ID ELMO2_PONAB Reviewed; 720 AA.
AC Q5RCC1; Q5R6I9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 84.
DE RecName: Full=Engulfment and cell motility protein 2;
GN Name=ELMO2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858353; CAH90586.1; -; mRNA.
DR EMBL; CR860500; CAH92621.1; -; mRNA.
DR RefSeq; NP_001126536.1; NM_001133064.1.
DR RefSeq; NP_001128780.1; NM_001135308.1.
DR AlphaFoldDB; Q5RCC1; -.
DR SMR; Q5RCC1; -.
DR STRING; 9601.ENSPPYP00000012394; -.
DR GeneID; 100173525; -.
DR GeneID; 100189680; -.
DR KEGG; pon:100173525; -.
DR CTD; 63916; -.
DR eggNOG; KOG2999; Eukaryota.
DR InParanoid; Q5RCC1; -.
DR OrthoDB; 4872856at2759; -.
DR Proteomes; UP000001595; 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
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:SF8; ENGULFMENT AND CELL MOTILITY PROTEIN 2; 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 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_0000312354"
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"
FT CONFLICT 199
FT /note="S -> N (in Ref. 1; CAH92621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 82603 MW; 666E77E3B272293E CRC64;
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR LDAMKELAKL SADVTFATEF
INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQIAGYV
SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
ALFLKAPEDK RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER
MMTKMDPNDQ AQRDIIFELR RIAFDAESDP 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
TPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP NKYEYCIWID
GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP EAPPPIPKEP SSYDFVYHYG
//
