id="PRO_0000153712"
FT DOMAIN 319..492
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT DOMAIN 555..676
FT /note="PH"
FT MOTIF 707..714
FT /note="SH3-binding"
FT MOD_RES 18
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:15952790"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 216
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:15952790"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPU7"
FT MOD_RES 395
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:15952790"
FT MOD_RES 511
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:15952790"
FT MOD_RES 720
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:15952790"
FT VAR_SEQ 1..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9179496"
FT /id="VSP_007480"
FT VAR_SEQ 1..298
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038550"
FT VAR_SEQ 299..362
FT /note="VLTFNLLEDRMMTKMDPQDQAQRDIIFELRRIAFDAESEPNNSSGSMEKRKS
FT MYTRDYKKLGFI -> MSEHQKEQTLDTPSLRTVTLTVRVHGFILEVSKTKNPPIPDTF
FT WPPRWDHRPSPGGETNAYCQM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038551"
FT VARIANT 362
FT /note="I -> S"
FT /evidence="ECO:0000269|PubMed:20869035"
FT /id="VAR_065824"
FT CONFLICT 716
FT /note="E -> A (in Ref. 3; CAB66721)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:6JPP"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6JPP"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6JPP"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:6JPP"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6JPP"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:6JPP"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6JPP"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6JPP"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6JPP"
FT HELIX 532..558
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:2VSZ"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:2VSZ"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 641..646
FT /evidence="ECO:0007829|PDB:3A98"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:3A98"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 659..672
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 680..697
FT /evidence="ECO:0007829|PDB:3A98"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:3A98"
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
