Q8BPU7

SS
Gene name
Elmo1
Protein name
Engulfment and cell motility protein 1
Names
Protein ced-12 homolog
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:140580
EC number
Protein Class

Descriptions

Engulfment and cell motility (ELMO) proteins bind a subset of DOCK members and act as critical regulators of Rac signaling. Although formation of a DOCK180/ELMO complex is not essential for Rac1 activation, ELMO mutants deficient in binding to DOCK180 are unable to promote cytoskeleton remodeling. ELMO facilitates the co-localization of DOCK180 and Rac at the membrane and therefore indirectly endorses the Rac GEF activity of this complex. ELMO is autoinhibited via an intramolecular interaction between the N-terminal Armadillo repeats (ARMs, renamed ELMO Inhibitory Domain (EID)) and the C-terminal region termed the ELMO Autoregulatory Domain (EAD). Relief of ELMO autoinhibition occurs through cell stimulation and ELMO Ras-binding domain (RBD) engagement (via a GTPase or other unknown binding partner). Cell stimulation leads to ELMO conformational changes that facilitate DOCK180/ELMO interactions, which in turn enhances the Rac GEF activity in DOCK180.

Autoinhibitory domains (AIDs)

113-315 (Armadillo repeats, EID) SS

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

676-707 (ELMO autoregulatory domain, EAD) SS

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8BPU7

Entry ID Method Resolution Chain Position Source
AF-Q8BPU7-F1 Predicted AlphaFoldDB

41 variants for Q8BPU7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389256351 77 L>F No EVA
rs3389273762 78 T>N No EVA
rs3389230850 114 V>A No EVA
rs3389230839 115 T>S No EVA
rs3389269528 121 I>T No EVA
rs3389282794 124 D>E No EVA
rs3389239607 145 K>T No EVA
rs3389267536 160 T>A No EVA
rs3389270142 161 A>T No EVA
rs3389270184 174 D>G No EVA
rs3389244698 177 S>* No EVA
rs3389267482 186 S>I No EVA
rs3389282748 193 I>K No EVA
rs3389244638 196 S>T No EVA
rs3389202036 227 Q>* No EVA
rs3389239575 242 Y>* No EVA
rs3389273975 269 K>E No EVA
rs3389271266 305 L>M No EVA
rs3389264029 319 A>V No EVA
rs3389279581 330 I>V No EVA
rs3389273983 331 A>D No EVA
rs3389230865 371 F>L No EVA
rs3389273739 373 Q>* No EVA
rs3404050201 392 Q>P No EVA
rs3402546706 394 A>V No EVA
rs3403949915 395 Y>C No EVA
rs3389279559 399 V>M No EVA
rs3389239599 403 S>I No EVA
rs3389244675 420 L>M No EVA
rs3389264054 420 L>P No EVA
rs3389244652 458 I>F No EVA
rs3403955389 537 K>* No EVA
rs3403952720 537 K>M No EVA
rs3404051938 539 K>N No EVA
rs3403963238 540 I>N No EVA
rs3389286876 624 H>Y No EVA
rs3389273803 645 L>I No EVA
rs3389279624 687 D>N No EVA
rs3389269503 707 P>L No EVA
rs3389269490 716 E>D No EVA
rs240257544 728 N>C No EVA

No associated diseases with Q8BPU7

3 regional properties for Q8BPU7

Type Name Position InterPro Accession
domain Pleckstrin homology domain 548 - 674 IPR001849
domain ELMO domain 303 - 492 IPR006816
domain ELMO, armadillo-like helical domain 115 - 280 IPR024574

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell membrane
  • Translocation to plasma membrane seems to be mediated by DOCK1 and CRK
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
guanyl-nucleotide exchange factor complex A protein complex that stimulates the exchange of guanyl nucleotides associated with a GTPase.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.

8 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
actin filament organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
actin filament-based process Any cellular process that depends upon or alters the actin cytoskeleton, that part of the cytoskeleton comprising actin filaments and their associated proteins.
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
cell motility Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
phagocytosis A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles.
phagocytosis, engulfment The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms
Rac protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Rac family of proteins switching to a GTP-bound active state.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A4FUD6 ELMO2 Engulfment and cell motility protein 2 Bos taurus (Bovine) SS
Q96BJ8 ELMO3 Engulfment and cell motility protein 3 Homo sapiens (Human) SS
Q96JJ3 ELMO2 Engulfment and cell motility protein 2 Homo sapiens (Human) SS
Q92556 ELMO1 Engulfment and cell motility protein 1 Homo sapiens (Human) EV
Q8BYZ7 Elmo3 Engulfment and cell motility protein 3 Mus musculus (Mouse) SS
Q8BHL5 Elmo2 Engulfment and cell motility protein 2 Mus musculus (Mouse) SS
Q499U2 Elmo3 Engulfment and cell motility protein 3 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MPPPSDIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY
70 80 90 100 110 120
ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF
130 140 150 160 170 180
INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF
190 200 210 220 230 240
IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGTDQEIQ
250 260 270 280 290 300
TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRYIILTHVI RAQRAINNEM AHQLYVLQVL
310 320 330 340 350 360
TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG
370 380 390 400 410 420
FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL
430 440 450 460 470 480
TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV
490 500 510 520 530 540
MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI
550 560 570 580 590 600
QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP
610 620 630 640 650 660
HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH
670 680 690 700 710 720
EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY
DFVYDCN