ID   LIMD2_RAT               Reviewed;         128 AA.
AC   Q4KM31;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=LIM domain-containing protein 2 {ECO:0000305};
GN   Name=Limd2;
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=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as an activator of the protein-kinase ILK, thereby
CC       regulating cell motility. {ECO:0000250|UniProtKB:Q9BT23}.
CC   -!- SUBUNIT: Interacts with ILK. {ECO:0000250|UniProtKB:Q9BT23}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BT23}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9BT23}. Note=Mainly found in cytoplasm,
CC       concentrated in membrane ruffles and in streaks reminiscent of focal
CC       adhesion plaques. Also found in nucleus.
CC       {ECO:0000250|UniProtKB:Q9BT23}.
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DR   EMBL; BC098855; AAH98855.1; -; mRNA.
DR   RefSeq; NP_001020886.1; NM_001025715.1.
DR   RefSeq; XP_006247683.1; XM_006247621.3.
DR   RefSeq; XP_006247684.1; XM_006247622.3.
DR   AlphaFoldDB; Q4KM31; -.
DR   BMRB; Q4KM31; -.
DR   SMR; Q4KM31; -.
DR   STRING; 10116.ENSRNOP00000033334; -.
DR   iPTMnet; Q4KM31; -.
DR   PhosphoSitePlus; Q4KM31; -.
DR   PaxDb; Q4KM31; -.
DR   PRIDE; Q4KM31; -.
DR   GeneID; 360646; -.
DR   KEGG; rno:360646; -.
DR   UCSC; RGD:1309967; rat.
DR   CTD; 80774; -.
DR   RGD; 1309967; Limd2.
DR   VEuPathDB; HostDB:ENSRNOG00000025448; -.
DR   eggNOG; KOG1700; Eukaryota.
DR   HOGENOM; CLU_026811_3_0_1; -.
DR   InParanoid; Q4KM31; -.
DR   OMA; MFQDAGA; -.
DR   OrthoDB; 1583903at2759; -.
DR   PhylomeDB; Q4KM31; -.
DR   PRO; PR:Q4KM31; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000025448; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q4KM31; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09486; LIM_Eplin_like_1; 1.
DR   InterPro; IPR044115; LIM_LIMD2.
DR   InterPro; IPR001781; Znf_LIM.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW   Reference proteome; Zinc.
FT   CHAIN           1..128
FT                   /note="LIM domain-containing protein 2"
FT                   /id="PRO_0000251209"
FT   DOMAIN          39..99
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT23"
SQ   SEQUENCE   128 AA;  14236 MW;  335D3D86D3B923F3 CRC64;
     MFQAAGAAQA TPSHEAKGSS GNSTVQRSKS FSLRAQVKET CAACQKTVYP MERLVADKLI
     FHNSCFCCKH CHTKLSLGSY AAMHGEFYCK PHFQQLFKSK GNYDEGFGRK QHKELWAHKE
     VDSGTKTA