LIMA1_HUMAN
ID LIMA1_HUMAN Reviewed; 759 AA.
AC Q9UHB6; B2RB09; Q2TAN7; Q59FE8; Q9BVF2; Q9H8J1; Q9HBN5; Q9NX96; Q9NXC3;
AC Q9NXU6; Q9P0H8; Q9UHB5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=LIM domain and actin-binding protein 1;
DE AltName: Full=Epithelial protein lost in neoplasm;
GN Name=LIMA1 {ECO:0000312|HGNC:HGNC:24636};
GN Synonyms=EPLIN {ECO:0000303|PubMed:10618726}, SREBP3; ORFNames=PP624;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=10618726; DOI=10.1038/sj.onc.1203206;
RA Maul R.S., Chang D.D.;
RT "EPLIN, epithelial protein lost in neoplasm.";
RL Oncogene 18:7838-7841(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA; BETA AND 3).
RC TISSUE=Colon, Hepatoma, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Brain, Cervix, Colon, and Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-759.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
RT "Systematic subcellular localization of novel proteins identified by large-
RT scale cDNA sequencing.";
RL EMBO Rep. 1:287-292(2000).
RN [10]
RP ALTERNATIVE PROMOTER USAGE, AND INDUCTION.
RX PubMed=10806352; DOI=10.1016/s0378-1119(00)00144-x;
RA Chen S., Maul R.S., Kim H.R., Chang D.D.;
RT "Characterization of the human EPLIN (Epithelial protein lost in neoplasm)
RT gene reveals distinct promoters for the two EPLIN isoforms.";
RL Gene 248:69-76(2000).
RN [11]
RP FUNCTION, AND ACTIN-BINDING REGION.
RX PubMed=12566430; DOI=10.1083/jcb.200212057;
RA Maul R.S., Song Y., Amann K.J., Gerbin S.C., Pollard T.D., Chang D.D.;
RT "EPLIN regulates actin dynamics by cross-linking and stabilizing
RT filaments.";
RL J. Cell Biol. 160:399-407(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-490; SER-686 AND
RP SER-692, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-362 AND SER-490, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-686 AND SER-692, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-225; TYR-229;
RP SER-362; SER-374; SER-490; SER-604; SER-609; SER-617; SER-686; SER-692 AND
RP SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-617 AND SER-686, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-132; SER-225; SER-263; SER-343; SER-362; SER-374;
RP SER-490; SER-604; SER-686 AND SER-692, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-343 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-183 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-350; SER-362;
RP SER-365; SER-369; SER-374; SER-490; SER-686; SER-698 AND SER-726, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 5 AND ALPHA), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-15; SER-55; SER-132;
RP SER-263; SER-362; SER-374; SER-490; SER-601; SER-604; SER-609; SER-617 AND
RP SER-686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-362; SER-365;
RP SER-374 AND SER-490, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
RX PubMed=24694988; DOI=10.1038/ki.2014.85;
RA Tsurumi H., Harita Y., Kurihara H., Kosako H., Hayashi K., Matsunaga A.,
RA Kajiho Y., Kanda S., Miura K., Sekine T., Oka A., Ishizuka K., Horita S.,
RA Hattori M., Hattori S., Igarashi T.;
RT "Epithelial protein lost in neoplasm modulates platelet-derived growth
RT factor-mediated adhesion and motility of mesangial cells.";
RL Kidney Int. 86:548-557(2014).
RN [26]
RP VARIANT ILE-25, CHARACTERIZATION OF VARIANT ILE-25, INTERACTION WITH NPCL1,
RP AND POLYMORPHISM.
RX PubMed=29880681; DOI=10.1126/science.aao6575;
RA Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J.,
RA Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y., Li B.L.,
RA Ma Y.T., Song B.L.;
RT "A LIMA1 variant promotes low plasma LDL cholesterol and decreases
RT intestinal cholesterol absorption.";
RL Science 360:1087-1092(2018).
RN [27]
RP STRUCTURE BY NMR OF 381-460.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the LIM domain of epithelial protein lost in
RT neoplasm.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Actin-binding protein involved in actin cytoskeleton
CC regulation and dynamics. Increases the number and size of actin stress
CC fibers and inhibits membrane ruffling. Inhibits actin filament
CC depolymerization. Bundles actin filaments, delays filament nucleation
CC and reduces formation of branched filaments (PubMed:12566430). Plays a
CC role in cholesterol homeostasis. Influences plasma cholesterol levels
CC through regulation of intestinal cholesterol absorption. May act as a
CC scaffold protein by regulating NPC1L1 transportation, an essential
CC protein for cholesterol absorption, to the plasma membrane by
CC recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By
CC similarity). {ECO:0000250|UniProtKB:Q9ERG0,
CC ECO:0000269|PubMed:12566430}.
