Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Engulfment and cell motility protein 1

Gene

Elmo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament-based process Source: MGI
  • apoptotic process Source: UniProtKB-KW
  • cell migration Source: InterPro
  • movement of cell or subcellular component Source: UniProtKB
  • phagocytosis Source: MGI
  • phagocytosis, engulfment Source: UniProtKB
  • Rac protein signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Phagocytosis

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Engulfment and cell motility protein 1
Alternative name(s):
Protein ced-12 homolog
Gene namesi
Name:Elmo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2153044. Elmo1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • guanyl-nucleotide exchange factor complex Source: WormBase
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 727727Engulfment and cell motility protein 1PRO_0000153713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphotyrosine; by HCKBy similarity
Modified residuei100 – 1001N6-acetyllysineBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei216 – 2161Phosphotyrosine; by HCKBy similarity
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei395 – 3951Phosphotyrosine; by HCKBy similarity
Modified residuei511 – 5111Phosphotyrosine; by HCKBy similarity
Modified residuei720 – 7201Phosphotyrosine; by HCKBy similarity

Post-translational modificationi

Phosphorylated by HCK.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BPU7.
MaxQBiQ8BPU7.
PaxDbiQ8BPU7.
PRIDEiQ8BPU7.

PTM databases

iPTMnetiQ8BPU7.
PhosphoSiteiQ8BPU7.

Expressioni

Gene expression databases

BgeeiQ8BPU7.
GenevisibleiQ8BPU7. MM.

Interactioni

Subunit structurei

Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Probably forms a heterotrimeric complex with DOCK1 and RAC1 (By similarity). Interacts with PLEKHG6. Interacts with HCK (via SH3 domain) (By similarity). Interacts with ADGRB1 (PubMed:17960134). Interacts with ADGRB3 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dock1Q8BUR413EBI-644162,EBI-646023

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-41244N.
IntActiQ8BPU7. 2 interactions.
MINTiMINT-219471.
STRINGi10090.ENSMUSP00000072334.

Structurei

3D structure databases

ProteinModelPortaliQ8BPU7.
SMRiQ8BPU7. Positions 530-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini319 – 492174ELMOPROSITE-ProRule annotationAdd
BLAST
Domaini555 – 676122PHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi707 – 7148SH3-binding

Sequence similaritiesi

Contains 1 ELMO domain.PROSITE-ProRule annotation
Contains 1 PH domain.Curated

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG2999. Eukaryota.
ENOG410XPKN. LUCA.
GeneTreeiENSGT00390000014155.
HOGENOMiHOG000252986.
HOVERGENiHBG051463.
InParanoidiQ8BPU7.
KOiK12366.
OMAiEMSHILA.
OrthoDBiEOG7D85VW.
PhylomeDBiQ8BPU7.
TreeFamiTF312966.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR030715. ELMO1.
IPR006816. ELMO_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR12771:SF23. PTHR12771:SF23. 1 hit.
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
PF16457. PH_12. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS51335. ELMO. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BPU7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPPSDIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA
60 70 80 90 100
LQHADSSNFY ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK
110 120 130 140 150
LEALKDLASL SRDVTFAQEF INLDGISLLT QMVESGTERY QKLQKIMKPC
160 170 180 190 200
FGDMLSFTLT AFVELMDHGI VSWDTFSVAF IKKIASFVNK SAIDISILQR
210 220 230 240 250
SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGTDQEIQ TYTIAVINAL
260 270 280 290 300
FLKAPDERRQ EMANILAQKQ LRYIILTHVI RAQRAINNEM AHQLYVLQVL
310 320 330 340 350
TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS
360 370 380 390 400
MYTRDYKKLG FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL
410 420 430 440 450
ENSSREDKHE CPFGRSSIEL TKMLCEILKV GELPSETCND FHPMFFTHDR
460 470 480 490 500
SFEEFFCICI QLLNKTWKEM RATSEDFNKV MQVVKEQVMR ALTTKPSSLD
510 520 530 540 550
QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI QPEILELIKQ
560 570 580 590 600
QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP
610 620 630 640 650
HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC
660 670 680 690 700
QLNFIAPDKH EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD
710 720
LENIQIPDAP PPIPKEPSNY DFVYDCN
Length:727
Mass (Da):83,936
Last modified:May 16, 2003 - v2
Checksum:i21B1BB9195504D28
GO
Isoform 2 (identifier: Q8BPU7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.

Note: No experimental confirmation available.
Show »
Length:247
Mass (Da):28,742
Checksum:iD02BCEC8D8A4383F
GO
Isoform 3 (identifier: Q8BPU7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     398-420: IVLENSSREDKHECPFGRSSIEL → VSMLASLRYCQCRMEFCFPTYAQ
     421-727: Missing.

