ELMOA_DICDI
ID ELMOA_DICDI Reviewed; 977 AA.
AC Q54YW1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=ELMO domain-containing protein A;
GN Name=elmoA; ORFNames=DDB_G0278051;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, INTERACTION WITH MHCA, AND DISRUPTION PHENOTYPE.
RX PubMed=18854143; DOI=10.1016/j.devcel.2008.08.006;
RA Isik N., Brzostowski J.A., Jin T.;
RT "An Elmo-like protein associated with myosin II restricts spurious F-actin
RT events to coordinate phagocytosis and chemotaxis.";
RL Dev. Cell 15:590-602(2008).
CC -!- FUNCTION: Functions as a negative regulator of actin polymerization.
CC Modulates actin/myosin II at cortex actinomyosins to prevent excessive
CC F-actin polymerization around the cell periphery, thereby maintaining
CC proper cell shape during phagocytosis and chemotaxis.
CC {ECO:0000269|PubMed:18854143}.
CC -!- SUBUNIT: Associates with mhcA.
CC -!- INTERACTION:
CC Q54YW1; P08799: mhcA; NbExp=2; IntAct=EBI-2928498, EBI-2928504;
CC -!- DISRUPTION PHENOTYPE: Null mutants show the remarkable ability to
CC engulf multiple particles simultaneously, also positively respond to a
CC cAMP gradient but form spurious peudopods which are normally suppressed
CC to promote efficient movement up a chemical gradient.
CC {ECO:0000269|PubMed:18854143}.
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DR EMBL; AAFI02000023; EAL68198.1; -; Genomic_DNA.
DR RefSeq; XP_642091.1; XM_636999.1.
DR AlphaFoldDB; Q54YW1; -.
DR SMR; Q54YW1; -.
DR IntAct; Q54YW1; 1.
DR STRING; 44689.DDB0233912; -.
DR PaxDb; Q54YW1; -.
DR EnsemblProtists; EAL68198; EAL68198; DDB_G0278051.
DR GeneID; 8621302; -.
DR KEGG; ddi:DDB_G0278051; -.
DR dictyBase; DDB_G0278051; elmoA.
DR eggNOG; KOG2998; Eukaryota.
DR HOGENOM; CLU_304284_0_0_1; -.
DR InParanoid; Q54YW1; -.
DR OMA; FEEVYCT; -.
DR Reactome; R-DDI-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR PRO; PR:Q54YW1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006816; ELMO_dom.
DR Pfam; PF04727; ELMO_CED12; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..977
FT /note="ELMO domain-containing protein A"
FT /id="PRO_0000333278"
FT DOMAIN 383..561
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT REGION 792..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 109938 MW; 7B0627F1043890A9 CRC64;
MKIKVTFQER IIEHNFETEI TNLQQVTQKL CSLFLITNYY SYSLFLSSGQ LVDNINLIDE
GSEIIIKHLN RLGTISIGSG YSNSVVGTTN NNAPSSPSSS ININGQQIQQ QIQQQIQQQQ
QQQQQQQQQV QLSPDTLINN LLNNLKDNTF KKKAFFDLKD LKEEILIKKF VEKNGIEVIV
CQLKELTGNT LSYALSALQT IMSYEFTITS MTSTDTASLI TQLLPLTENT SNPSISKTSL
SLLCLFLNQS NNLNFKQFSS TLVLEYNEKT KRNYNHTLVQ LLSSSNTVDV QLNALTLINI
IIGKTMSTTI PGLENGSVTG GENGFNKLLK ELDEYEINQK LKKLVESIIV APELKRQLYI
YQRHRFQVIT NRKNVTFNKE SSEHDALLMK LWSLTYPGVK LESRVSEQWK QMGFQGTDPC
TDFRAMGIWG LDNLIYFAQN YNEKFRKIVN SQIDRKEREY PTATAGIVLT FELYNSIFKM
GTPNLNPYNS TTSNTTSNTT STTNIDDLPF FPLFFSHPHA FEEVYCTTFQ ILDSTWDDMN
GTYMHFQKIM SSVKNLIITA LESKPTTLEA FDWKCQKNTK NSNGGTNSNQ NNSSSNLLLS
NFANGSSLLS LLNDLSSSSR DDMKKLLTGV NYQVLDLIKS QKISYFQEGF QFKLHKQLKT
KQSLPLNWIF IRLFNNNNNN NNNNENCSYE IQYCFLSTEL NQPPLPNQSI PTNYNTIKIS
DLFFNGESTN SNNKKKDKSL SYFNISIKDE QIQSLIQNQL PLSNLNNSSN SLQLDSSTSM
NSIKDSIINI SSSNNNIKDN LTNNNTNTNT NNTNNNTSNG NGNSNSVSMS SININNSGQL
SPNTTSPILI PQQQQQQPQS SSLSVQHQQS STPTPSSPVL LSSPSLQSSS SSSSSSSNPN
LFTIDLISSN RDDVSNFWDS IKLLSGQEIK SQEGLDDYHS LLSINTSVKL LDLDGIDIPK
ETPQIPILPD NFDFRTV