ID   A0A3Q1IU25_ANATE        Unreviewed;       628 AA.
AC   A0A3Q1IU25;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Engulfment and cell motility 3 {ECO:0000313|Ensembl:ENSATEP00000022749.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000022749.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000022749.2}
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}.
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DR   AlphaFoldDB; A0A3Q1IU25; -.
DR   Ensembl; ENSATET00000023120.2; ENSATEP00000022749.2; ENSATEG00000015694.2.
DR   GeneTree; ENSGT00940000159455; -.
DR   Proteomes; UP000265040; 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:SF16; ENGULFMENT AND CELL MOTILITY PROTEIN 3; 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:UP000265040};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          221..391
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
SQ   SEQUENCE   628 AA;  72147 MW;  0C6E2310390DF2CB CRC64;
     AIISFGRCAE DLFKGIQNLD SGVRCDSLKE LAGVSTDVTF AQEFISRDGH LLLVKIVEDS
     NDNVIMTHTL LSFMELMDHG IVSWENLSSV FIKKIASFVN TKSTDASIQQ VSLDILESMV
     LSSQSLFLQV KQEVTMERLI AHIQVTNQQI QTKAMALLMA LLQTSGVYER QVLLVYFLQN
     ILHCSSSVQD EMAHYLYVLQ SVTLNHLEPR MKTPLDCYSQ EQRDILHGLR QAAFETESEN
     SLSNERRRSL CAKEFKKLGF SNNSNPGQDL LRAPPGLLAL DTMSYFAMRY PDAYSRFVLE
     NSSREDKHEC PFARSSIELT LILCEILRIG EPPSETGSDY HPIFFSQDRL LEELFCVCIQ
     LLNKTWKEMR ATQEDFDKVM QVVREQITRT LSSKPTSLEF FKSKVNALNY SEILKLRQTE
     RLHQEETLAP PVLELKERLK PELLELIRQQ RLNRLCQGTM FRKITQRRRQ DKLWYCRLSP
     NHKMLHYGDV EEDTDNPPIE TLQMKIPVAD IKGLLTGKDC PHMKENKGKQ NKVLDMAFSI
     TYDVEESSLD FIAPSRTDFC LWTDGLNVLL GREMSSESMR SELEILLSME IKLRLLDLEN
     VPIPDSAPVV PKPPSNFNFC YDFSHNEQ
//