Note: No experimental confirmation available.
Show »
Length:420
Mass (Da):48,152
Checksum:i46C679F33F7C703F
GO
Isoform 4 (identifier: Q8BPU7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.
     636-642: EVLELAF → VWFSKSL
     643-727: Missing.

Note: No experimental confirmation available.
Show »
Length:162
Mass (Da):19,044
Checksum:i260CB9B8C7353874
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → E in BAC25925 (PubMed:16141072).Curated
Sequence conflicti315 – 3151P → H in BAC25925 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 480480Missing in isoform 2 and isoform 4. 2 PublicationsVSP_007481Add
BLAST
Alternative sequencei398 – 42023IVLEN…SSIEL → VSMLASLRYCQCRMEFCFPT YAQ in isoform 3. 1 PublicationVSP_007482Add
BLAST
Alternative sequencei421 – 727307Missing in isoform 3. 1 PublicationVSP_007483Add
BLAST
Alternative sequencei636 – 6427EVLELAF → VWFSKSL in isoform 4. 1 PublicationVSP_007484
Alternative sequencei643 – 72785Missing in isoform 4. 1 PublicationVSP_007485Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398883 mRNA. Translation: AAL14464.1.
AK028389 mRNA. Translation: BAC25925.1.
AK053306 mRNA. Translation: BAC35336.1.
BC024727 mRNA. Translation: AAH24727.1.
BC031782 mRNA. Translation: AAH31782.1.
CCDSiCCDS26265.1. [Q8BPU7-1]
RefSeqiNP_525027.1. NM_080288.2. [Q8BPU7-1]
NP_932761.1. NM_198093.3. [Q8BPU7-2]
XP_006516610.1. XM_006516547.2. [Q8BPU7-1]
UniGeneiMm.342392.

Genome annotation databases

EnsembliENSMUST00000072519; ENSMUSP00000072334; ENSMUSG00000041112. [Q8BPU7-1]
GeneIDi140580.
KEGGimmu:140580.
UCSCiuc007ppn.3. mouse. [Q8BPU7-1]
uc007ppo.1. mouse. [Q8BPU7-3]
uc007ppq.2. mouse. [Q8BPU7-4]
uc007ppr.3. mouse. [Q8BPU7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398883 mRNA. Translation: AAL14464.1.
AK028389 mRNA. Translation: BAC25925.1.
AK053306 mRNA. Translation: BAC35336.1.
BC024727 mRNA. Translation: AAH24727.1.
BC031782 mRNA. Translation: AAH31782.1.
CCDSiCCDS26265.1. [Q8BPU7-1]
RefSeqiNP_525027.1. NM_080288.2. [Q8BPU7-1]
NP_932761.1. NM_198093.3. [Q8BPU7-2]
XP_006516610.1. XM_006516547.2. [Q8BPU7-1]
UniGeneiMm.342392.

3D structure databases

ProteinModelPortaliQ8BPU7.
SMRiQ8BPU7. Positions 530-727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41244N.
IntActiQ8BPU7. 2 interactions.
MINTiMINT-219471.
STRINGi10090.ENSMUSP00000072334.

PTM databases

iPTMnetiQ8BPU7.
PhosphoSiteiQ8BPU7.

Proteomic databases

EPDiQ8BPU7.
MaxQBiQ8BPU7.
PaxDbiQ8BPU7.
PRIDEiQ8BPU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072519; ENSMUSP00000072334; ENSMUSG00000041112. [Q8BPU7-1]
GeneIDi140580.
KEGGimmu:140580.
UCSCiuc007ppn.3. mouse. [Q8BPU7-1]
uc007ppo.1. mouse. [Q8BPU7-3]
uc007ppq.2. mouse. [Q8BPU7-4]
uc007ppr.3. mouse. [Q8BPU7-2]

Organism-specific databases

CTDi9844.
MGIiMGI:2153044. Elmo1.

Phylogenomic databases

eggNOGiKOG2999. Eukaryota.
ENOG410XPKN. LUCA.
GeneTreeiENSGT00390000014155.
HOGENOMiHOG000252986.
HOVERGENiHBG051463.
InParanoidiQ8BPU7.
KOiK12366.
OMAiEMSHILA.
OrthoDBiEOG7D85VW.
PhylomeDBiQ8BPU7.
TreeFamiTF312966.

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi369899.
PROiQ8BPU7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BPU7.
GenevisibleiQ8BPU7. MM.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR030715. ELMO1.
IPR006816. ELMO_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR12771:SF23. PTHR12771:SF23. 1 hit.
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
PF16457. PH_12. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS51335. ELMO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-727 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Eye, Mammary tumor and Retina.
  4. "BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module."
    Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.
    Nature 450:430-434(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADGRB1 AND DOCK1.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung, Spleen and Testis.

Entry informationi

Entry nameiELMO1_MOUSE
AccessioniPrimary (citable) accession number: Q8BPU7
Secondary accession number(s): Q8BSY9, Q8K2C5, Q91ZU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: May 11, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.