ID M9LTA3_PSEA3 Unreviewed; 817 AA.
AC M9LTA3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Regulator of Rac1 {ECO:0000313|EMBL:GAC77551.1};
GN ORFNames=PANT_27c00006 {ECO:0000313|EMBL:GAC77551.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC77551.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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; DF196793; GAC77551.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LTA3; -.
DR STRING; 1151754.M9LTA3; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000011976; 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 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 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:UP000011976};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 368..542
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 90118 MW; DB8712F8178899E5 CRC64;
MSASQAGPSR TTLHTPASPT AQQSYIDPAA APLASPQLAN RINLVTYKQS TIKALIDPSL
PVQDVIRQLC ANAHLGVQEP PALFALRDDD NDELIDDANM AKKIEAGANF KLCSSPTIEA
ADMVDKLGSR DERVLKMATY TLQRLIREAP FTNEFVARGG VRELLNVIRN HSSGNTLAYA
LTSCQNLMEG FEYGWDIIDA DIVAKVVNLL VSQERINVCR PATAILKKLV VSGPQDSPKM
GRVLTDGSGA ASAAPPPVYR YGFDFVYAEF QREPLFLQTL TNRIGSSDTT LKLYSLSLIN
SLLRNVSDEL FESFTSELEK LNASKAVAWL MDSHRGDELA SSILDYQTNV IRTAHRRMRT
AVTPTDKRHV HALSYIWLQA KISDVVVPNK NPAQTTLNGA SRTAGGATTR YKWRRIGFAS
ESAAKEFGRT GWLGLLCLES FVRSDPDLYA KIILEQINRP EERRCMFARA SIEVTSILAD
HWDIESGSFT ASTSYLPFLL SLTKVHNLAL RFFLRMWNES GAAASDFSRV SALVRSQVHD
ALGKQDEVSR TWIDLEDAFL HSEYRTVRDR QIKELEVDED YNSKASIRNL RGRIYRESYE
FVRQQRIQCL LEGAWFRNVV ASSAVGAGAM GAKQRRGSTS TVETTNTAMP TISNGATAPT
KPWRFYRLAP NKKFLYFCDS SDRVPIRGGL DDLPDRIDLS LVTEISHHGG AATGGGSGGA
ATGRELVISL LQSPDVCVAE MQALNASQLS EWTDGLNMLR DEGGVVSTRE TADLINMLTE
IGIKVKMLDL TGEQIELPAT VQAPPLPSTT EFFFAEL
//