CC -!- SUBUNIT: Interacts with NPCL1; bridges NPC1L1 with MYO5B
CC (PubMed:29880681). Interacts with MYO5B; bridges NPC1L1 with MYO5B
CC (PubMed:29880681). Interacts with PXN; this complex stabilizes actin
CC dynamics (PubMed:24694988). Interacts with F-actin and G-actin
CC (PubMed:12566430). {ECO:0000269|PubMed:12566430,
CC ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681}.
CC -!- INTERACTION:
CC Q9UHB6; P12830: CDH1; NbExp=2; IntAct=EBI-351479, EBI-727477;
CC Q9UHB6; P35221: CTNNA1; NbExp=2; IntAct=EBI-351479, EBI-701918;
CC Q9UHB6; P53355: DAPK1; NbExp=2; IntAct=EBI-351479, EBI-358616;
CC Q9UHB6; O46385: SVIL; Xeno; NbExp=3; IntAct=EBI-351479, EBI-6995105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:10618726, ECO:0000269|PubMed:24694988}. Cytoplasm,
CC cytoskeleton. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:10618726}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9ERG0}. Note=Expressed in the brush border
CC membrane of the small intestine and colocalizes with NPC1L1 and MYO5B
CC (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial
CC cells (PubMed:24694988). Colocalizes with actin stress fibers in
CC quiescent cells. PDGF stimulation induced disassembly of stress fibers
CC and formation of peripheral and dorsal ruffles, where LIMA1 is
CC relocalized (By similarity). {ECO:0000250|UniProtKB:Q9ERG0,
CC ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=Beta;
CC IsoId=Q9UHB6-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q9UHB6-2; Sequence=VSP_003116;
CC Name=3;
CC IsoId=Q9UHB6-3; Sequence=VSP_003117;
CC Name=4;
CC IsoId=Q9UHB6-4; Sequence=VSP_040136;
CC Name=5;
CC IsoId=Q9UHB6-5; Sequence=VSP_003116, VSP_040136;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, kidney, pancreas,
CC prostate, ovary, spleen and heart. Also detected in lung, liver, brain,
CC skeletal muscle, thymus, testis and intestine. Not detected in
CC leukocytes. Isoform Beta expressed generally at very low levels.
CC Isoform Alpha abundant in epithelial cells from mammary gland, prostate
CC and in normal oral keratinocytes. Low levels in aortic endothelial
CC cells and dermal fibroblasts. Not detectable in myocardium.
CC {ECO:0000269|PubMed:24694988}.
CC -!- INDUCTION: Down-regulated in some cancer cell lines. Isoform Alpha is
CC induced by serum. Isoform Beta is constitutively expressed.
CC {ECO:0000269|PubMed:10806352}.
CC -!- DOMAIN: Contains at least 2 actin-binding domains, one on each side of
CC the LIM domain. Both domains bind actin monomers and filaments. The C-
CC terminal domain binds filaments more efficiently than the N-terminus.
CC {ECO:0000269|PubMed:12566430}.
CC -!- PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces
CC its association with F-actin and contributes to actin filament
CC reorganization and enhances cell motility.
CC {ECO:0000250|UniProtKB:Q9ERG0}.
CC -!- POLYMORPHISM: Genetic variations in LIMA1 influence low density
CC lipoprotein cholesterol (LDL-C) variability and contribute to the low
CC density lipoprotein cholesterol level quantitative trait locus 8
CC (LDLCQ8) [MIM:618079]. {ECO:0000269|PubMed:29880681}.
CC -!- MISCELLANEOUS: [Isoform Beta]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform Alpha]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC Beta. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17267.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91120.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92749.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF198454; AAF23755.1; -; mRNA.
DR EMBL; AF198455; AAF23756.1; -; mRNA.
DR EMBL; AF157325; AAF67491.1; -; mRNA.
DR EMBL; AL136911; CAB66845.1; -; mRNA.
DR EMBL; AK000372; BAA91120.1; ALT_FRAME; mRNA.
DR EMBL; AK000335; BAA91092.1; -; mRNA.
DR EMBL; AK023649; BAB14625.1; -; mRNA.
DR EMBL; AK000057; BAA90914.1; -; mRNA.
