ID   LIME_DICDI              Reviewed;         199 AA.
AC   O60952; Q54WP2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=LIM domain-containing protein E;
DE   AltName: Full=DdLim;
GN   Name=limE; Synonyms=crp; ORFNames=DDB_G0279415;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   INTERACTION WITH RAC1A.
RC   STRAIN=AX3;
RX   PubMed=9487125; DOI=10.1091/mbc.9.3.545;
RA   Prassler J., Murr A., Stocker S., Faix J., Murphy J., Marriott G.;
RT   "DdLIM is a cytoskeleton-associated protein involved in the protrusion of
RT   lamellipodia in Dictyostelium.";
RL   Mol. Biol. Cell 9:545-559(1998).
RN   [2]
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=14506710; DOI=10.1002/cm.10139;
RA   Schneider N., Weber I., Faix J., Prassler J., Mueller-Taubenberger A.,
RA   Koehler J., Burghardt E., Gerisch G., Marriott G.;
RT   "A Lim protein involved in the progression of cytokinesis and regulation of
RT   the mitotic spindle.";
RL   Cell Motil. Cytoskeleton 56:130-139(2003).
CC   -!- FUNCTION: Associates with the actin cytoskeleton and may regulate actin
CC       polymerization in lamellipodia, through a rac1-dependent signaling
CC       pathway. May play a role in cell motility. Involved in cytokinesis by
CC       regulating the microtubule system and linking it to the cortical actin
CC       network. {ECO:0000269|PubMed:14506710}.
CC   -!- SUBUNIT: May interact with rac1A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex. Nucleus. Cell
CC       projection, lamellipodium. Cell projection, filopodium. Cytoplasm,
CC       cytoskeleton. Note=Weakly expressed in cytoplasm. Found in actin-rich
CC       protrusions, and lamellipodia and filopodia during motility.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 0 hours to 12 hours upon starvation
CC       (at protein level). Expressed in the polar region during cytokinesis.
CC       {ECO:0000269|PubMed:14506710, ECO:0000269|PubMed:9487125}.
CC   -!- DISRUPTION PHENOTYPE: Cells exhibit longer microtubules than normal.
CC       During mitosis, interphase microtubules and the spindle persist far
CC       longer than in wild-type cells. {ECO:0000269|PubMed:14506710}.
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DR   EMBL; U97699; AAC05729.1; -; mRNA.
DR   EMBL; AAFI02000031; EAL67646.1; -; Genomic_DNA.
DR   RefSeq; XP_641675.1; XM_636583.1.
DR   AlphaFoldDB; O60952; -.
DR   IntAct; O60952; 2.
DR   STRING; 44689.DDB0214939; -.
DR   PaxDb; O60952; -.
DR   EnsemblProtists; EAL67646; EAL67646; DDB_G0279415.
DR   GeneID; 8622083; -.
DR   KEGG; ddi:DDB_G0279415; -.
DR   dictyBase; DDB_G0279415; limE.
DR   eggNOG; KOG1702; Eukaryota.
DR   HOGENOM; CLU_1374438_0_0_1; -.
DR   InParanoid; O60952; -.
DR   OMA; YQQEGEY; -.
DR   PhylomeDB; O60952; -.
DR   PRO; PR:O60952; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR045268; LIMA-like.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24206; PTHR24206; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00132; LIM; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell projection; Cytoplasm; Cytoskeleton; LIM domain;
KW   Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..199
FT                   /note="LIM domain-containing protein E"
FT                   /id="PRO_0000328168"
FT   DOMAIN          5..65
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          134..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..199
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22058 MW;  D2557325E2FF8D24 CRC64;
     MSASVKCGAC AKTAYPLESV VANNNSYHKG CFKCSTCNST LNVKTFKSFE GKLYCPVHTP
     KVSATAVTDS VALKNALNAP KKVAEGLGNA HRGLDEKPNI GLDSMATANA LNAPKKVVEG
     LGNVQKGIGG KPTYAVFGAD GQPTGEQQEQ QQYTEEQYEQ PQEEQQYQEE QQQYQEEEQQ
     YQEEEQQYQE EEQQYEEEQ