ELMO1_MOUSE
ID ELMO1_MOUSE Reviewed; 727 AA.
AC Q8BPU7; Q8BSY9; Q8K2C5; Q91ZU3;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Engulfment and cell motility protein 1;
DE AltName: Full=Protein ced-12 homolog;
GN Name=Elmo1;
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 1).
RC STRAIN=C57BL/6J;
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 3 AND 4).
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 MRNA] OF 309-727 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, Mammary tumor, and Retina;
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 ADGRB1 AND DOCK1.
RX PubMed=17960134; DOI=10.1038/nature06329;
RA Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z.,
RA Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT ELMO/Dock180/Rac module.";
RL Nature 450:430-434(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and 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).
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. Probably forms a heterotrimeric complex with DOCK1 and
CC RAC1 (By similarity). Interacts with PLEKHG6. Interacts with HCK (via
CC SH3 domain) (By similarity). Interacts with ADGRB1 (PubMed:17960134).
CC Interacts with ADGRB3 (By similarity). {ECO:0000250|UniProtKB:Q92556,
CC ECO:0000269|PubMed:17960134}.
CC -!- INTERACTION:
CC Q8BPU7-1; Q8BUR4: Dock1; NbExp=13; IntAct=EBI-644162, EBI-646023;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocation to plasma membrane seems to be
CC mediated by DOCK1 and CRK. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BPU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPU7-2; Sequence=VSP_007481;
CC Name=3;
CC IsoId=Q8BPU7-3; Sequence=VSP_007482, VSP_007483;
CC Name=4;
CC IsoId=Q8BPU7-4; Sequence=VSP_007481, VSP_007484, VSP_007485;
CC -!- PTM: Phosphorylated by HCK. {ECO:0000250}.
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DR EMBL; AF398883; AAL14464.1; -; mRNA.
DR EMBL; AK028389; BAC25925.1; -; mRNA.
DR EMBL; AK053306; BAC35336.1; -; mRNA.
DR EMBL; BC024727; AAH24727.1; -; mRNA.
DR EMBL; BC031782; AAH31782.1; -; mRNA.
DR CCDS; CCDS26265.1; -. [Q8BPU7-1]
DR RefSeq; NP_525027.1; NM_080288.2. [Q8BPU7-1]
DR RefSeq; NP_932761.1; NM_198093.3. [Q8BPU7-2]
DR RefSeq; XP_006516610.1; XM_006516547.3. [Q8BPU7-1]
DR AlphaFoldDB; Q8BPU7; -.
DR SMR; Q8BPU7; -.
DR BioGRID; 228288; 6.
DR CORUM; Q8BPU7; -.
DR DIP; DIP-41244N; -.
DR IntAct; Q8BPU7; 5.
DR MINT; Q8BPU7; -.
DR STRING; 10090.ENSMUSP00000072334; -.
DR iPTMnet; Q8BPU7; -.
DR PhosphoSitePlus; Q8BPU7; -.
DR EPD; Q8BPU7; -.
DR jPOST; Q8BPU7; -.
DR MaxQB; Q8BPU7; -.
DR PaxDb; Q8BPU7; -.
DR PeptideAtlas; Q8BPU7; -.
DR PRIDE; Q8BPU7; -.
DR ProteomicsDB; 275594; -. [Q8BPU7-1]
DR ProteomicsDB; 275595; -. [Q8BPU7-2]
DR ProteomicsDB; 275596; -. [Q8BPU7-3]
DR ProteomicsDB; 275597; -. [Q8BPU7-4]
DR Antibodypedia; 12940; 232 antibodies from 34 providers.
DR DNASU; 140580; -.
DR Ensembl; ENSMUST00000072519; ENSMUSP00000072334; ENSMUSG00000041112. [Q8BPU7-1]
DR Ensembl; ENSMUST00000180626; ENSMUSP00000152595; ENSMUSG00000041112. [Q8BPU7-3]
DR GeneID; 140580; -.
DR KEGG; mmu:140580; -.
DR UCSC; uc007ppn.3; mouse. [Q8BPU7-1]
DR UCSC; uc007ppo.1; mouse. [Q8BPU7-3]
DR UCSC; uc007ppq.2; mouse. [Q8BPU7-4]
DR UCSC; uc007ppr.3; mouse. [Q8BPU7-2]
DR CTD; 9844; -.
DR MGI; MGI:2153044; Elmo1.
DR VEuPathDB; HostDB:ENSMUSG00000041112; -.
DR eggNOG; KOG2999; Eukaryota.
DR GeneTree; ENSGT00940000155994; -.
DR HOGENOM; CLU_023887_0_0_1; -.
DR InParanoid; Q8BPU7; -.
DR OMA; WESHARP; -.
DR OrthoDB; 234725at2759; -.
DR PhylomeDB; Q8BPU7; -.
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 BioGRID-ORCS; 140580; 5 hits in 69 CRISPR screens.
DR ChiTaRS; Elmo1; mouse.
DR PRO; PR:Q8BPU7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BPU7; protein.
DR Bgee; ENSMUSG00000041112; Expressed in medial dorsal nucleus of thalamus and 255 other tissues.
DR ExpressionAtlas; Q8BPU7; baseline and differential.
DR Genevisible; Q8BPU7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030029; P:actin filament-based process; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IDA:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
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 Acetylation; Alternative splicing; Apoptosis; Cell membrane; Cytoplasm;
KW Membrane; Phagocytosis; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..727
FT /note="Engulfment and cell motility protein 1"
FT /id="PRO_0000153713"
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:0000250|UniProtKB:Q92556"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT MOD_RES 216
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT MOD_RES 511
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT MOD_RES 720
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000250|UniProtKB:Q92556"
FT VAR_SEQ 1..480
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007481"
FT VAR_SEQ 398..420
FT /note="IVLENSSREDKHECPFGRSSIEL -> VSMLASLRYCQCRMEFCFPTYAQ
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007482"
FT VAR_SEQ 421..727
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007483"
FT VAR_SEQ 636..642
FT /note="EVLELAF -> VWFSKSL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007484"
FT VAR_SEQ 643..727
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007485"
FT CONFLICT 9
FT /note="K -> E (in Ref. 2; BAC25925)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="P -> H (in Ref. 2; BAC25925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 83936 MW; 21B1BB9195504D28 CRC64;
MPPPSDIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY
ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF
INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF
IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGTDQEIQ
TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRYIILTHVI 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
