ID   A0A3Q1H2E9_9TELE        Unreviewed;       709 AA.
AC   A0A3Q1H2E9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Engulfment and cell motility 2 {ECO:0000313|Ensembl:ENSAPOP00000033927.1};
GN   Name=ELMO2 {ECO:0000313|Ensembl:ENSAPOP00000033927.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000033927.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000033927.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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   AlphaFoldDB; A0A3Q1H2E9; -.
DR   Ensembl; ENSAPOT00000029244.1; ENSAPOP00000033927.1; ENSAPOG00000022894.1.
DR   GeneTree; ENSGT00940000159236; -.
DR   Proteomes; UP000257200; Unplaced.
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:UP000257200};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          305..474
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
SQ   SEQUENCE   709 AA;  81217 MW;  C8E9828A76C881D0 CRC64;
     MPPPADIVKV AIEWPGANAQ LIEMDQKRPL SSIIREVCDG WSLSGSEQFA LRYADGPQLY
     ITEQSRGDIK NGTILRLAIS PGRAARQLLE RIQSHGIDAR LEALKELAKL SADPTFATEF
     INMEGIGTLA RLVESGTHFG EMLAFTLTAF LELMDHGIVS WDLISLSFIK QIAGYVNQPM
     VDVSILQRSL AILESMVLNS HSLYHRVAQE ITVGQLIGHL SNQEIQTYAI ALINALFLKA
     PEDRRQEMAS TLAQKHLRSI ILNHVIRGNR PIKAEMAHQL YVLQVLTFNL LEERMMTKMD
     PNDQAQRDII FELRRIAFDG ENDPTGTEKR KAMYTKDYKM LGFTNHVNPA MDFTQTPPGM
     LALDNMLYLA KVHQDTYIRI VLENSSREDK HECPFGRCAI ELTRMLCEIL QVGELPNEGC
     NDYHPMFFTH DRAWEEFFCV CIQLLNKTWK EMRATAEDFN KVMQVVREQI TRALAMKPSS
     IDQLKNKLRG LNYSEILRLR QSERMSQDDF QSPPIIELRE RIQPEILELI KQQRLNRLCE
     GSCFRKLGNR RRQEKFWFCR LSLNHKVLHY GDLDESPQGE VPFELLSDKI PVSDIKSVVT
     GKDCPHMKEK SALKQNKEVL ELAFSVLYDP DETLNFVAPN KYEYCIWTDG LCALLGREMG
     SDLTRSDLDT LISMEMKLRL LDLENITIPE APPPVPKEPS SYNFTYNYS
//