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Database: UniProt
Entry: A0A3B5PU47_XIPMA
LinkDB: A0A3B5PU47_XIPMA
Original site: A0A3B5PU47_XIPMA 
ID   A0A3B5PU47_XIPMA        Unreviewed;       721 AA.
AC   A0A3B5PU47;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Engulfment and cell motility 2 {ECO:0000313|Ensembl:ENSXMAP00000022440.1};
GN   Name=ELMO2 {ECO:0000313|Ensembl:ENSXMAP00000022440.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000022440.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000022440.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000022440.1};
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; A0A3B5PU47; -.
DR   STRING; 8083.ENSXMAP00000022440; -.
DR   Ensembl; ENSXMAT00000026593.1; ENSXMAP00000022440.1; ENSXMAG00000003634.2.
DR   GeneTree; ENSGT00940000159236; -.
DR   InParanoid; A0A3B5PU47; -.
DR   OMA; XDMANAF; -.
DR   Proteomes; UP000002852; 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   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:SF8; ENGULFMENT AND CELL MOTILITY PROTEIN 2; 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:UP000002852};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          317..486
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
SQ   SEQUENCE   721 AA;  82674 MW;  B3DCE612DCB6A186 CRC64;
     MPPPADIVKV AIEWPGANAQ LIEMDQKRPL ASIIREVCDG WSLSGSEQFA LRYADGPQLY
     ITEQSRGDIK NGTILRLAIS PARAARQLLE RIQSHGIDAR LEALKELAKL SADPTFAAEF
     INMEGIGTLA RLVESGTHFG EMLAFTLTAF LELMDHGIVS WDMISLSFIK QIAGYVNQPM
     VDVSILQRSL AILESMVLNS HSLYHRVAQE ITVGQLIGHL SNQEIQTYAI ALINALFLKA
     PEDRRQEEYT NPLEQHLTEM ASTLAQKHLR SIILNHVIRG NRPIKAEMAH QLYVLQVLTF
     NLLEERMMTK MDPNDQAQRD IIFELRRIAF DGDTDPTGTE KRKAMYTKDY KMLGFTNHLN
     PAMDFTQTPP GMLALDNMLY LARVHQDTYI RIVLENSSRE DKHECPFGRC AIELTRMLCE
     ILQVGELPNE GCNDYHPMFF THDRAWEEFF CVCIQLLNKT WKEMRATAED FNKVMQVVRE
     QITRALAMKP SSIDQLKNKL RGLSYSEILR LRQSERMSQD DFQSPPIIEL RERIQPEILE
     LIKQQRLNRL CEGSCFRKLG NRRRQEKFWF CRLSLNHKVL HYGDLEESPQ GEVPFELLSD
     KIPVSDIKSV LTGKDCPHMK EKSALKQNKE VLELAFSVLY DPDETLNFVA PNKYEYCIWT
     DGLCALLGRE MGSDLTRSDL DTLISMEMKL RLLDLENITI PEAPPPVPKE PSSYNFTYNY
     S
//
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