ID   A0A3Q0TBT2_AMPCI        Unreviewed;       701 AA.
AC   A0A3Q0TBT2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Engulfment and cell motility 2 {ECO:0000313|Ensembl:ENSACIP00000029531.1};
GN   Name=ELMO2 {ECO:0000313|Ensembl:ENSACIP00000029531.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000029531.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000029531.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3Q0TBT2; -.
DR   STRING; 61819.ENSACIP00000029531; -.
DR   Ensembl; ENSACIT00000030310.1; ENSACIP00000029531.1; ENSACIG00000022851.1.
DR   GeneTree; ENSGT00940000159236; -.
DR   OMA; XDMANAF; -.
DR   Proteomes; UP000261340; 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   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          307..466
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
SQ   SEQUENCE   701 AA;  80134 MW;  17661566ABB55FE9 CRC64;
     MPPPADIVKV AIEWPGANAQ LIEMDQKRPL SSIIREVCDG WSLSGSEQFA LRYADGPQLY
     ITEQSRGDIK NGTILRLAIS PARAARQLLE RIQSHGIDAR LEALKELAKL SADPTFAAEF
     INMEGIGTLA RLVESGTHFG EMLAFTLTAF LELMDHGIVS WDLISLSFIK QIAGYVNQPM
     VDVSILQRSL AILESMVLNS HSLYHRVAQE ITVGQLIGHL QVSNQEIQTY AIALINALFL
     KAPEDRRQEM ASSLAQKHLR SIILNHVIRG NRPIKAEMAH QLYVLQVLTF NLLEERMMTK
     MDPNDQAQRD IIFELRRIAF DGENDPTGTE KRKAMYTKDY KMLGFTNHVN PAMDFTQTPP
     GMLALDNMLY LAKVHQDTYI RIVLENSSRE DKHECPFGRC AIELTRMLCE ILQVGELRNI
     SLACQCFSFR NLFFCLLNKT WKEMRATAED FNKVMQVVRE QITRALAMKP SSIDQLKTKL
     RGLNYSEILR LRQSERMSQD DFQSPPIIEL RERIQPEILE LIKQQRLNRL CEGSCFRKLG
     NRRRQEKFWF CRLSLNHKVL HYGDLDESPQ GEVPFELLSD KIPVSDIKSV VTGKDCPHMK
     EKSALKQNKE VLELAFSVLY DPDETLNFVA PNKYEYCIWT DGLCALLGRE MGSDLTRSDL
     DTLISMEMKL RLLDLENITI PEAPPPVPKE PSSYNFTYNY S
//