AJUBA_RAT
ID AJUBA_RAT Reviewed; 548 AA.
AC Q5U2Z2; Q99ND4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=LIM domain-containing protein ajuba;
GN Name=Ajuba; Synonyms=Jub;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-548, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH SLC1A2.
RX PubMed=11860269; DOI=10.1006/mcne.2001.1066;
RA Marie H., Billups D., Bedford F.K., Dumoulin A., Goyal R.K., Longmore G.D.,
RA Moss S.J., Attwell D.;
RT "The amino terminus of the glial glutamate transporter GLT-1 interacts with
RT the LIM protein Ajuba.";
RL Mol. Cell. Neurosci. 19:152-164(2002).
CC -!- FUNCTION: Adapter or scaffold protein which participates in the
CC assembly of numerous protein complexes and is involved in several
CC cellular processes such as cell fate determination, cytoskeletal
CC organization, repression of gene transcription, mitosis, cell-cell
CC adhesion, cell differentiation, proliferation and migration.
CC Contributes to the linking and/or strengthening of epithelia cell-cell
CC junctions in part by linking adhesive receptors to the actin
CC cytoskeleton. May be involved in signal transduction from cell adhesion
CC sites to the nucleus. Plays an important role in regulation of the
CC kinase activity of AURKA for mitotic commitment. Also a component of
CC the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by
CC influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6
CC multiprotein signaling complex. Functions as an HDAC-dependent
CC corepressor for a subset of GFI1 target genes. Acts as a
CC transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent
CC repression of E-cadherin transcription. Acts as a hypoxic regulator by
CC bridging an association between the prolyl hydroxylases and VHL
CC enabling efficient degradation of HIF1A. Positively regulates microRNA
CC (miRNA)-mediated gene silencing. Negatively regulates the Hippo
CC signaling pathway and antagonizes phosphorylation of YAP1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GRB2 and PIP5K1B. Interacts with AURKA; the
CC interaction occurs during mitosis and both proteins are phosphorylated
CC as they form a complex. Interacts with CTNNA1 and with F-actin.
CC Interacts with LATS2; the interaction occurs during mitosis and the
CC complex regulates organization of the spindle apparatus through
CC recruitment of TUBG to the centrosome. Forms a complex with SQSTM1,
CC PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1 repressor complex.
CC Interacts directly (via the LIM domains) with GFI1; the interaction
CC results in the HDAC-dependent corepression of a subset of GFI1 target
CC genes, and is independent of the GFI1 SNAG domain. Interacts with
CC HDAC1, HDAC2 and HDAC3 (By similarity). Interacts with SLC1A2.
CC Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1,
CC EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with VHL (By
CC similarity). Interacts (via LIM domains) with SNAI1 (via SNAG domain),
CC SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11860269}. Cell membrane
CC {ECO:0000269|PubMed:11860269}. Cell junction {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus (By similarity).
CC Localizes on centrosomes during G2-M phase (By similarity). Colocalizes
CC with GFI1 in the nucleus (By similarity). Preferentially colocalizes
CC with cadherin-adhesive complexes at sites of cell-cell contacts.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, testis, kidney, heart, lung
CC and liver. {ECO:0000269|PubMed:11860269}.
CC -!- DOMAIN: LIM region interacts with CTNNA1. The preLIM region binds
CC directly actin filaments (By similarity). {ECO:0000250}.
CC -!- DOMAIN: LIM-2 and LIM-3 domains mediate the interaction with the N-
CC terminal region of AURKA. The association between LATS2 and AJUBA
CC required the second LIM domain of AJUBA (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Ajuba' means 'curiosity' in Urdu, an Indian dialect.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; BC085802; AAH85802.1; -; mRNA.
DR EMBL; AJ306292; CAC28536.1; -; mRNA.
DR RefSeq; NP_445955.1; NM_053503.1.
DR AlphaFoldDB; Q5U2Z2; -.
DR STRING; 10116.ENSRNOP00000017753; -.
DR iPTMnet; Q5U2Z2; -.
DR PhosphoSitePlus; Q5U2Z2; -.
DR PaxDb; Q5U2Z2; -.
DR PRIDE; Q5U2Z2; -.
DR Ensembl; ENSRNOT00000017753; ENSRNOP00000017753; ENSRNOG00000012791.
DR GeneID; 85265; -.
DR KEGG; rno:85265; -.
DR UCSC; RGD:620407; rat.
DR CTD; 84962; -.
DR RGD; 620407; Ajuba.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000160978; -.
DR HOGENOM; CLU_001357_11_2_1; -.
DR InParanoid; Q5U2Z2; -.
DR OMA; HQGTANY; -.
DR OrthoDB; 326249at2759; -.
DR PhylomeDB; Q5U2Z2; -.
DR TreeFam; TF320310; -.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR PRO; PR:Q5U2Z2; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000012791; Expressed in lung and 19 other tissues.
DR Genevisible; Q5U2Z2; RN.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000932; C:P-body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; ISO:RGD.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISS:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; ISO:RGD.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:RGD.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell cycle; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; LIM domain; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..548
FT /note="LIM domain-containing protein ajuba"
FT /id="PRO_0000312627"
FT DOMAIN 346..407
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 411..471
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 472..540
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..345
FT /note="PreLIM"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..298
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT CONFLICT 343..344
FT /note="DY -> GD (in Ref. 2; CAC28536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 58081 MW; AC0C2D897DAF8907 CRC64;
MERLGEKASR LLEKLRLSDS GSAKFGRRKG EASRSGSDGT PGAGKGRLSG LGGPRKSGHR
GANGGPGDEA LEPAREQGPL DAERNARGSF EAQRFEGSFP GGPPPTRALP LPLSSPPDFR
LETTAPALSP RSSFASSSAS DASKPSSPRG SLLLDGAGAS GAGGSRPCSN RTSGISMGYD
QRHGSPLPAG PCLFGLPLTT APSGYSSGGV PSAYPELHAA LDRLCAHRPV GFGCQESRHS
YPPALGSPGA LTGAVVGTAG PLERRGTQPG RHSVTGYGDC AAGARYQDEL TALLRLTVAT
GGREAGARGE PLGIEPSGLE ESPGSFVPEA SRSRIREPEA REDYFGTCIK CNKGIYGQSN
ACQALDSLYH TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA EKCCVCGHLI
LEKILQAMGK SYHPGCFRCI VCNKCLDGVP FTVDFSNQVY CVTDYHKNYA PKCAACGQPI
LPSEGCEDIV RVISMDRDYH FECYHCEDCR MQLSDEEGCC CFPLDGHLLC HGCHMQRLSA
RQPPTNYI
