ID   ELMO2_BOVIN             Reviewed;         720 AA.
AC   A4FUD6;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Engulfment and cell motility protein 2;
GN   Name=ELMO2;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) 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: Interacts directly with the SH3-domain of DOCK1 via its SH3-
CC       binding site (By similarity). Probably forms a heterotrimeric complex
CC       with DOCK1 and RAC1. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates
CC       activation of RAC1 by EPHA2 (By similarity). Interacts with ADGRB3 (By
CC       similarity). Interacts with AUTS2; the interaction is direct (By
CC       similarity). {ECO:0000250|UniProtKB:Q8BHL5,
CC       ECO:0000250|UniProtKB:Q96JJ3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96JJ3}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96JJ3}. Membrane
CC       {ECO:0000250|UniProtKB:Q96JJ3}.
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DR   EMBL; BC114724; AAI14725.1; -; mRNA.
DR   RefSeq; NP_001076860.1; NM_001083391.1.
DR   AlphaFoldDB; A4FUD6; -.
DR   SMR; A4FUD6; -.
DR   STRING; 9913.ENSBTAP00000004747; -.
DR   PaxDb; A4FUD6; -.
DR   PRIDE; A4FUD6; -.
DR   GeneID; 508361; -.
DR   KEGG; bta:508361; -.
DR   CTD; 63916; -.
DR   eggNOG; KOG2999; Eukaryota.
DR   InParanoid; A4FUD6; -.
DR   OrthoDB; 234725at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
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:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
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; IPR030713; ELMO2.
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:SF8; PTHR12771:SF8; 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; Membrane; Phagocytosis; Phosphoprotein;
KW   Reference proteome; SH3-binding.
FT   CHAIN           1..720
FT                   /note="Engulfment and cell motility protein 2"
FT                   /id="PRO_0000312353"
FT   DOMAIN          310..484
FT                   /note="ELMO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT   DOMAIN          553..674
FT                   /note="PH"
FT   MOTIF           700..707
FT                   /note="SH3-binding"
FT   MOD_RES         48
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL5"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JJ3"
FT   MOD_RES         717
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL5"
SQ   SEQUENCE   720 AA;  82589 MW;  8233A17435284AFD CRC64;
     MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
     ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSSMETR LDAMKELAKL SADVTFATEF
     INMDGIVVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQIAGYV
     SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
     ALFLKAPEDK RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER
     MMTKMDPNDQ AQRDIIFELR RIAFDADSDP SNAPGSGTEK RKAMYTKDYK MLGFTNHINP
     AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED KHECPFGRSA IELTKMLCEI
     LQVGELPNEG RNDYHPMFFT HDRAFEELFG ICIQLLNKTW KEMRATAEDF NKVMQVVREQ
     ITRALPSKPN SLDQFKSKLR SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL
     IKQQRLNRLC EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK
     IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP NKYEYCIWID
     GLSALLGKDM SSELTKSDRD TLLSMEMKLR LLDLENIQIP EAPPPVPKEP SSYDFVYHYG