ID A0A3Q3XNM7_MOLML Unreviewed; 733 AA.
AC A0A3Q3XNM7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000026166.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000026166.1}
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 AlphaFoldDB; A0A3Q3XNM7; -.
DR STRING; 94237.ENSMMOP00000026166; -.
DR Ensembl; ENSMMOT00000026608.1; ENSMMOP00000026166.1; ENSMMOG00000019840.1.
DR OMA; WESHARP; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..498
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 733 AA; 84858 MW; C08C4BC8811628EC CRC64;
MFINASWILK NSPQVSARIT LSFSPHLNPM SCVLRCSQPL ILIMQFCFVF LLYIPLAFRW
SLGNHENFAL QIADATNFYI TEKNRNDIKN GSILRLTTSP YQTAVQLHER IQSSSMDAKL
ESLKDLAHAS RDITFAQEFI NLDGISLLTQ MVESGTDFGD LLSFTLTAFV ELMDHGIVSW
DTFSVAFIKK IASYVNKSAM DMAVLQRSLA ILESMVLNSQ DLYQKVAQEI TIGQLIPHLQ
GTDQDIQTYT IAVINALFLK APEEKRQEMA HILAQKQLRS IILSNVIRSP MPINDEMAHQ
LYVLQVLTFN LLEDRMMTKM DPQDQAQRDI IFELRRIAFD VECEPNNSGS IEKRKSMYTR
DYKKLGFINH VNPAVDFTQI PPGMLALDNM LYFARHHQDA YVRIVLENSS REDKHECPFG
RSSIELTKML CEILKVGELP SENCHDFHPM FFTHDRSFEE FFCTCIQLLN KTWKEMRATS
EDFNKVMQVV REQIMRALTL KPNSLDQFKS RLQNLSYTEI LKIRQSERMN QEDFQSRPIL
ELREKIQPEI MELIKQQRLN RLCEGTCFRK ISSRRRQDKF WYCRLSPNHK VLHYGDLEES
PQGEVPHESL QDKLPVADIK AVITGKDCPH MKEKGALKQN KEVLELAFSV LYESDEYLNF
IAPDKHEYCV WTDGLNALLG KEMTSNYTKS DMDTLLSMEM KLRLLDLENI QIPEAPPPIP
KEPSNYDFVY DCN
//
