ID ELMO3_HUMAN Reviewed; 720 AA.
AC Q96BJ8; B4DV86; Q9H8A5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 24-JAN-2024, entry version 166.
DE RecName: Full=Engulfment and cell motility protein 3;
GN Name=ELMO3;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLN-13.
RC TISSUE=Small intestine, and Thyroid;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-720 (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [4]
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).
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: Probably interacts directly with the SH3-domain of DOCK1 via
CC its SH3-binding site. Part of a complex with DOCK1 and RAC1 (By
CC similarity). Interacts with ADGRB3 (PubMed:24567399). {ECO:0000250,
CC ECO:0000269|PubMed:24567399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q96BJ8-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96BJ8-2; Sequence=VSP_037341;
CC Name=3;
CC IsoId=Q96BJ8-3; Sequence=VSP_037342;
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; AK300976; BAG62598.1; -; mRNA.
DR EMBL; AK023886; BAB14712.1; -; mRNA.
DR EMBL; AC040160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015524; AAH15524.1; -; mRNA.
DR EMBL; BC034410; AAH34410.2; -; mRNA.
DR CCDS; CCDS10833.3; -. [Q96BJ8-1]
DR RefSeq; NP_078988.2; NM_024712.3. [Q96BJ8-1]
DR AlphaFoldDB; Q96BJ8; -.
DR SMR; Q96BJ8; -.
DR BioGRID; 122872; 68.
DR IntAct; Q96BJ8; 23.
DR STRING; 9606.ENSP00000498602; -.
DR GlyGen; Q96BJ8; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q96BJ8; -.
DR PhosphoSitePlus; Q96BJ8; -.
DR BioMuta; ELMO3; -.
DR DMDM; 238054390; -.
DR EPD; Q96BJ8; -.
DR jPOST; Q96BJ8; -.
DR MassIVE; Q96BJ8; -.
DR MaxQB; Q96BJ8; -.
DR PaxDb; 9606-ENSP00000377566; -.
DR PeptideAtlas; Q96BJ8; -.
DR ProteomicsDB; 76083; -. [Q96BJ8-1]
DR ProteomicsDB; 76084; -. [Q96BJ8-2]
DR ProteomicsDB; 76085; -. [Q96BJ8-3]
DR Pumba; Q96BJ8; -.
DR Antibodypedia; 15666; 235 antibodies from 30 providers.
DR DNASU; 79767; -.
DR Ensembl; ENST00000393997.8; ENSP00000377566.3; ENSG00000102890.16. [Q96BJ8-1]
DR Ensembl; ENST00000477898.5; ENSP00000458539.1; ENSG00000102890.16. [Q96BJ8-2]
DR Ensembl; ENST00000652269.1; ENSP00000498602.1; ENSG00000102890.16. [Q96BJ8-3]
DR GeneID; 79767; -.
DR KEGG; hsa:79767; -.
DR MANE-Select; ENST00000393997.8; ENSP00000377566.3; NM_024712.5; NP_078988.3.
DR UCSC; uc002esa.4; human. [Q96BJ8-1]
DR AGR; HGNC:17289; -.
DR CTD; 79767; -.
DR DisGeNET; 79767; -.
DR GeneCards; ELMO3; -.
DR HGNC; HGNC:17289; ELMO3.
DR HPA; ENSG00000102890; Low tissue specificity.
DR MIM; 606422; gene.
DR neXtProt; NX_Q96BJ8; -.
DR OpenTargets; ENSG00000102890; -.
DR PharmGKB; PA27756; -.
DR VEuPathDB; HostDB:ENSG00000102890; -.
DR eggNOG; KOG2999; Eukaryota.
DR GeneTree; ENSGT00940000159455; -.
DR HOGENOM; CLU_023887_0_0_1; -.
DR InParanoid; Q96BJ8; -.
DR OrthoDB; 4872856at2759; -.
DR PhylomeDB; Q96BJ8; -.
DR TreeFam; TF312966; -.
DR PathwayCommons; Q96BJ8; -.
DR SignaLink; Q96BJ8; -.
DR BioGRID-ORCS; 79767; 15 hits in 1153 CRISPR screens.
DR GenomeRNAi; 79767; -.
DR Pharos; Q96BJ8; Tbio.
DR PRO; PR:Q96BJ8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96BJ8; Protein.
DR Bgee; ENSG00000102890; Expressed in mucosa of transverse colon and 127 other cell types or tissues.
DR ExpressionAtlas; Q96BJ8; baseline and differential.
DR Genevisible; Q96BJ8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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:SF16; ENGULFMENT AND CELL MOTILITY PROTEIN 3; 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 Alternative splicing; Apoptosis; Cytoplasm; Phagocytosis;
KW Reference proteome; SH3-binding.
FT CHAIN 1..720
FT /note="Engulfment and cell motility protein 3"
FT /id="PRO_0000153716"
FT DOMAIN 307..479
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT DOMAIN 542..664
FT /note="PH"
FT MOTIF 696..706
FT /note="SH3-binding"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037341"
FT VAR_SEQ 1
FT /note="M -> MARSSSLGRECGTPRSGLGKGGPPRPQGPQARCTLGRRCTVSGKCRR
FT PRPSWTM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037342"
FT VARIANT 13
FT /note="K -> Q (in dbSNP:rs12923138)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055402"
FT VARIANT 95
FT /note="N -> D (in dbSNP:rs8058861)"
FT /id="VAR_055403"
FT VARIANT 316
FT /note="R -> C (in dbSNP:rs33948247)"
FT /id="VAR_055404"
FT CONFLICT 65
FT /note="N -> S (in Ref. 1; BAG62598)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="R -> Q (in Ref. 1; BAG62598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 81467 MW; D8D81291B059618D CRC64;
MAPPRNVVKI AIKMRDAIPQ LIQLDQAKPL AAVLKEVCDA WSLTHSERYA LQFADGHRRY
ITENNRAEIK NGSILCLSTA PDLEAEQLLG GLQSNSPEGR REALRRLVPL ASDMIFAREV
ISRNGLQILG TIIEDGDDLG EVLALSLRAF SELMEHGVVS WETLSIPFVR KVVCYVNMNL
MDASVPPLAL GLLESVTLSS PALGQLVKSE VPLDRLLVHL QVMNQQLQTK AMALLTALLQ
GASPVERKHM LDYLWQRNLR QFIYKNIIHS AAPMGDEMAH HLYVLQALML GLLEPRMRTP
LDPYSQEQRE QLQVLRQAAF EVEGESSGAG LSADRRRSLC AREFRKLGFS NSNPAQDLER
VPPGLLALDN MLYFSRNAPS AYSRFVLENS SREDKHECPF ARGSIQLTVL LCELLRVGEP
CSETAQDFSP MFFGQDQSFH ELFCVGIQLL NKTWKEMRAT QEDFDKVMQV VREQLARTLA
LKPTSLELFR TKVNALTYGE VLRLRQTERL HQEGTLAPPI LELREKLKPE LMGLIRQQRL
LRLCEGTLFR KISSRRRQDK LWFCCLSPNH KLLQYGDMEE GASPPTLESL PEQLPVADMR
ALLTGKDCPH VREKGSGKQN KDLYELAFSI SYDRGEEEAY LNFIAPSKRE FYLWTDGLSA
LLGSPMGSEQ TRLDLEQLLT METKLRLLEL ENVPIPERPP PVPPPPTNFN FCYDCSIAEP
//
