ID A0A452S947_URSAM Unreviewed; 717 AA.
AC A0A452S947;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Engulfment and cell motility 1 {ECO:0000313|Ensembl:ENSUAMP00000028741.1};
GN Name=ELMO1 {ECO:0000313|Ensembl:ENSUAMP00000028741.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000028741.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000028741.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452S947; -.
DR Ensembl; ENSUAMT00000032094.1; ENSUAMP00000028741.1; ENSUAMG00000020630.1.
DR GeneTree; ENSGT00940000155994; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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 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:UP000291022};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 309..482
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 717 AA; 82559 MW; 43733731326B34A7 CRC64;
MGSVRKAVNS HHEINSHCLK VESLGLETFP WYRVCIWSCA FGLCIFVFQR NGSFLSVVVS
SVNTLPFVFV LDEAQNAQQL HERIQSSSMD AKLEALKDLA SLSRDVTFAQ EFINLDGISL
LTQMVESGTD FGDMLSFTLT AFVELMDHGI VSWDTFSVAF IKKIASFVNK SGMDISILQR
SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGTDQEIQ TYTIAVINAL FLKAPDERRQ
VLCGCVFPHQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL TFNLLEDRMM
TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG FINHVNPAMD
FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL TKMLCEILKV
GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV MQVVKEQVMR
ALTTKPSSLD QFKCKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI QPEILELIKQ
QRLNRLVEGT CFRKLNCRRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP HDSLQDKLPV
ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH EYCIWTDGLN
ALLGKDMMSE LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY DFVYDCN
//