Q499U2

SS
Gene name
Elmo3
Protein name
Engulfment and cell motility protein 3
Names
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:291962
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)

113-303 (Armadillo repeats, EID) SS

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

665-696 (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 Q499U2

Entry ID Method Resolution Chain Position Source
AF-Q499U2-F1 Predicted AlphaFoldDB

1 variants for Q499U2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs8148600 691 E>* No EVA

No associated diseases with Q499U2

8 regional properties for Q499U2

Type Name Position InterPro Accession
domain CDC48, N-terminal subdomain 8 - 92 IPR003338
domain AAA+ ATPase domain 257 - 404 IPR003593-1
domain AAA+ ATPase domain 540 - 676 IPR003593-2
domain ATPase, AAA-type, core 261 - 401 IPR003959-1
domain ATPase, AAA-type, core 544 - 670 IPR003959-2
conserved_site ATPase, AAA-type, conserved site 372 - 390 IPR003960
domain CDC48, domain 2 117 - 188 IPR004201
domain AAA ATPase, AAA+ lid domain 428 - 464 IPR041569

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 GO annotations of molecular function

Name Definition
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.

4 GO annotations of biological process

Name Definition
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.
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.

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
Q92556 ELMO1 Engulfment and cell motility protein 1 Homo sapiens (Human) EV
Q96JJ3 ELMO2 Engulfment and cell motility protein 2 Homo sapiens (Human) SS
Q96BJ8 ELMO3 Engulfment and cell motility protein 3 Homo sapiens (Human) SS
Q8BHL5 Elmo2 Engulfment and cell motility protein 2 Mus musculus (Mouse) SS
Q8BPU7 Elmo1 Engulfment and cell motility protein 1 Mus musculus (Mouse) SS
Q8BYZ7 Elmo3 Engulfment and cell motility protein 3 Mus musculus (Mouse) SS
10 20 30 40 50 60
MAPPRNVVKI AVQMSDAIPQ LIQLDQAKPL ATVLKEVCDT WSLTHPEHYA LQFADGHRKY
70 80 90 100 110 120
ITENNRSEIK NGSILCLSTA PDLKAQQLLS RLQNASREGC CEVLRNLVPL ASDMTFAQEV
130 140 150 160 170 180
ISRDGLQKLS TIIENGDDLG EMLALGLRAF LELMEHGVVS WETLSISFVR KVVSYVNMNL
190 200 210 220 230 240
MDASVQPLAL RLLESVTLSS PTLGQLVKSE VPLDRLLVHL QVMNQQLQTK AMALLTALLQ
250 260 270 280 290 300
GASPAERKDM LDCLWKKNLR QFIYKNIIHS AAPMGDEMAH HLYVLQALTL GLLEPRMRTP
310 320 330 340 350 360
LDPYSQEQRE QLQALRQAAF EPDGESLGTG LSADRRRSLC VREFRKLGFS NSSPAQDLER
370 380 390 400 410 420
VPPGLLALDN MLYFSRHAPS AYSRFVLENS SREDKHECPF ARSSIQLTVL LCELLHVGEP
430 440 450 460 470 480
CSETAQDFSP MFFSQDHSFH ELFCVAIQLL NKTWKEMRAT QEDFDKVMQV VREQLARTLA
490 500 510 520 530 540
LKPTSLELFR TKVNALTYGE VLRLRQTERL HQEGTLAPPI LELREKLKPE LMGLIRQQRL
550 560 570 580 590 600
LRLCEGMLFR KISSRRRQDK LWFCCLSPNH KVLQYGDVEE GANPPTLESL TEQLPVADIR
610 620 630 640 650 660
ALLMGKDCPH VREKGSGKQN KDLYELAFSI SYDHGEEEAY LNFIAPSKRD FYLWTDGLSA
670 680 690 700 710
LLGSTMGSEQ TRLDLEQLLT METKLRLLEL ENVPIPEHPP PVPPPPTNFN FCYDYSMTEP