ID A0A2K6MN37_RHIBE Unreviewed; 718 AA.
AC A0A2K6MN37;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Engulfment and cell motility 2 {ECO:0000313|Ensembl:ENSRBIP00000037200.1};
GN Name=ELMO2 {ECO:0000313|Ensembl:ENSRBIP00000037200.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000037200.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000037200.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000037200.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Acts in association
CC with DOCK1 and CRK. Was initially proposed to be required in complex
CC with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine
CC nucleotide exchange factor (GEF) activity of DOCK1.
CC {ECO:0000256|ARBA:ARBA00024863}.
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DR AlphaFoldDB; A0A2K6MN37; -.
DR STRING; 61621.ENSRBIP00000037200; -.
DR Ensembl; ENSRBIT00000061212.1; ENSRBIP00000037200.1; ENSRBIG00000042187.1.
DR GeneTree; ENSGT00940000159236; -.
DR OMA; XDMANAF; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR CDD; cd13359; PH_ELMO1_CED-12; 1.
DR Gene3D; 6.10.250.810; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12771; ENGULFMENT AND CELL MOTILITY; 1.
DR PANTHER; PTHR12771:SF8; ENGULFMENT AND CELL MOTILITY PROTEIN 2; 1.
DR Pfam; PF11841; ELMO_ARM; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 309..483
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 718 AA; 82580 MW; 649C847E0C3619F5 CRC64;
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
ITEQVSTGRG KITSRAARQL MERTQSSNME TRLDAMKELA KLSADVTFAT EFINMDGIIV
LTRLVESGTK LLSHYSEMLA FTLTAFLELM DHGIVSWDMV SITFIKQIAG YVSQPMVDVS
ILQRSLAILE SMVLNSQSLY QKIAEEITVG QLISHLQVSN QEIQTYAIAL INALFLKAPE
DKRQVCGCLF IYFIWAFLRE FSPHILLHVI RGNRPIKTEM AHQLYVLQVL TFNLLEERMM
TKMDPNDQAQ RDIIFELRRI AFDAESDPSN VPGSGTEKRK AMYTKDYKML GFTNHINPAM
DFTQTPPGML ALDNMLYLAK VHQDTYIRIV LENSSREDKH ECPFGRSAIE LTKMLCEILQ
VGELPNEGRN DYHPMFFTHD RAFEELFGIC IQLLNKTWKE MRATAEDFNK VMQVVREQIT
RALPSKPNSL DQFKSKLRSL SYSEILRLRQ SERMSQDDFQ SPPIVELREK IQPEILELIK
QQRLNRLCEG SSFRKIGNRR RQERFWYCRL ALNHKVLHYG DLDDNPQGEV TFESLQEKIP
VADIKAIVTG KDCPHMKEKS ALKQNKEVLE LAFSILYDPD ETLNFIAPNK YEYCIWIDGL
SALLGKDMSS ELTKSDLDTL LSMEMKLRLL DLENIQIPEA PPPIPKEPSS YDFVYHYG
//