LIMS2_MOUSE
ID LIMS2_MOUSE Reviewed; 341 AA.
AC Q91XD2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=LIM and senescent cell antigen-like-containing domain protein 2;
DE AltName: Full=Particularly interesting new Cys-His protein 2;
DE Short=PINCH-2;
GN Name=Lims2; Synonyms=Pinch2;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12651156; DOI=10.1016/s0014-4827(02)00039-3;
RA Braun A., Bordoy R., Stanchi F., Moser M., Kostka G., Ehler E., Brandau O.,
RA Faessler R.;
RT "PINCH2 is a new five LIM domain protein, homologous to PINCH and localized
RT to focal adhesions.";
RL Exp. Cell Res. 284:239-250(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 INTERACTION WITH TGFB1I1.
RX PubMed=16737959; DOI=10.1074/jbc.m513111200;
RA Mori K., Asakawa M., Hayashi M., Imura M., Ohki T., Hirao E.,
RA Kim-Kaneyama J.-R., Nose K., Shibanuma M.;
RT "Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a
RT nuclear-cytoplasmic shuttling complex.";
RL J. Biol. Chem. 281:22048-22061(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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: Adapter protein in a cytoplasmic complex linking beta-
CC integrins to the actin cytoskeleton, bridges the complex to cell
CC surface receptor tyrosine kinases and growth factor receptors.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with integrin-linked protein kinase 1 (ILK) via the
CC first LIM domain, and in competition with LIMS1. Part of the
CC heterotrimeric IPP complex composed of integrin-linked kinase (ILK),
CC LIMS1 or LIMS2, and PARVA (By similarity). Interacts with TGFB1I1.
CC {ECO:0000250, ECO:0000269|PubMed:16737959}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:12651156}. Cell membrane
CC {ECO:0000269|PubMed:12651156}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12651156}; Cytoplasmic side
CC {ECO:0000269|PubMed:12651156}.
CC -!- TISSUE SPECIFICITY: Detected in heart, lung, kidney, liver, urinary
CC bladder, fat, skin, skeletal muscle, uterus, large intestine and
CC testis. {ECO:0000269|PubMed:12651156}.
CC -!- DEVELOPMENTAL STAGE: Not detectable during early stages of
CC embryogenesis. Detected at low levels at 14.5 dpc and 15.5 dpc. Highly
CC expressed at 17.5 dpc.
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; AJ420860; CAD12820.1; -; Genomic_DNA.
DR EMBL; AJ420861; CAD12820.1; JOINED; Genomic_DNA.
DR EMBL; AJ420863; CAD12820.1; JOINED; Genomic_DNA.
DR EMBL; AJ420862; CAD12820.1; JOINED; Genomic_DNA.
DR EMBL; BC010816; AAH10816.1; -; mRNA.
DR CCDS; CCDS29113.1; -.
DR RefSeq; NP_659111.1; NM_144862.3.
DR AlphaFoldDB; Q91XD2; -.
DR SMR; Q91XD2; -.
DR BioGRID; 230384; 6.
DR STRING; 10090.ENSMUSP00000025254; -.
DR iPTMnet; Q91XD2; -.
DR PhosphoSitePlus; Q91XD2; -.
DR MaxQB; Q91XD2; -.
DR PaxDb; Q91XD2; -.
DR PeptideAtlas; Q91XD2; -.
DR PRIDE; Q91XD2; -.
DR ProteomicsDB; 286205; -.
DR Antibodypedia; 55985; 157 antibodies from 22 providers.
DR DNASU; 225341; -.
DR Ensembl; ENSMUST00000025254; ENSMUSP00000025254; ENSMUSG00000024395.
DR GeneID; 225341; -.
DR KEGG; mmu:225341; -.
DR UCSC; uc008eiv.1; mouse.
DR CTD; 55679; -.
DR MGI; MGI:2385067; Lims2.
DR VEuPathDB; HostDB:ENSMUSG00000024395; -.
DR eggNOG; KOG2272; Eukaryota.
DR GeneTree; ENSGT00940000153518; -.
DR HOGENOM; CLU_001357_0_0_1; -.
DR InParanoid; Q91XD2; -.
DR OMA; FHEHCFV; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; Q91XD2; -.
DR TreeFam; TF314113; -.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR BioGRID-ORCS; 225341; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Lims2; mouse.
DR PRO; PR:Q91XD2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91XD2; protein.
DR Bgee; ENSMUSG00000024395; Expressed in aorta tunica media and 168 other tissues.
DR ExpressionAtlas; Q91XD2; baseline and differential.
DR Genevisible; Q91XD2; MM.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; IGI:MGI.
DR GO; GO:1990705; P:cholangiocyte proliferation; IGI:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:1904055; P:negative regulation of cholangiocyte proliferation; IGI:MGI.
DR GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IGI:MGI.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IGI:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IGI:MGI.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR InterPro; IPR017351; PINCH_1-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24210; PTHR24210; 1.
DR Pfam; PF00412; LIM; 5.
DR PIRSF; PIRSF038003; PINCH; 1.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; LIM domain; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..341
FT /note="LIM and senescent cell antigen-like-containing
FT domain protein 2"
FT /id="PRO_0000266012"
FT DOMAIN 13..74
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 76..133
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 138..195
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 196..255
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 256..315
FT /note="LIM zinc-binding 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4I7"
SQ SEQUENCE 341 AA; 39031 MW; 7A93F9845BDAED91 CRC64;
MTGSNMSECL ADAMCQRCQA RFAPTERIVN SNGELYHEHC FVCAQCFRPF PEGLFYEFEG
RKYCEHDFQM LFAPCCGFCG EFVIGRVIKA MNANWHPGCF RCELCDVELA DLGFVKNAGR
HLCRPCHNRE KAKGLGKFIC QRCHLAIDEQ PLMFKNDPYH PDHFSCSNCG KELTSDAREL
KGELYCLPCH DKMGIPICGA CRRPIEGRVV NALGKQWHVE HFVCAKCEKP FLGHRHYEKK
GLAYCETHYN QLFGDVCYNC SHVIEGDVVS ALSKAWCVNC FSCSTCNMKL TLKNKFVEFD
MKPVCKRCYE RFPLELKKRL KKLSDLSSRK AQPKSVDVNS L
