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)

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8BYZ7

Entry ID Method Resolution Chain Position Source
AF-Q8BYZ7-F1 Predicted AlphaFoldDB

39 variants for Q8BYZ7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389007503 2 A>E No EVA
rs3389008117 12 V>D No EVA
rs3398635865 26 Q>L No EVA
rs3389003048 40 A>V No EVA
rs3389000250 71 N>K No EVA
rs3389000173 80 A>V No EVA
rs3399470240 82 D>E No EVA
rs3399377600 153 L>P No EVA
rs3398635883 157 G>R No EVA
rs3389000210 173 I>L No EVA
rs3389003050 220 L>V No EVA
rs3389003068 241 G>R No EVA
rs3389006551 267 I>F No EVA
rs3389006486 284 V>L No EVA
rs3389006309 304 Y>H No EVA
rs3389011967 313 Q>E No EVA
rs3388998555 325 E>K No EVA
rs3389011885 333 A>G No EVA
rs248550917 360 R>H No EVA
rs3399470242 361 V>G No EVA
rs3399557973 363 P>A No EVA
rs3399796026 365 L>P No EVA
rs3399082147 367 A>V No EVA
rs3389003402 380 S>N No EVA
rs3388976129 441 E>K No EVA
rs3388981911 457 M>K No EVA
rs3389000195 477 R>H No EVA
rs3413053031 501 V>M No EVA
rs234561437 514 G>C No EVA
rs3389006339 539 R>L No EVA
rs3389011944 576 G>W No EVA
rs263554355 583 K>N No EVA
rs3547045793 635 G>R No EVA
rs3388986629 638 E>K No EVA
rs3389008169 659 S>R No EVA
rs3388976128 668 S>N No EVA
rs3389000258 683 T>I No EVA
rs3388981980 712 C>* No EVA
rs233566897 718 T>I No EVA

No associated diseases with Q8BYZ7

7 regional properties for Q8BYZ7

Type Name Position InterPro Accession
domain Zinc finger, TRAF-type 151 - 192 IPR001293-1
domain Zinc finger, TRAF-type 204 - 261 IPR001293-2
domain MATH/TRAF domain 350 - 499 IPR002083
conserved_site Zinc finger, RING-type, conserved site 85 - 94 IPR017907
domain TNF receptor-associated factor 6, C3HC3D-type RING zinc finger 67 - 124 IPR027139
domain TNF receptor-associated factor 6, MATH domain 351 - 500 IPR037309
domain TNF receptor-associated factor 6, zinc finger 2 157 - 183 IPR041310

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
Q8BPU7 Elmo1 Engulfment and cell motility protein 1 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
MAPPRNVVKI AVQMSDAIPQ LIQLDQAKPL ATVLKEVCDA WSLTHPEHYA LQFADGHRKY
70 80 90 100 110 120
ITENNRLEIK NGSILCLSTA PDLKAQQLLG RLQNTSREGC CEVLRNLVLL ASDMTFAQEV
130 140 150 160 170 180
ISRDGLQKLS TIIENGDDLG EMLALGLRAF LELMEHGVVS WETLSISFVR KVISYVNMNL
190 200 210 220 230 240
MDASVQPLAL RLLESVTLSS PALGQLVKSE VPLDRLLVHL QVMNHQLQTK AMALLTALLQ
250 260 270 280 290 300
GASPTERKEM LDHLWKKNLR QFIYKNIIHS ATPMGDEMAH HLYVLQALTL GLLEPRMRTP
310 320 330 340 350 360
LDPYSQEQRD QLQALRQAAF EPEGESLGTG LSADRRRSLC VREFRKLGFS NSNPAQDLER
370 380 390 400 410 420
VPPGLLALDN MLYFSRHAPS AYSRFVLENS SREDKHECPF ARSSIQLTAL LCELLRVGEP
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 GAKPPTLESL PEQLPVADIR
610 620 630 640 650 660
ALLMGKDCPH VREKGSGKQN KDLYELAFSI SYDHGEEEAY LNFIAPSKRD FYLWTDGLSA
670 680 690 700 710
LLGSTMGSEL TRLDLEQLLT METKLRLLEL ENVPIPEQPP PVPPPPTNFN FCYDYSITEP