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ELMO3_MOUSE
ID   ELMO3_MOUSE             Reviewed;         720 AA.
AC   Q8BYZ7; Q6PDE4;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Engulfment and cell motility protein 3;
GN   Name=Elmo3;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; 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   [4]
RP   PROTEIN SEQUENCE OF 607-612, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Pancreas;
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).
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 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q96BJ8}.
CC   -!- INTERACTION:
CC       Q8BYZ7; Q8BUR4: Dock1; NbExp=4; IntAct=EBI-646035, EBI-646023;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYZ7-2; Sequence=VSP_037343;
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DR   EMBL; AK037067; BAC29692.1; -; mRNA.
DR   EMBL; CH466525; EDL11267.1; -; Genomic_DNA.
DR   EMBL; BC058752; AAH58752.3; -; mRNA.
DR   EMBL; BC138887; AAI38888.1; -; mRNA.
DR   CCDS; CCDS22598.1; -. [Q8BYZ7-1]
DR   RefSeq; NP_766348.3; NM_172760.3. [Q8BYZ7-1]
DR   AlphaFoldDB; Q8BYZ7; -.
DR   SMR; Q8BYZ7; -.
DR   BioGRID; 231558; 1.
DR   IntAct; Q8BYZ7; 1.
DR   STRING; 10090.ENSMUSP00000105000; -.
DR   PhosphoSitePlus; Q8BYZ7; -.
DR   MaxQB; Q8BYZ7; -.
DR   PaxDb; Q8BYZ7; -.
DR   PeptideAtlas; Q8BYZ7; -.
DR   PRIDE; Q8BYZ7; -.
DR   ProteomicsDB; 275742; -. [Q8BYZ7-1]
DR   ProteomicsDB; 275743; -. [Q8BYZ7-2]
DR   Antibodypedia; 15666; 215 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000109375; ENSMUSP00000105000; ENSMUSG00000014791. [Q8BYZ7-1]
DR   GeneID; 234683; -.
DR   KEGG; mmu:234683; -.
DR   UCSC; uc009ncn.2; mouse. [Q8BYZ7-1]
DR   CTD; 79767; -.
DR   MGI; MGI:2679007; Elmo3.
DR   VEuPathDB; HostDB:ENSMUSG00000014791; -.
DR   eggNOG; KOG2999; Eukaryota.
DR   GeneTree; ENSGT00940000159455; -.
DR   HOGENOM; CLU_023887_0_0_1; -.
DR   InParanoid; Q8BYZ7; -.
DR   OMA; CPHIREK; -.
DR   OrthoDB; 234725at2759; -.
DR   PhylomeDB; Q8BYZ7; -.
DR   TreeFam; TF312966; -.
DR   BioGRID-ORCS; 234683; 6 hits in 71 CRISPR screens.
DR   ChiTaRS; Elmo3; mouse.
DR   PRO; PR:Q8BYZ7; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BYZ7; protein.
DR   Bgee; ENSMUSG00000014791; Expressed in spermatocyte and 202 other tissues.
DR   ExpressionAtlas; Q8BYZ7; baseline and differential.
DR   Genevisible; Q8BYZ7; MM.
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   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; IPR030719; ELMO3.
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:SF16; PTHR12771:SF16; 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   Alternative splicing; Apoptosis; Cytoplasm; Direct protein sequencing;
KW   Phagocytosis; Reference proteome; SH3-binding.
FT   CHAIN           1..720
FT                   /note="Engulfment and cell motility protein 3"
FT                   /id="PRO_0000153717"
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 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_037343"
SQ   SEQUENCE   720 AA;  81758 MW;  FDDB6FCDA422309B CRC64;
     MAPPRNVVKI AVQMSDAIPQ LIQLDQAKPL ATVLKEVCDA WSLTHPEHYA LQFADGHRKY
     ITENNRLEIK NGSILCLSTA PDLKAQQLLG RLQNTSREGC CEVLRNLVLL ASDMTFAQEV
     ISRDGLQKLS TIIENGDDLG EMLALGLRAF LELMEHGVVS WETLSISFVR KVISYVNMNL
     MDASVQPLAL RLLESVTLSS PALGQLVKSE VPLDRLLVHL QVMNHQLQTK AMALLTALLQ
     GASPTERKEM LDHLWKKNLR QFIYKNIIHS ATPMGDEMAH HLYVLQALTL GLLEPRMRTP
     LDPYSQEQRD QLQALRQAAF EPEGESLGTG LSADRRRSLC VREFRKLGFS NSNPAQDLER
     VPPGLLALDN MLYFSRHAPS AYSRFVLENS SREDKHECPF ARSSIQLTAL LCELLRVGEP
     CSETAQDFSP MFFSQDHSFH ELFCVAIQLL NKTWKEMRAT QEDFDKVMQV VREQLARTLA
     LKPTSLELFR TKVNALTYGE VLRLRQTERL HQEGTLAPPI LELREKLKPE LMGLIRQQRL
     LRLCEGMLFR KISSRRRQDK LWFCCLSPNH KVLQYGDVEE GAKPPTLESL PEQLPVADIR
     ALLMGKDCPH VREKGSGKQN KDLYELAFSI SYDHGEEEAY LNFIAPSKRD FYLWTDGLSA
     LLGSTMGSEL TRLDLEQLLT METKLRLLEL ENVPIPEQPP PVPPPPTNFN FCYDYSITEP
 
 
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