ID   ELMO3_RAT               Reviewed;         720 AA.
AC   Q499U2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Engulfment and cell motility protein 3;
GN   Name=Elmo3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; CH473972; EDL92366.1; -; Genomic_DNA.
DR   EMBL; BC099761; AAH99761.1; -; mRNA.
DR   RefSeq; NP_001025199.1; NM_001030028.1.
DR   AlphaFoldDB; Q499U2; -.
DR   SMR; Q499U2; -.
DR   STRING; 10116.ENSRNOP00000021362; -.
DR   jPOST; Q499U2; -.
DR   PaxDb; Q499U2; -.
DR   Ensembl; ENSRNOT00000021362; ENSRNOP00000021362; ENSRNOG00000015800.
DR   GeneID; 291962; -.
DR   KEGG; rno:291962; -.
DR   UCSC; RGD:1304734; rat.
DR   CTD; 79767; -.
DR   RGD; 1304734; Elmo3.
DR   eggNOG; KOG2999; Eukaryota.
DR   GeneTree; ENSGT00940000159455; -.
DR   HOGENOM; CLU_023887_0_0_1; -.
DR   InParanoid; Q499U2; -.
DR   OMA; CPHIREK; -.
DR   OrthoDB; 234725at2759; -.
DR   PhylomeDB; Q499U2; -.
DR   PRO; PR:Q499U2; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Proteomes; UP000234681; Chromosome 19.
DR   Bgee; ENSRNOG00000015800; Expressed in jejunum and 19 other tissues.
DR   Genevisible; Q499U2; RN.
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..720
FT                   /note="Engulfment and cell motility protein 3"
FT                   /id="PRO_0000375223"
FT   DOMAIN          307..479
FT                   /note="ELMO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT   DOMAIN          541..663
FT                   /note="PH"
SQ   SEQUENCE   720 AA;  81659 MW;  2F4230B0146340D4 CRC64;
     MAPPRNVVKI AVQMSDAIPQ LIQLDQAKPL ATVLKEVCDT WSLTHPEHYA LQFADGHRKY
     ITENNRSEIK NGSILCLSTA PDLKAQQLLS RLQNASREGC CEVLRNLVPL ASDMTFAQEV
     ISRDGLQKLS TIIENGDDLG EMLALGLRAF LELMEHGVVS WETLSISFVR KVVSYVNMNL
     MDASVQPLAL RLLESVTLSS PTLGQLVKSE VPLDRLLVHL QVMNQQLQTK AMALLTALLQ
     GASPAERKDM LDCLWKKNLR QFIYKNIIHS AAPMGDEMAH HLYVLQALTL GLLEPRMRTP
     LDPYSQEQRE QLQALRQAAF EPDGESLGTG LSADRRRSLC VREFRKLGFS NSSPAQDLER
     VPPGLLALDN MLYFSRHAPS AYSRFVLENS SREDKHECPF ARSSIQLTVL LCELLHVGEP
     CSETAQDFSP MFFSQDHSFH ELFCVAIQLL NKTWKEMRAT QEDFDKVMQV VREQLARTLA
     LKPTSLELFR TKVNALTYGE VLRLRQTERL HQEGTLAPPI LELREKLKPE LMGLIRQQRL
     LRLCEGMLFR KISSRRRQDK LWFCCLSPNH KVLQYGDVEE GANPPTLESL TEQLPVADIR
     ALLMGKDCPH VREKGSGKQN KDLYELAFSI SYDHGEEEAY LNFIAPSKRD FYLWTDGLSA
     LLGSTMGSEQ TRLDLEQLLT METKLRLLEL ENVPIPEHPP PVPPPPTNFN FCYDYSMTEP