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Database: UniProt
Entry: A0A091GJP4_9AVES
LinkDB: A0A091GJP4_9AVES
Original site: A0A091GJP4_9AVES 
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}.
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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
//
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