DR EMBL; AK314447; BAG37056.1; -; mRNA.
DR EMBL; AB209512; BAD92749.1; ALT_INIT; mRNA.
DR EMBL; CH471111; EAW58135.1; -; Genomic_DNA.
DR EMBL; BC001247; AAH01247.2; -; mRNA.
DR EMBL; BC010664; AAH10664.1; -; mRNA.
DR EMBL; BC110815; AAI10816.1; -; mRNA.
DR EMBL; BC136763; AAI36764.1; -; mRNA.
DR EMBL; AF218025; AAG17267.1; ALT_FRAME; mRNA.
DR CCDS; CCDS44877.1; -. [Q9UHB6-4]
DR CCDS; CCDS55826.1; -. [Q9UHB6-5]
DR CCDS; CCDS58230.1; -. [Q9UHB6-3]
DR CCDS; CCDS8802.1; -. [Q9UHB6-1]
DR RefSeq; NP_001107018.1; NM_001113546.1. [Q9UHB6-4]
DR RefSeq; NP_001107019.1; NM_001113547.1. [Q9UHB6-5]
DR RefSeq; NP_001230704.1; NM_001243775.1. [Q9UHB6-3]
DR RefSeq; NP_057441.1; NM_016357.4. [Q9UHB6-1]
DR RefSeq; XP_011536757.1; XM_011538455.2. [Q9UHB6-4]
DR RefSeq; XP_016874919.1; XM_017019430.1. [Q9UHB6-3]
DR PDB; 2D8Y; NMR; -; A=381-457.
DR PDBsum; 2D8Y; -.
DR AlphaFoldDB; Q9UHB6; -.
DR SMR; Q9UHB6; -.
DR BioGRID; 119559; 379.
DR DIP; DIP-29633N; -.
DR IntAct; Q9UHB6; 238.
DR MINT; Q9UHB6; -.
DR STRING; 9606.ENSP00000378400; -.
DR GlyGen; Q9UHB6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHB6; -.
DR MetOSite; Q9UHB6; -.
DR PhosphoSitePlus; Q9UHB6; -.
DR BioMuta; LIMA1; -.
DR DMDM; 20138067; -.
DR EPD; Q9UHB6; -.
DR jPOST; Q9UHB6; -.
DR MassIVE; Q9UHB6; -.
DR MaxQB; Q9UHB6; -.
DR PaxDb; Q9UHB6; -.
DR PeptideAtlas; Q9UHB6; -.
DR PRIDE; Q9UHB6; -.
DR ProteomicsDB; 84296; -. [Q9UHB6-1]
DR ProteomicsDB; 84297; -. [Q9UHB6-2]
DR ProteomicsDB; 84298; -. [Q9UHB6-3]
DR ProteomicsDB; 84299; -. [Q9UHB6-4]
DR Antibodypedia; 14200; 337 antibodies from 33 providers.
DR DNASU; 51474; -.
DR Ensembl; ENST00000341247.9; ENSP00000340184.4; ENSG00000050405.14. [Q9UHB6-1]
DR Ensembl; ENST00000394943.7; ENSP00000378400.3; ENSG00000050405.14. [Q9UHB6-4]
DR Ensembl; ENST00000547825.5; ENSP00000448706.1; ENSG00000050405.14. [Q9UHB6-3]
DR Ensembl; ENST00000552783.5; ENSP00000448779.1; ENSG00000050405.14. [Q9UHB6-5]
DR Ensembl; ENST00000552823.5; ENSP00000450266.1; ENSG00000050405.14. [Q9UHB6-2]
DR GeneID; 51474; -.
DR KEGG; hsa:51474; -.
DR MANE-Select; ENST00000341247.9; ENSP00000340184.4; NM_016357.5; NP_057441.1.
DR UCSC; uc001rwg.5; human. [Q9UHB6-1]
DR CTD; 51474; -.
DR DisGeNET; 51474; -.
DR GeneCards; LIMA1; -.
DR HGNC; HGNC:24636; LIMA1.
DR HPA; ENSG00000050405; Low tissue specificity.
DR MalaCards; LIMA1; -.
DR MIM; 608364; gene.
DR MIM; 618079; phenotype.
DR neXtProt; NX_Q9UHB6; -.
DR OpenTargets; ENSG00000050405; -.
DR PharmGKB; PA143485527; -.
DR VEuPathDB; HostDB:ENSG00000050405; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158313; -.
DR HOGENOM; CLU_021314_1_0_1; -.
