LIMA1_RAT
ID LIMA1_RAT Reviewed; 755 AA.
AC F1LR10; G3V8I6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=LIM domain and actin-binding protein 1;
DE AltName: Full=Epithelial protein lost in neoplasm;
GN Name=Lima1 {ECO:0000312|RGD:1564050}; Synonyms=eplin;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP TISSUE SPECIFICITY.
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).
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 (By similarity). 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:0000250|UniProtKB:Q9UHB6}.
CC -!- SUBUNIT: Interacts with NPC1L1; bridges NPC1L1 with MYO5B. Interacts
CC with MYO5B; bridges MYO5B with NPC1L1 (By similarity). Interacts with
CC PXN; this complex stabilizes actin dynamics. Interacts with F-actin and
CC G-actin (By similarity). {ECO:0000250|UniProtKB:Q9ERG0,
CC ECO:0000250|UniProtKB:Q9UHB6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB6}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9ERG0}. Note=This cytoskeletal protein
CC colocalizes with actin stress fibers and focal adhesion plaques.
CC Expressed mainly in the brush border membrane of the small intestine
CC and colocalizes with NPC1L1 and MYO5B (By similarity). Colocalizes with
CC PXN at focal adhesions in mesangial cells (By similarity). Colocalizes
CC with actin stress fibers in quiescent cells. PDGF stimulation induced
CC disassembly of stress fibers and formation of peripheral and dorsal
CC ruffles, where LIMA1 is relocalized (By similarity).
CC {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000250|UniProtKB:Q9UHB6}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the kidney, including renal
CC cortex, medulla, and glomeruli (PubMed:24694988). Expressed in
CC glomeruli, tubular epithelial cells, and extraglomerular vascular
CC endothelial cells (at protein level) (PubMed:24694988).
CC {ECO:0000269|PubMed:24694988}.
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 enhanced cell motility.
CC {ECO:0000250|UniProtKB:Q9ERG0}.
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DR EMBL; AABR07058874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07058881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07073547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474035; EDL86966.1; -; Genomic_DNA.
DR RefSeq; NP_001178544.1; NM_001191615.2.
DR RefSeq; XP_006257417.1; XM_006257355.3.
DR AlphaFoldDB; F1LR10; -.
DR SMR; F1LR10; -.
DR IntAct; F1LR10; 2.
DR STRING; 10116.ENSRNOP00000063172; -.
DR jPOST; F1LR10; -.
DR PaxDb; F1LR10; -.
DR PRIDE; F1LR10; -.
DR Ensembl; ENSRNOT00000091702; ENSRNOP00000072604; ENSRNOG00000059801.
DR GeneID; 300228; -.
DR KEGG; rno:300228; -.
DR CTD; 51474; -.
DR RGD; 1564050; Lima1.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158313; -.
DR HOGENOM; CLU_021314_0_0_1; -.
DR InParanoid; F1LR10; -.
DR OMA; PEVCISH; -.
DR OrthoDB; 1583903at2759; -.
DR TreeFam; TF350273; -.
DR PRO; PR:F1LR10; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000059801; Expressed in duodenum and 20 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0032154; C:cleavage furrow; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; ISS: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 Acetylation; Actin-binding; Cell junction; Cell membrane;
KW Cholesterol metabolism; Cytoplasm; Cytoskeleton; LIM domain;
KW Lipid metabolism; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Zinc.
FT CHAIN 1..755
FT /note="LIM domain and actin-binding protein 1"
FT /id="PRO_0000445466"
FT DOMAIN 386..446
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 43..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Required for interaction with MYO5B"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT REGION 505..714
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 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
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:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 437
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
SQ SEQUENCE 755 AA; 83797 MW; B97CE0D0B4B5E90B CRC64;
MESTPFNRRQ WTSLSLRVTA KELSLVNKNK SSTIVEIFSK YQKAAEEANM ERKKNNTESL
PQHFRRGTLS VLKKKWENPV AGAESHTDSL PNSSSDGGHT ADHPPAEVTA KAAPGARADR
EEHTQPRSRF GSRPEAVTQC RYPRSEDSHD FKAQATESQN MENCLGDSRH EAEKPEMSEN
TETSGKIEKY NVPLNRLKMM FEKGEHSQNK SPWTQGRNAG GRRLSENSCS LDDLEIGAGH
LSSSAFNSEK NESKRNLELP RLSETSIKDR MAKYQAAVSK QSSPASYASE LKPSESKTHK
WEQKENVPPG PEACSIHQEG SKVSATENSL VAHPVPAEDD TCNSQGRSEA QQPIYTKPLS
PDARTSSLPE SSPSKTAKKF QAPARESCVE CQKTVYPMER LLANQQVFHI SCFRCSYCNN
KLSLGTYASL HGRIYCKPHF NQLFKSKGNY DEGFGHKQHK DLWASKGENE ETLGRPAQPP
SAGETPHSPG VEDAPIAKVG VLAASMEAKA SSQREREENK PAETKKLRIA WPPPAEQGSS
GSAPEEGFKV SKPKWPPEDE VCKTEAPEDV DLDLKKLRRS SSLKERSRPF TVAASFRTSS
VKSPKPLSPS LRKGWSEPEP EQSEEFGGGT VTQTESPRPS REKESVGKSR WQSEEAEAEA
EEAPRGRDGR SFELESESFI GNGASIAEDD VAPAQRSPLE PESPGWPGFG DTTTAKEFNQ
KSQDVGFWEG EVVRELSVEE QIKRNRYYDE DEDEE
