ID   LIMD2_BOVIN             Reviewed;         128 AA.
AC   Q1LZA7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=LIM domain-containing protein 2 {ECO:0000305};
GN   Name=LIMD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; BC116116; AAI16117.1; -; mRNA.
DR   RefSeq; NP_001035602.2; NM_001040512.2.
DR   RefSeq; XP_005220893.1; XM_005220836.1.
DR   RefSeq; XP_005220894.1; XM_005220837.2.
DR   AlphaFoldDB; Q1LZA7; -.
DR   BMRB; Q1LZA7; -.
DR   SMR; Q1LZA7; -.
DR   STRING; 9913.ENSBTAP00000010719; -.
DR   PaxDb; Q1LZA7; -.
DR   PRIDE; Q1LZA7; -.
DR   Ensembl; ENSBTAT00000010719; ENSBTAP00000010719; ENSBTAG00000008154.
DR   GeneID; 508942; -.
DR   KEGG; bta:508942; -.
DR   CTD; 80774; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008154; -.
DR   VGNC; VGNC:30889; LIMD2.
DR   eggNOG; KOG1700; Eukaryota.
DR   GeneTree; ENSGT00940000158377; -.
DR   HOGENOM; CLU_026811_3_0_1; -.
DR   InParanoid; Q1LZA7; -.
DR   OMA; MFQDAGA; -.
DR   OrthoDB; 1583903at2759; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000008154; Expressed in blood and 105 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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_0000251206"
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;  14144 MW;  ED6E812C47547E14 CRC64;
     MFQAAGAAQA TPSHEAKGGG SSSTVQRSKS FSLRAQVKET CAACQKTVYP MERLVADKLI
     FHSSCFCCKH CHTKLSLGSY AALHGEFYCK PHFQQLFKSK GNYDEGFGRK QHKELWAHKE
     VDPGTKTA