Q8BHL5

SS
Gene name
Elmo2 (Kiaa1834)
Protein name
Engulfment and cell motility protein 2
Names
Protein ced-12 homolog A
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:140579
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)

113-319 (Armadillo repeats, EID) SS

Target domain

1-113 (Ras-binding domain)

Relief mechanism

Partner binding

Assay

681-712 (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

2 structures for Q8BHL5

Entry ID Method Resolution Chain Position Source
6UKA X-ray 240 A B 1-80 PDB
AF-Q8BHL5-F1 Predicted AlphaFoldDB

27 variants for Q8BHL5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388612113 14 W>R No EVA
rs3388614122 16 G>D No EVA
rs3388596380 29 P>S No EVA
rs3388614155 36 E>V No EVA
rs3388613347 85 A>T No EVA
rs3388603139 96 S>T No EVA
rs3388610499 105 K>N No EVA
rs3392508056 152 T>N No EVA
rs3388615470 185 V>I No EVA
rs3392342825 221 I>L No EVA
rs3388603132 255 H>L No EVA
rs229728771 345 V>I No EVA
rs3388596365 384 L>M No EVA
rs3411138623 406 E>K No EVA
rs3388614163 422 A>G No EVA
rs3388608559 487 Q>L No EVA
rs28266076 545 I>V No EVA
rs3540874427 555 Q>R No EVA
rs48338777 559 N>S No EVA
rs3388614129 566 S>I No EVA
rs3388614165 608 S>Y No EVA
rs3388605328 644 E>G No EVA
rs3388603939 649 I>V No EVA
rs3388612100 663 N>S No EVA
rs3388610429 683 S>P No EVA
rs3388612082 683 S>Y No EVA
rs3388610503 703 L>I No EVA

No associated diseases with Q8BHL5

3 regional properties for Q8BHL5

Type Name Position InterPro Accession
domain Pleckstrin homology domain 553 - 679 IPR001849
domain ELMO domain 307 - 497 IPR006816
domain ELMO, armadillo-like helical domain 115 - 284 IPR024574

Functions

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

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

2 GO annotations of molecular function

Name Definition
receptor tyrosine kinase binding Binding to a receptor that possesses protein tyrosine kinase activity.
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.

5 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 chemotaxis The directed movement of a motile cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
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
Q96BJ8 ELMO3 Engulfment and cell motility protein 3 Homo sapiens (Human) SS
Q96JJ3 ELMO2 Engulfment and cell motility protein 2 Homo sapiens (Human) 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
Q499U2 Elmo3 Engulfment and cell motility protein 3 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
70 80 90 100 110 120
VTEQTRNDIK NGTILQLAVS PSRAARQLME RTQSSSMETR LDAMKELAKL SADVTFATEF
130 140 150 160 170 180
INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSV TFIKQIAGYV
190 200 210 220 230 240
SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
250 260 270 280 290 300
ALFLKAPEDK RQDKHLNPLD LPVTDMANAF AQKHLRSIIL NHVIRGNRPI KTEMAHQLYV
310 320 330 340 350 360
LQVLTFNLLE ERMMTKMDPN DQAQRDIIFE LRRIAFDAES DPSNVPGSGT EKRKAMYTKD
370 380 390 400 410 420
YKMLGFTNHI NPALDFTQTP PGMLALDNML YLAKVHQDTY IRIVLENSSR EDKHECPFGR
430 440 450 460 470 480
SAIELTKMLC EILQVGELPN EGRNDYHPMF FTHDRAFEEL FGICIQLLNK TWKEMRATAE
490 500 510 520 530 540
DFNKVMQVVR EQITRALPSK PNSLDQFKSK LRSLSYSEIL RLRQSERMSQ DDFQSPPIVE
550 560 570 580 590 600
LREKIQPEIL ELIKQQRLNR LCEGSSFRKI GNRRRQERFW HCRLALNHKV LHYGDLDDNP
610 620 630 640 650 660
QGEVTFESLQ EKIPVADIKA IVTGKDCPHM KEKSALKQNK EVLELAFSIL YDPDETLNFI
670 680 690 700 710 720
APNKYEYCIW IDGLSALLGK DMSSELTKSD LDTLLSMEMK LRLLDLENIQ IPEAPPPVPK
730
EPSSYDFVYH YG