LIMB_DICDI
ID LIMB_DICDI Reviewed; 553 AA.
AC Q54NW4; Q9U628;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=LIM domain-containing protein B;
DE AltName: Full=Paxillin-A;
GN Name=limB; Synonyms=lim2, paxA; ORFNames=DDB_G0284863;
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], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3-1;
RX PubMed=10749929; DOI=10.1091/mbc.11.4.1275;
RA Chien S., Chung C.Y., Sukumaran S., Osborne N., Lee S., Ellsworth C.,
RA McNally J.G., Firtel R.A.;
RT "The Dictyostelium LIM domain-containing protein LIM2 is essential for
RT proper chemotaxis and morphogenesis.";
RL Mol. Biol. Cell 11:1275-1291(2000).
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.
RX PubMed=16155255; DOI=10.1242/jcs.02557;
RA Bukharova T., Weijer G., Bosgraaf L., Dormann D., van Haastert P.J.,
RA Weijer C.J.;
RT "Paxillin is required for cell-substrate adhesion, cell sorting and slug
RT migration during Dictyostelium development.";
RL J. Cell Sci. 118:4295-4310(2005).
CC -!- FUNCTION: Regulates and controls rearrangements of the actin
CC cytoskeleton. Required for tip formation, morphogenesis, cell adhesion
CC and motility, chemotaxis and aggregates formation. May function
CC downstream of paxB. {ECO:0000269|PubMed:10749929,
CC ECO:0000269|PubMed:16155255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10749929}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10749929}.
CC -!- DEVELOPMENTAL STAGE: Expressed after 4 hours of development, reaches a
CC peak at 8 to 12 hours, and then decreases.
CC {ECO:0000269|PubMed:10749929}.
CC -!- DISRUPTION PHENOTYPE: Cells exhibit an aberrant actin cytoskeleton and
CC numerous F-actin-enriched microspikes. Cells aggregate poorly and
CC aggregates arrest at the mound stage. They exhibit poor adhesion, form
CC weak cell-cell agglomerates in suspension, do not polarize in
CC chemoattractant gradient and move very poorly.
CC {ECO:0000269|PubMed:10749929}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF198250; AAF05849.1; -; mRNA.
DR EMBL; AAFI02000073; EAL64895.1; -; Genomic_DNA.
DR RefSeq; XP_639953.1; XM_634861.1.
DR AlphaFoldDB; Q54NW4; -.
DR SMR; Q54NW4; -.
DR STRING; 44689.DDB0191245; -.
DR PaxDb; Q54NW4; -.
DR EnsemblProtists; EAL64895; EAL64895; DDB_G0284863.
DR GeneID; 8624865; -.
DR KEGG; ddi:DDB_G0284863; -.
DR dictyBase; DDB_G0284863; limB.
DR eggNOG; KOG2272; Eukaryota.
DR HOGENOM; CLU_492984_0_0_1; -.
DR InParanoid; Q54NW4; -.
DR OMA; VCAQCFE; -.
DR PhylomeDB; Q54NW4; -.
DR Reactome; R-DDI-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR PRO; PR:Q54NW4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; ISS:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR InterPro; IPR017351; PINCH_1-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24210; PTHR24210; 2.
DR Pfam; PF00412; LIM; 5.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
PE 2: Evidence at transcript level;
KW Chemotaxis; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..553
FT /note="LIM domain-containing protein B"
FT /id="PRO_0000328165"
FT DOMAIN 205..262
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 263..322
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 328..387
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 388..447
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 448..505
FT /note="LIM zinc-binding 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 43..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 143..146
FT /note="Missing (in Ref. 1; AAF05849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 60341 MW; 9E763FC22380B4E0 CRC64;
MANKNVLSEM DDLMAELGLV ETTATPTSDQ IKQPQQETAP TYLTYKDPNV STGPGGDFRN
LNDNNGGISR GPGLMSTGPG LVSTGPGLMS TGPGLMSKGP GLPNNSINNN ISNNNGGGIS
SGPGLSFGVS SGVSSGVSSG VSSGVSSGVT LVAQNHLARQ PSPPLNSQQQ QQQQLPTYLD
GVGTLQPISL AATTPDGRVV KANGPICGAC GDMIIGVCTN ALGRSYHPEH FVCTYCKLPF
SGSFIEHEEK LYCENDYLEL FSPRCFACIK PIEDTCINAL GNRYHPECFS CSGCGDKLRG
KPYKEEDGEV YCNTCKIARQ KRLAAKSEIC SKCKLPITGE YIILQGQPVH SEHYRCEECG
CEFNVGKTCH EYEGRLYCYE DYQKQILNIC GACSKPIVGR SITALGKVWH PEHFTCTTCQ
VPFAGSAFRE HAGKPYCESH YHQFFGRQCF KCSKPVVDTG VEVFGKIYHR EHFTCTGCEC
VLGKEIMEWD GKPLCFKCFD ALPKEVRKRI KEKKAGDKKA EAYREKLAKK EAKELKKERE
RAAKEKEKES KAK
