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Database: UniProt
Entry: A0A091E9Q3_CORBR
LinkDB: A0A091E9Q3_CORBR
Original site: A0A091E9Q3_CORBR 
ID   A0A091E9Q3_CORBR        Unreviewed;       701 AA.
AC   A0A091E9Q3;
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:KFO53189.1};
DE   Flags: Fragment;
GN   ORFNames=N302_00249 {ECO:0000313|EMBL:KFO53189.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO53189.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO53189.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO53189.1};
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; KK717962; KFO53189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091E9Q3; -.
DR   STRING; 85066.A0A091E9Q3; -.
DR   Proteomes; UP000052976; 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:UP000052976};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          311..485
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
FT   NON_TER         701
FT                   /evidence="ECO:0000313|EMBL:KFO53189.1"
SQ   SEQUENCE   701 AA;  80599 MW;  52CBC9D37DA53281 CRC64;
     MPPPSDIVKV AVEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
     ITEQTRCDIK NGTILQLAVS PSRAARQLME RIQSHSMEAR LDAMKELAKL SADVTFATEF
     INMEGITVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQIAGYV
     SQPMVDVSIL QRSLAILESM VLNSQTLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
     ALFLKAPEDK RQEMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER
     MMTKMDPNDQ AQRDIIFELR RIAFDAESDS NTVPGGGTEK RKAMYTKDYK MLGFTNHINP
     AMDFTQTPPG MLALDNMLYL AKFHQDTYIR IVLENSSRED KHECPFGRSA IELTRMLCEI
     LQVGELPNEG RNDYHPMFFT HDRAFEELFA ICIQLLNKTW KEMRATAEDF NKVMQVVREQ
     ITRALPSKPN SLDQFKSKLR SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL
     IKQQRLNRLC EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLEDNAQG EVTFESLQEK
     IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP NKYEYCIWID
     GLNALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP E
//
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