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Database: UniProt
Entry: A0A3Q3DZU6_9LABR
LinkDB: A0A3Q3DZU6_9LABR
Original site: A0A3Q3DZU6_9LABR 
ID   A0A3Q3DZU6_9LABR        Unreviewed;       715 AA.
AC   A0A3Q3DZU6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Engulfment and cell motility protein 3-like {ECO:0000313|Ensembl:ENSLBEP00000000197.1};
GN   Name=ELMO3 {ECO:0000313|Ensembl:ENSLBEP00000000197.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000000197.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000000197.1}
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}.
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DR   AlphaFoldDB; A0A3Q3DZU6; -.
DR   STRING; 56723.ENSLBEP00000000197; -.
DR   Ensembl; ENSLBET00000000202.1; ENSLBEP00000000197.1; ENSLBEG00000000163.1.
DR   GeneTree; ENSGT00940000159455; -.
DR   InParanoid; A0A3Q3DZU6; -.
DR   OrthoDB; 4872856at2759; -.
DR   Proteomes; UP000261660; 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:UP000261660};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          307..477
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
SQ   SEQUENCE   715 AA;  81869 MW;  2584FFEAB542B2D1 CRC64;
     MPQQKDIVKI AIQMPGAYPQ LIQLDQKKPL SAVIKEVCDG WNLPGPDNYA LQNADGVQTY
     ITESNRLDIK NGCILRLTKA PGRCAEDLFK GIQSSDSGVR CDSLKELAST STDVTFAQEF
     ISRDGHLLLV KIVEDSNESN VIMTHTLTGF MELMDHGIVS WENLSSVFIK KIASFVNAKP
     TDASIQQVSL DILESMVLSS HSLFLQVKQE VTMERLIAHL QVTNQQIQTK AMALLMALLQ
     TAGDSDRQDM FAFLSKKNLR QYIYKNIIHS SGAVQDEMAH YLYVLQSVTL NHLEPRMRTP
     LDCYSQEQRD ILHGLRQAAF ETESENSLSH ERRRSLCAKE FKKLGFSNNS NPGQDLVRTP
     PGLLALDTMF YFAARYPDAY SRFVLENSSR EDKHECPFAR SSIQLTLILC EILRIGEPPS
     ETGSHYHPIF FSQDRLMEEL FCVCIQLLNK TWKEMRATQE DFDKVMQVVR EQITRTLSSK
     PTSLELFKNK VNALNYSEIL KLRQTERLHQ EETLAPPVLE LKERLKPELL ELIRQQRLNR
     LCQGTMFRKI SSRRRQDKLW YCRLSPNHKM LHYGDVEEDT ENPPIESLQE KIPVADIKGL
     LTGKDCPHMK EHKGKQNKEV LDQAFSISYD VEEYSLNFIA PSRTDFCLWT DGLSVLLGRE
     MSSESMRSEL EILLSMEIKL RLLDLENVPI PDSAPVIPKP PSNYNFCYDF SQTEQ
//
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