DR InParanoid; Q9UHB6; -.
DR OMA; PEVCISH; -.
DR OrthoDB; 1583903at2759; -.
DR PhylomeDB; Q9UHB6; -.
DR TreeFam; TF350273; -.
DR PathwayCommons; Q9UHB6; -.
DR SignaLink; Q9UHB6; -.
DR SIGNOR; Q9UHB6; -.
DR BioGRID-ORCS; 51474; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; LIMA1; human.
DR EvolutionaryTrace; Q9UHB6; -.
DR GeneWiki; LIMA1; -.
DR GenomeRNAi; 51474; -.
DR Pharos; Q9UHB6; Tbio.
DR PRO; PR:Q9UHB6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UHB6; protein.
DR Bgee; ENSG00000050405; Expressed in oocyte and 202 other tissues.
DR ExpressionAtlas; Q9UHB6; baseline and differential.
DR Genevisible; Q9UHB6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISS:UniProtKB.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; IDA:UniProtKB.
DR InterPro; IPR028740; EPLIN.
DR InterPro; IPR045268; LIMA-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 2.
DR PANTHER; PTHR24206:SF57; PTHR24206:SF57; 2.
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 3D-structure; Acetylation; Actin-binding; Alternative promoter usage;
KW Alternative splicing; Cell junction; Cell membrane; Cholesterol metabolism;
KW Cytoplasm; Cytoskeleton; LIM domain; Lipid metabolism; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Steroid metabolism;
KW Sterol metabolism; Zinc.
FT CHAIN 1..759
FT /note="LIM domain and actin-binding protein 1"
FT /id="PRO_0000075730"
FT DOMAIN 388..448
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 78..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..513
FT /note="Required for interaction with MYO5B"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT REGION 509..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..166
FT /note="Required for interaction with NPC1L1"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 229
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 439
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT VAR_SEQ 1..302
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_003117"
FT VAR_SEQ 1..160
FT /note="Missing (in isoform Alpha and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10618726,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_003116"
FT VAR_SEQ 344
FT /note="R -> PG (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10931946, ECO:0000303|Ref.5"
FT /id="VSP_040136"
FT VARIANT 25
FT /note="L -> I (associated with lower plasma levels of low-
FT density lipoprotein cholesterol; reduces protein stability;
FT dbSNP:rs140372565)"
FT /evidence="ECO:0000269|PubMed:29880681"
FT /id="VAR_080864"
FT CONFLICT 381
FT /note="Missing (in Ref. 4; BAA90914 and 7; AAH01247)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="F -> L (in Ref. 8; AAG17267)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> G (in Ref. 4; BAA90914)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="P -> Q (in Ref. 2; AAF67491)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..521
FT /note="DK -> NR (in Ref. 2; AAF67491)"
FT /evidence="ECO:0000305"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:2D8Y"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2D8Y"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2D8Y"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:2D8Y"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:2D8Y"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2D8Y"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:2D8Y"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:2D8Y"
FT HELIX 439..445
FT /evidence="ECO:0007829|PDB:2D8Y"
FT MOD_RES Q9UHB6-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9UHB6-4:343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9UHB6-5:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9UHB6-5:183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 759 AA; 85226 MW; 996378AFD3B003D5 CRC64;
MESSPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEETNM EKKRSNTENL
SQHFRKGTLT VLKKKWENPG LGAESHTDSL RNSSTEIRHR ADHPPAEVTS HAASGAKADQ
EEQIHPRSRL RSPPEALVQG RYPHIKDGED LKDHSTESKK MENCLGESRH EVEKSEISEN
TDASGKIEKY NVPLNRLKMM FEKGEPTQTK ILRAQSRSAS GRKISENSYS LDDLEIGPGQ
LSSSTFDSEK NESRRNLELP RLSETSIKDR MAKYQAAVSK QSSSTNYTNE LKASGGEIKI
HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE DDSRDSQVKS EVQQPVHPKP
LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM ERLLANQQVF HISCFRCSYC
NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG NYDEGFGHRP HKDLWASKNE NEEILERPAQ
LANARETPHS PGVEDAPIAK VGVLAASMEA KASSQQEKED KPAETKKLRI AWPPPTELGS
SGSALEEGIK MSKPKWPPED EISKPEVPED VDLDLKKLRR SSSLKERSRP FTVAASFQST
SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK ASKKNGNVGK TTWQNKESKG
ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ EPKSLNWSSF VDNTFAEEFT
TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR YYDEDEDEE
