ID A0A0M3QT03_DROBS Unreviewed; 725 AA.
AC A0A0M3QT03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Ced-12 {ECO:0000313|EMBL:ALC38063.1};
GN ORFNames=Dbus_chr2Lg1468 {ECO:0000313|EMBL:ALC39383.1}, Dbus_chr2Lg148
GN {ECO:0000313|EMBL:ALC38063.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC38063.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC38063.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC38063.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) 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.
CC {ECO:0000256|ARBA:ARBA00024863}.
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DR EMBL; CP012523; ALC38063.1; -; Genomic_DNA.
DR EMBL; CP012523; ALC39383.1; -; Genomic_DNA.
DR RefSeq; XP_017839992.1; XM_017984503.1.
DR RefSeq; XP_017840167.1; XM_017984678.1.
DR AlphaFoldDB; A0A0M3QT03; -.
DR SMR; A0A0M3QT03; -.
DR STRING; 30019.A0A0M3QT03; -.
DR GeneID; 108598061; -.
DR OMA; WESHARP; -.
DR OrthoDB; 4872856at2759; -.
DR Proteomes; UP000494163; Chromosome 2l 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 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:SF56; CED-12; 1.
DR PANTHER; PTHR12771; ENGULFMENT AND CELL MOTILITY; 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:UP000494163};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 310..491
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
SQ SEQUENCE 725 AA; 83542 MW; 30CE97BBAF4EA641 CRC64;
MIPKKMPVKD AHIVKIAVER ENQMAQLINL DQRHPLASKI QEICNIWSIS DHQNYALQFC
ETNNMKYVTE KNRNEIKNGS VLRLQYSPSK TASDALEILI NGNVQDKAQR LKELTALSMD
HTFALEFIKE QGLDILIKMI EDVHQQDEEI LKYSLASFVE LMEHGTVSWE VPELSFVARN
IDIVRNFQKY PTKCGESALS NLENIVQSSS KYVLVAEDIK LQDILRLLQE VNSPVMRQNA
IALLNALFMK ADETRKREIA HTISAKQYRL ALIGNGLSTE MTHQLYVLQT VTLGLLEKRM
RMKMNAQDQD AHEKIKELRR IAFDENSGTL GINEEHIRRG GGGSGGGNVN FSQYYKKLGF
KCDINPAQDF IETPPGILAL DCMVYFSRNY TPQYKKIVHE NSCRADEHEC PFGRTSIELV
KLLCDILRIG EPPAEQSGDF QPMFFTHDQP FEEFFCICVI TLNRTWKDMR ATAEDFQKVF
SVLREQIQRT LKLRPENLED FRNKIALLTY QQITTLRQQE RTSKEECDST ASAIVKLKEK
ISPQIVELIK QQRLSFLVEG TRFSKYSRGT RTKDKFWYAR LSPNHKVIHY GDCDEKNIPT
LEELPKKLPI IDIKQLLEGK ECPHMKETRI RKSAVNLAFS ITFESMDHST LDFVAPDESV
FHYWTDGINA LLGQEMCSKQ KKEDFDTLLS MEIKLRLLDT EGVDISKDPP PIPEDPENYD
FCFES
//
