ID A0A1C7MCG8_GRIFR Unreviewed; 761 AA.
AC A0A1C7MCG8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Engulfment and cell motility protein 3 {ECO:0000313|EMBL:OBZ74056.1};
GN Name=Elmo3 {ECO:0000313|EMBL:OBZ74056.1};
GN ORFNames=A0H81_06169 {ECO:0000313|EMBL:OBZ74056.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ74056.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ74056.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ74056.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBZ74056.1}.
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DR EMBL; LUGG01000006; OBZ74056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MCG8; -.
DR STRING; 5627.A0A1C7MCG8; -.
DR OMA; XDMANAF; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000092993; Unassembled WGS sequence.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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:SF56; CED-12; 1.
DR PANTHER; PTHR12771; ENGULFMENT AND CELL MOTILITY; 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 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:UP000092993};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 383..539
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 761 AA; 87019 MW; 0C89D59CA53573B0 CRC64;
MANKRPDDCH DEKKLNIVRK VGVGKRRGKS VLSFLLKYRT HCISFRSQEA PGSYFLHLSR
YHHSLCLQTH RLPRMSHESL PPLHCPHPRP TEGLTVRARI EPTLTVDDVI RQLCVSLKLK
DPAVMYALRD ENDELVTNDN LRKKIKGKIN LKLVNAPALE AAEIVEKLGA KDARLGLALT
SLRKLIREEQ FANEFLNRDG LRELIEVINT SHGNVLAYAL TAMQNLMELD YGWDNLDNVF
ILKIVQILSS ESSLINAASS SRGPPSPPPG SVYRYGFDVV FEQMRKEKRL LETVVSRLGS
ADTTMALYSM MLINSLMAHA SDPRWDEFIA ELERLNVRKA VIRLMSSHTI EDLTSCILDF
QANMVRVAFR KKMTLVEPDF EPLHDSALKY IWTNSKLQEE REDAITAVKW RKIGFDSEDI
GQEFREVGVL GLDCLKHVVA TDPDYWAKVV QEQISRPEER RCPIAKASNE VADLLSEHWA
IYAPGYSTST TFQPFFLNFY KVHALATHFF LRMWNESGAS RGDFPRLVAL TRSQVNVALR
RENIRPWHEV EQDFLECEYR AVRDRQMQEL EMEDDIMSKI PIRNMRAKLY KESFEFVRQQ
RIHCLLEGAW FMNGIPLATT VPRDTIRRPT RPWRFIRLDN GMKYLHYVDS AVKFPVRKGL
EDLPERIDVS LISEVATGTC APFPNFLREP TDVTLGSSSP ISPQTSRETE VFVQALTEIG
LKIKLLDLSG EKVEIPSGLV AGPPPTNSDF FFSDLSYDTQ G
//