LIMD2_MOUSE
ID LIMD2_MOUSE Reviewed; 128 AA.
AC Q8BGB5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=LIM domain-containing protein 2 {ECO:0000305};
GN Name=Limd2 {ECO:0000312|MGI:MGI:1915053};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Hippocampus, Olfactory bulb, Placenta, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK012581; BAC25371.1; -; mRNA.
DR EMBL; AK032430; BAC27866.1; -; mRNA.
DR EMBL; AK049809; BAC33928.1; -; mRNA.
DR EMBL; AK167349; BAE39448.1; -; mRNA.
DR EMBL; AK169829; BAE41396.1; -; mRNA.
DR EMBL; AK171794; BAE42667.1; -; mRNA.
DR EMBL; BC068130; AAH68130.1; -; mRNA.
DR CCDS; CCDS25549.1; -.
DR RefSeq; NP_765985.1; NM_172397.3.
DR RefSeq; XP_006534082.1; XM_006534019.3.
DR RefSeq; XP_006534083.1; XM_006534020.3.
DR AlphaFoldDB; Q8BGB5; -.
DR BMRB; Q8BGB5; -.
DR SMR; Q8BGB5; -.
DR BioGRID; 212451; 2.
DR STRING; 10090.ENSMUSP00000045357; -.
DR iPTMnet; Q8BGB5; -.
DR PhosphoSitePlus; Q8BGB5; -.
DR EPD; Q8BGB5; -.
DR jPOST; Q8BGB5; -.
DR MaxQB; Q8BGB5; -.
DR PaxDb; Q8BGB5; -.
DR PeptideAtlas; Q8BGB5; -.
DR PRIDE; Q8BGB5; -.
DR ProteomicsDB; 265071; -.
DR Antibodypedia; 45674; 89 antibodies from 19 providers.
DR DNASU; 67803; -.
DR Ensembl; ENSMUST00000045923; ENSMUSP00000045357; ENSMUSG00000040699.
DR Ensembl; ENSMUST00000064545; ENSMUSP00000067070; ENSMUSG00000040699.
DR Ensembl; ENSMUST00000106875; ENSMUSP00000102488; ENSMUSG00000040699.
DR GeneID; 67803; -.
DR KEGG; mmu:67803; -.
DR UCSC; uc007lyd.1; mouse.
DR CTD; 80774; -.
DR MGI; MGI:1915053; Limd2.
DR VEuPathDB; HostDB:ENSMUSG00000040699; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158377; -.
DR HOGENOM; CLU_026811_3_0_1; -.
DR InParanoid; Q8BGB5; -.
DR OMA; MFQDAGA; -.
DR OrthoDB; 1583903at2759; -.
DR PhylomeDB; Q8BGB5; -.
DR BioGRID-ORCS; 67803; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Limd2; mouse.
DR PRO; PR:Q8BGB5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BGB5; protein.
DR Bgee; ENSMUSG00000040699; Expressed in peripheral lymph node and 251 other tissues.
DR Genevisible; Q8BGB5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 1: Evidence at protein 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_0000251208"
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; 14237 MW; ADF9161771331D13 CRC64;
MFQAAGAAQA TPSHEAKGSS GSSTVQRSKS FSLRAQVKET CAACQKTVYP MERLVADKLI
FHNSCFCCKH CHTKLSLGSY AAMHGEFYCR PHFQQLFKSK GNYDEGFGRK QHKELWAHKE
VDSGTKTA
