ID   A0A3B3Y7Y2_9TELE        Unreviewed;       695 AA.
AC   A0A3B3Y7Y2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000023200.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000023200.1}
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}.
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DR   AlphaFoldDB; A0A3B3Y7Y2; -.
DR   STRING; 48701.ENSPMEP00000023200; -.
DR   Ensembl; ENSPMET00000010775.1; ENSPMEP00000023200.1; ENSPMEG00000004679.1.
DR   Proteomes; UP000261480; 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          298..460
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
FT   REGION          676..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  79615 MW;  9C2710128238B68B CRC64;
     MPPPADIVKV AIEWPGANAQ LIEMDQKRPL SSIIREVCDG WSLSGSEQFA LRYADGPQLY
     ITEQSRGDIK NGTILRLAIS PARAARQLLE RIQSHGIDAR LEALKELAKL SADPTFAAEF
     INMEGIGTLA RLVESGTHFF SPSFGEMLAF TLTAFLELMD HGIVSWDLIS LSFIKQIAGY
     VNQPMVDVSI LQRSLAILES MVLNSHSLYH RVAQEITVGQ LIGHLQVSNQ EIQTYAIALI
     NALFLKAPED RRQEMASTLA QKHLRSIILN HVIRGNRPIK AEMAHQLYVL QVLTFNLLEE
     RMMTKMDPND QAQRDIIFEL RRIAFDGDTD PTGTEKRKAM YTKDYKMLGF TVTWPGLNLS
     FCLWQIVLEN SSREDKHECP FGRCAIELTR MLCEILQVGE LPNEGCNDYH PMFFTHDRAW
     EEFFCVCIQL LNKTWKEMRA TAEDFNKVMQ VVREQITRAL AMKPSSIDQL KNKLRGLSYS
     EILRLRQSER MSQDDFQSPP IIELRERIQP EILELIKQQR LNRLCEGSCF RKLGNRRRQE
     KFWFCRLSLN HKVLHYGDLE ESPQGEVPFE LLSDKIPVSD IKSVLTGKDC PHMKEKSALK
     QNKEVLELAF SILYDPDETL NFVAPNKYEY CIWTDGLCAL LGREMGSDLT RSDLDTLISM
     EMKLRLLDLE NITIPEAPPP VPKEPSSYNF SYNYS
//