LIMA1_PIG
ID LIMA1_PIG Reviewed; 756 AA.
AC B0KYV5; B0KYV6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=LIM domain and actin-binding protein 1 {ECO:0000250|UniProtKB:Q9UHB6};
DE AltName: Full=Epithelial protein lost in neoplasm {ECO:0000303|PubMed:17453649};
GN Name=LIMA1 {ECO:0000250|UniProtKB:Q9UHB6};
GN Synonyms=EPLIN {ECO:0000303|PubMed:17453649};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC96266.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Longissimus dorsi muscle {ECO:0000269|PubMed:17453649};
RX PubMed=17453649; DOI=10.1080/10495390600864660;
RA Wang H., Wang H., Zhu Z., Yang S., Feng S., Li K.;
RT "Characterization of porcine EPLIN gene revealed distinct expression
RT patterns for the two isoforms.";
RL Anim. Biotechnol. 18:101-108(2007).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:17453649}; Synonyms=EPLIN-beta
CC {ECO:0000303|PubMed:17453649}, EPLIN-b {ECO:0000312|EMBL:ABC96266.1};
CC IsoId=B0KYV5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:17453649}; Synonyms=EPLIN-alpha
CC {ECO:0000303|PubMed:17453649}, EPLIN-a {ECO:0000312|EMBL:ABC96267.1};
CC IsoId=B0KYV5-2; Sequence=VSP_044628;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels of isoform 2 are
CC expressed in lung, spleen and small intestine. Isoform 2 is expressed
CC at higher levels than isoform 1 in most tissues except liver, fat and
CC kidney. Isoform 1 and isoform 2 are expressed at low levels in skeletal
CC muscle, heart, stomach and lymph. {ECO:0000269|PubMed:17453649}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed at low levels at embryonic
CC day 33 (E33) and in the adult. Isoform 2 is expressed abundantly
CC throughout embryonic development with a peak at E65 and is expressed at
CC lower levels in the neonate and adult. Isoform 1 and isoform 2 are
CC expressed at similar levels in the adult.
CC {ECO:0000269|PubMed:17453649}.
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 (By similarity). {ECO:0000250|UniProtKB:Q9UHB6}.
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}.
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DR EMBL; DQ364062; ABC96266.1; -; mRNA.
DR EMBL; DQ364063; ABC96267.1; -; mRNA.
DR RefSeq; NP_001108148.1; NM_001114676.1. [B0KYV5-1]
DR AlphaFoldDB; B0KYV5; -.
DR SMR; B0KYV5; -.
DR STRING; 9823.ENSSSCP00000026919; -.
DR PaxDb; B0KYV5; -.
DR PeptideAtlas; B0KYV5; -.
DR PRIDE; B0KYV5; -.
DR GeneID; 100137084; -.
DR KEGG; ssc:100137084; -.
DR CTD; 51474; -.
DR eggNOG; KOG1700; Eukaryota.
DR InParanoid; B0KYV5; -.
DR OrthoDB; 1583903at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
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:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Alternative promoter usage; 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..756
FT /note="LIM domain and actin-binding protein 1"
FT /id="PRO_0000420756"
FT DOMAIN 384..444
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 44..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..509
FT /note="Required for interaction with MYO5B"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT REGION 508..726
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 139..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..724
FT /note="Polar 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 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 435
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG0"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17453649"
FT /id="VSP_044628"
SQ SEQUENCE 756 AA; 83990 MW; 16FF83C6FEF1A489 CRC64;
MESTPFNRQQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEEANM EKRRSNTENL
PQHFRRGNLT VLKKKWENPA PGVESLPEST RNSSAEVRHR GDPPPAEVAS SSASGVEADQ
GVCPRPRFSS PPEVPYPNPR IKDTEHLKDH SAESKKMENC LAESRHEVGK PETSENAEAS
NKIEKYNVPL NRLKMMFERG EPAQTKILRA QSRSTGGRKI SENSYSLDDL EIGPGQLSSS
AFNTEKSESR RNLEFPRLSD TSIKDRMAKY QAAVSKQSSS TNYTNELKAN GGEIKTHKLE
QKENVPPGPE VCISHQDGEK VSASENSLAA CSTPPEDDSC KSQVKSDVQQ PVHPKPLSPV
ARASSLSESS PPKAVKKFQA PARETCVECQ KTVYPMERLL ANQQVFHISC FRCSYCNNKL
SLGTYASLHG RIYCKPHFNQ LFKSKGNYDE GFGHRPHKDL WASKLENEET LERPAQLPNA
AEIPQSPGVE DAPIAKVGVL TASMEAKASS QLEKEDKPAE TKKLRIAWPP PTELSSSGSA
LEEGIKVSKP KWPPEDEVSK PEAPEDVDLD LKKLRRSSSL KERSRPFTVA ASFRTASVKS
PKPLSPPMRK GWSLSEQSEE FGGGVAAERK QMEKASASEK NGSVGKTTWP SKESRGGEAA
GRSKEVQDFE IGSENLIENG ASLDEGDRDL LQQQSPLEPK SKNWSSFADN TSAKEFTTQK
QKSQDVEFWE GEVVEELSVE EQIKRNRYYD EEEDEE
