Search Results

Overview

Uniprot IDF1LR10
Protein NameLIM domain and actin-binding protein 1
Gene NameLima1
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
189 ETSGKIEKYNVPLNR
198 NVPLNRLKMMFEKGE
203 RLKMMFEKGEHSQNK
210 KGEHSQNKSPWTQGR
268 RLSETSIKDRMAKYQ
273 SIKDRMAKYQAAVSK
300 PSESKTHKWEQKENV
375 LPESSPSKTAKKFQA
445 PHFNQLFKSKGNYDE
447 FNQLFKSKGNYDEGF
457 YDEGFGHKQHKDLWA
575 EDVDLDLKKLRRSSS
648 REKESVGKSRWQSEE

Function

Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Acts as a negative regulator of primary cilium formation (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity)

Protein Sequence

10 MESTPFNRRQ 20 WTSLSLRVTA 30 KELSLVNKNK 40 SSTIVEIFSK 50 YQKAAEEANM 60 ERKKNNTESL 70 PQHFRRGTLS 80 VLKKKWENPV 90 AGAESHTDSL 100 PNSSSDGGHT 110 ADHPPAEVTA 120 KAAPGARADR 130 EEHTQPRSRF 140 GSRPEAVTQC 150 RYPRSEDSHD 160 FKAQATESQN 170 MENCLGDSRH 180 EAEKPEMSEN 190 TETSGKIEKY 200 NVPLNRLKMM 210 FEKGEHSQNK 220 SPWTQGRNAG 230 GRRLSENSCS 240 LDDLEIGAGH 250 LSSSAFNSEK 260 NESKRNLELP 270 RLSETSIKDR 280 MAKYQAAVSK 290 QSSPASYASE 300 LKPSESKTHK 310 WEQKENVPPG 320 PEACSIHQEG 330 SKVSATENSL 340 VAHPVPAEDD 350 TCNSQGRSEA 360 QQPIYTKPLS 370 PDARTSSLPE 380 SSPSKTAKKF 390 QAPARESCVE 400 CQKTVYPMER 410 LLANQQVFHI 420 SCFRCSYCNN 430 KLSLGTYASL 440 HGRIYCKPHF 450 NQLFKSKGNY 460 DEGFGHKQHK 470 DLWASKGENE 480 ETLGRPAQPP 490 SAGETPHSPG 500 VEDAPIAKVG 510 VLAASMEAKA 520 SSQREREENK 530 PAETKKLRIA 540 WPPPAEQGSS 550 GSAPEEGFKV 560 SKPKWPPEDE 570 VCKTEAPEDV 580 DLDLKKLRRS 590 SSLKERSRPF 600 TVAASFRTSS 610 VKSPKPLSPS 620 LRKGWSEPEP 630 EQSEEFGGGT 640 VTQTESPRPS 650 REKESVGKSR 660 WQSEEAEAEA 670 EEAPRGRDGR 680 SFELESESFI 690 GNGASIAEDD 700 VAPAQRSPLE 710 PESPGWPGFG 720 DTTTAKEFNQ 730 KSQDVGFWEG 740 EVVRELSVEE 750 QIKRNRYYDE DEDEE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Biological Process GO:0030299 intestinal cholesterol absorption
Biological Process GO:0030835 negative regulation of actin filament depolymerization
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:1902018 negative regulation of cilium assembly
Biological Process GO:0032233 positive regulation of actin filament bundle assembly
Biological Process GO:1902743 regulation of lamellipodium organization
Biological Process GO:0031529 ruffle organization
Cellular Component GO:0005884 actin filament
Cellular Component GO:0005903 brush border
Cellular Component GO:0031526 brush border membrane
Cellular Component GO:0032154 cleavage furrow
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0001726 ruffle
Cellular Component GO:0001725 stress fiber
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0003785 actin monomer binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0140778 microtubule stabilizing activity
Biological Process GO:0051017 actin filament bundle assembly
Biological Process GO:0016477 cell migration
Biological Process GO:0042632 cholesterol homeostasis
Biological Process GO:0008203 cholesterol metabolic process

Reference

[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.