ID A0A091GJP4_9AVES Unreviewed; 724 AA.
AC A0A091GJP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Engulfment and cell motility protein 2 {ECO:0000313|EMBL:KFO74302.1};
GN ORFNames=N303_13184 {ECO:0000313|EMBL:KFO74302.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO74302.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74302.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74302.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL447510; KFO74302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GJP4; -.
DR STRING; 55661.A0A091GJP4; -.
DR Proteomes; UP000053760; 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 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:UP000053760};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 315..489
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 724 AA; 83308 MW; 0A6F6F9A50538507 CRC64;
MPPPSDIVKV AVEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
ITEQTRCDIK NGTILQLAVS PSRAARQLME RIQSHSMEAR LDAMKELAKL SADVTFATEF
INMEGITMLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQVSLDR
KGYVSQPMVD VSILQRSLAI LESMVLNSQT LYQKIAEEIT VGQLISHLQV SNQEIQTYAI
ALINALFLKA PEDKRQEMAN AFAQKHLRSI ILNHVIRGNR PIKTEMAHQL YVLQVLTFNL
LEERMMTKMD PNDQAQRDII FELRRIAFDA ESDSNTVPGS GTEKRKAMYT KDYKMLGFTN
HINPAMDFTQ TPPGMLALDN MLYLAKFHQD TYIRIVLENS SREDKHECPF GRSAIELTRM
LCEILQVGEL PNEGRNDYHP MFFTHDRAFE ELFAICIQLL NKTWKEMRAT AEDFNKVMQV
VREQITRALP SKPNSLDQFK SKLRSLSYSE ILRLRQSERM SQDDFQSPPI VELREKIQPE
ILELIKQQRL NRLCEGSSFR KIGNRRRQER FWYCRLALNH KVLHYGDLED NAQGEVTFES
LQEKIPVADI KAVVTGKDCP HMKEKSALKQ NKEVLELAFS ILYDPDETLN FIAPNKYEYC
IWIDGLNALL GKDMSSELTK SDLDTLLSME MKLRLLDLEN IQIPEAPPPI PKEPSSYDFV
YHYG
//