LIMS1_MOUSE
ID LIMS1_MOUSE Reviewed; 325 AA.
AC Q99JW4; Q3UAT7; Q8BTR6; Q9D5T4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=LIM and senescent cell antigen-like-containing domain protein 1;
DE AltName: Full=Particularly interesting new Cys-His protein 1;
DE Short=PINCH-1;
GN Name=Lims1; Synonyms=Pinch1;
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; TISSUE=Bone marrow, Testis, 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=FVB/N; TISSUE=Mammary tumor;
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=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and 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: 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. Involved
CC in the regulation of cell survival, cell proliferation and cell
CC differentiation.
CC -!- SUBUNIT: Interacts with integrin-linked protein kinase 1 (ILK) via the
CC first LIM domain, and in competition with LIMS2. Part of the
CC heterotrimeric IPP complex composed of integrin-linked kinase (ILK),
CC LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter NCK2, thereby
CC linking the complex to cell surface receptors (By similarity).
CC Interacts (via LIM zinc-binding 5) with TGFB1I1. {ECO:0000250,
CC ECO:0000269|PubMed:16737959}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC40663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014954; BAB29637.1; ALT_INIT; mRNA.
DR EMBL; AK082932; BAC38699.1; ALT_INIT; mRNA.
DR EMBL; AK088939; BAC40663.1; ALT_INIT; mRNA.
DR EMBL; AK151235; BAE30227.1; ALT_INIT; mRNA.
DR EMBL; AK151938; BAE30814.1; ALT_INIT; mRNA.
DR EMBL; AK152679; BAE31411.1; ALT_INIT; mRNA.
DR EMBL; AK153346; BAE31922.1; ALT_INIT; mRNA.
DR EMBL; BC005621; AAH05621.1; ALT_INIT; mRNA.
DR RefSeq; NP_080424.2; NM_026148.3.
DR RefSeq; XP_006513136.1; XM_006513073.2.
DR AlphaFoldDB; Q99JW4; -.
DR SMR; Q99JW4; -.
DR BioGRID; 225940; 7.
DR CORUM; Q99JW4; -.
DR DIP; DIP-59289N; -.
DR IntAct; Q99JW4; 3.
DR MINT; Q99JW4; -.
DR STRING; 10090.ENSMUSP00000020078; -.
DR iPTMnet; Q99JW4; -.
DR PhosphoSitePlus; Q99JW4; -.
DR SwissPalm; Q99JW4; -.
DR EPD; Q99JW4; -.
DR MaxQB; Q99JW4; -.
DR PaxDb; Q99JW4; -.
DR PRIDE; Q99JW4; -.
DR ProteomicsDB; 286204; -.
DR DNASU; 110829; -.
DR GeneID; 110829; -.
DR KEGG; mmu:110829; -.
DR UCSC; uc011xeb.1; mouse.
DR CTD; 3987; -.
DR MGI; MGI:1195263; Lims1.
DR eggNOG; KOG2272; Eukaryota.
DR InParanoid; Q99JW4; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; Q99JW4; -.
DR TreeFam; TF314113; -.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR BioGRID-ORCS; 110829; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Lims1; mouse.
DR PRO; PR:Q99JW4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99JW4; protein.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; IGI:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:1990705; P:cholangiocyte proliferation; IGI:MGI.
DR GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:1904055; P:negative regulation of cholangiocyte proliferation; IGI:MGI.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; 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:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IGI:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
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 Acetylation; Cell junction; Cell membrane; LIM domain; Membrane;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48059"
FT CHAIN 2..325
FT /note="LIM and senescent cell antigen-like-containing
FT domain protein 1"
FT /id="PRO_0000266009"
FT DOMAIN 10..62
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 71..121
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 135..184
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 193..243
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 252..303
FT /note="LIM zinc-binding 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48059"
FT CONFLICT 59
FT /note="C -> S (in Ref. 1; BAE30227)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="N -> D (in Ref. 1; BAB29637)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> T (in Ref. 1; BAB29637)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> V (in Ref. 1; BAC40663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37240 MW; E665FEA59B5FFDFE CRC64;
MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF YEFEGRKYCE
HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC QEVLADIGFV KNAGRHLCRP
CHNREKARGL GKYICQKCHA IIDEQPLIFK NDPYHPDHFN CANCGKELTA DARELKGELY
CLPCHDKMGV PICGACRRPI EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC
ETHYNQLFGD VCFHCNRVIE GDVVSALNKA WCVSCFACST CNTKLTLKNK FVEFDMKPVC
KKCYEKFPLE LKKRLKKLSE TLGRK
