ID   ELMO3_BOVIN             Reviewed;         652 AA.
AC   A6QR40;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Engulfment and cell motility protein 3;
GN   Name=ELMO3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Probably interacts directly with the SH3-domain of DOCK1 via
CC       its SH3-binding site. Part of a complex with DOCK1 and RAC1 (By
CC       similarity). Interacts with ADGRB3 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q96BJ8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC150105; AAI50106.1; -; mRNA.
DR   RefSeq; NP_001095561.1; NM_001102091.1.
DR   AlphaFoldDB; A6QR40; -.
DR   SMR; A6QR40; -.
DR   STRING; 9913.ENSBTAP00000001696; -.
DR   PaxDb; A6QR40; -.
DR   PRIDE; A6QR40; -.
DR   Ensembl; ENSBTAT00000001696; ENSBTAP00000001696; ENSBTAG00000001286.
DR   GeneID; 525427; -.
DR   KEGG; bta:525427; -.
DR   CTD; 79767; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001286; -.
DR   VGNC; VGNC:28440; ELMO3.
DR   eggNOG; KOG2999; Eukaryota.
DR   GeneTree; ENSGT00940000159455; -.
DR   HOGENOM; CLU_023887_0_0_1; -.
DR   InParanoid; A6QR40; -.
DR   OMA; CPHIREK; -.
DR   OrthoDB; 234725at2759; -.
DR   TreeFam; TF312966; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000001286; Expressed in urinary bladder and 99 other tissues.
DR   ExpressionAtlas; A6QR40; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR030719; ELMO3.
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:SF16; PTHR12771:SF16; 1.
DR   Pfam; PF11841; DUF3361; 1.
DR   Pfam; PF04727; ELMO_CED12; 1.
DR   Pfam; PF16457; PH_12; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51335; ELMO; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Phagocytosis; Reference proteome; SH3-binding.
FT   CHAIN           1..652
FT                   /note="Engulfment and cell motility protein 3"
FT                   /id="PRO_0000375222"
FT   DOMAIN          307..479
FT                   /note="ELMO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
SQ   SEQUENCE   652 AA;  73958 MW;  6EDFA62032EC82B0 CRC64;
     MAPPRNVVKI AVQMRDAIPQ LIQLDQAKPL AAVLKEVCDA WSLPHSERYA LQFADGHRRY
     ITENNRMEIK NGSILCLSTA PDREAERLLR GLQSESREGR REALRHLLLL APDLTFAREV
     ISRDGLQRLG TIIEDGDDLG EVLALALRAF LELMEHGVVS WETLSIPFVR KVVCYVNMNL
     MDASVQPLAL GLLENVTLSS PTLGQLVKSE VPLDRLLVHL QVMNQQLQTK AMALLTALLQ
     GATPAERKHM LDYLWQRNLR QFIYKNIIHS AAPLGDEMAH HLYVLQALML GLLEPRMRTP
     LDPYSQEQRE QLQALRQAAF EPEGESVGAG LSADRRRSLC AREFRKLGFS NSNPAQDLER
     VPPGLLALDN MLYFSRQAPS AYSRFVLENS SREDKHECPF ARSSIQLTVL LCDLLHVGEP
     CSETAQDFSP MFFGQDQSFH ELFCVSIQLL NKTWKEMRAT QEDFDKVMQV VREQLARTLA
     LKPSSLELFR TKVNALTYGE VLRLRQTERL HQEGTLAPPI LELREKLKPE LMGLIRQQRL
     LRLCEGTLFH KISSRRRQDK LWFCCLSPNH KVLQYGDVEE GVGPPTPESL PEQLPVADIR
     ALLTGKDCPH VREKGSGKQN KDVCELAFSV SYDHGEEEAY LNFIAPSKRE MG