ID A0A2I3S6R6_PANTR Unreviewed; 769 AA.
AC A0A2I3S6R6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Engulfment and cell motility 1 {ECO:0000313|Ensembl:ENSPTRP00000072252.1};
GN Name=ELMO1 {ECO:0000313|Ensembl:ENSPTRP00000072252.1,
GN ECO:0000313|VGNC:VGNC:4337};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000072252.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000072252.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000072252.1}
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 EMBL; AACZ04038753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04038756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC211790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC216030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3S6R6; -.
DR Ensembl; ENSPTRT00000105534.1; ENSPTRP00000072252.1; ENSPTRG00000019087.6.
DR VGNC; VGNC:4337; ELMO1.
DR GeneTree; ENSGT00940000155994; -.
DR InParanoid; A0A2I3S6R6; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000019087; Expressed in Brodmann (1909) area 10 and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
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:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
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 Gene3D; 2.30.30.40; SH3 Domains; 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:SF23; ENGULFMENT AND CELL MOTILITY PROTEIN 1; 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:UP000002277};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 361..534
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 769 AA; 88833 MW; 4547C8E6BA3EBE70 CRC64;
MKCLKVSSRP SIRSRQSTHE MIGLRVMEGR LKSFCFRNCI VVYVGIGPIP ITGCLVHPTL
KNCKNENGHF HFSNQYTLVF LRWSLANHEY FALQHADSSN FYITEKNRNE IKNGTILRLT
TSPAQNAQQL HERIQSSSMD AKLEALKDLA SLSRDVTFAQ EFINLDGISL LTQMVESGTE
RYQKLQKIMK PCFGDMLSFT LTAFVELMDH GIVSWDTFSV AFIKKIASFV NKSAIDISIL
QRSLAILESM VLNSHDLYQK VAQEITIGQL IPHLQGSDQE IQTYTIAVIN ALFLKAPDER
RQEMANILAQ KQLRSIILTH VIRAQRAINN EMAHQLYVLQ VLTFNLLEDR MMTKMDPQDQ
AQRDIIFELR RIAFDAESEP NNSSGSMEKR KSMYTRDYKK LGFINHVNPA MDFTQTPPGM
LALDNMLYFA KHHQDAYIRI VLENSSREDK HECPFGRSSI ELTKMLCEIL KVGELPSETC
NDFHPMFFTH DRSFEEFFCI CIQLLNKTWK EMRATSEDFN KVMQVVKEQV MRALTTKPSS
LDQFKSKLQN LSYTEILKIR QSERMNQEDF QSRPILELKE KIQPEILELI KQQRLNRLVE
GTCFRKLNAR RRQDKFWYCR LSPNHKVLHY GDLEESPQGE VPHDSLQDKL PVADIKAVVT
GKDCPHMKEK GALKQNKEVL ELAFSILYDS NCQLNFIAPD KHEYCIWTDG LNALLGKDMM
SDLTRNDLDT LLSMEIKLRL LDLENIQIPD APPPIPKEPS NYDFVYDCN
//
