LOCUS       NP_001178544             755 aa            linear   ROD 01-APR-2024
DEFINITION  LIM domain and actin-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_001178544 XP_006257417 XP_217039
VERSION     NP_001178544.1
DBSOURCE    REFSEQ: accession NM_001191615.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Zhang,Y.Y., Fu,Z.Y., Wei,J., Qi,W., Baituola,G., Luo,J., Meng,Y.J.,
            Guo,S.Y., Yin,H., Jiang,S.Y., Li,Y.F., Miao,H.H., Liu,Y., Wang,Y.,
            Li,B.L., Ma,Y.T. and Song,B.L.
  TITLE     A LIMA1 variant promotes low plasma LDL cholesterol and decreases
            intestinal cholesterol absorption
  JOURNAL   Science 360 (6393), 1087-1092 (2018)
   PUBMED   29880681
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Tsurumi,H., Harita,Y., Kurihara,H., Kosako,H., Hayashi,K.,
            Matsunaga,A., Kajiho,Y., Kanda,S., Miura,K., Sekine,T., Oka,A.,
            Ishizuka,K., Horita,S., Hattori,M., Hattori,S. and Igarashi,T.
  TITLE     Epithelial protein lost in neoplasm modulates platelet-derived
            growth factor-mediated adhesion and motility of mesangial cells
  JOURNAL   Kidney Int 86 (3), 548-557 (2014)
   PUBMED   24694988
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   5  (residues 1 to 755)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 755)
  AUTHORS   Smith,T.C., Fang,Z. and Luna,E.J.
  TITLE     Novel interactors and a role for supervillin in early cytokinesis
  JOURNAL   Cytoskeleton (Hoboken) 67 (6), 346-364 (2010)
   PUBMED   20309963
REFERENCE   7  (residues 1 to 755)
  AUTHORS   Han,M.Y., Kosako,H., Watanabe,T. and Hattori,S.
  TITLE     Extracellular signal-regulated kinase/mitogen-activated protein
            kinase regulates actin organization and cell motility by
            phosphorylating the actin cross-linking protein EPLIN
  JOURNAL   Mol Cell Biol 27 (23), 8190-8204 (2007)
   PUBMED   17875928
REFERENCE   8  (residues 1 to 755)
  AUTHORS   Maul,R.S., Song,Y., Amann,K.J., Gerbin,S.C., Pollard,T.D. and
            Chang,D.D.
  TITLE     EPLIN regulates actin dynamics by cross-linking and stabilizing
            filaments
  JOURNAL   J Cell Biol 160 (3), 399-407 (2003)
   PUBMED   12566430
REFERENCE   9  (residues 1 to 755)
  AUTHORS   Maul,R.S., Sachi Gerbin,C. and Chang,D.D.
  TITLE     Characterization of mouse epithelial protein lost in neoplasm
            (EPLIN) and comparison of mammalian and zebrafish EPLIN
  JOURNAL   Gene 262 (1-2), 155-160 (2001)
   PUBMED   11179679
REFERENCE   10 (residues 1 to 755)
  AUTHORS   Maul,R.S. and Chang,D.D.
  TITLE     EPLIN, epithelial protein lost in neoplasm
  JOURNAL   Oncogene 18 (54), 7838-7841 (1999)
   PUBMED   10618726
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Dec 15, 2022 this sequence version replaced
            XP_006257417.1, XP_217039.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.944759.1,
                                           SRR26643289.22006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..755
                     /product="LIM domain and actin-binding protein 1"
                     /note="epithelial protein lost in neoplasm"
                     /calculated_mol_wt=83666
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          43..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          164..166
                     /region_name="Required for interaction with NPC1L1.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          168..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          241..379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          388..440
                     /region_name="LIM_Eplin_alpha_beta"
                     /note="The Lim domain of Epithelial Protein Lost in
                     Neoplasm (Eplin); cd09485"
                     /db_xref="CDD:188869"
     Site            order(388,391,409,412,415,418,436,439)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188869"
     Region          468..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          491..511
                     /region_name="Required for interaction with MYO5B.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Region          505..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHB6; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (F1LR10.2)"
     CDS             1..755
                     /gene="Lima1"
                     /gene_synonym="eplin"
                     /coded_by="NM_001191615.3:121..2388"
                     /db_xref="GeneID:300228"
                     /db_xref="RGD:1564050"
ORIGIN      
        1 mestpfnrrq wtslslrvta kelslvnknk sstiveifsk yqkaaeeanm erkknntesl
       61 pqhfrrgtls vlkkkwenpv agaeshtdsl pnsssdgght adhppaevta kaapgaradr
      121 eehtqprsrf gsrpeavtqc ryprsedshd fkaqatesqn menclgdsrh eaekpemsen
      181 tetsgkieky nvplnrlkmm fekgehsqnk spwtqgrnag grrlsenscs lddleigagh
      241 lsssafnsek neskrnlelp rlsetsikdr makyqaavsk qsspasyase lkpseskthk
      301 weqkenvppg peacsihqeg skvsatensl vahpvpaedd tcnsqgrsea qqpiytkpls
      361 pdartsslpe sspsktakkf qaparescve cqktvypmer llanqqvfhi scfrcsycnn
      421 klslgtyasl hgriyckphf nqlfkskgny degfghkqhk dlwaskgene etlgrpaqpp
      481 sagetphspg vedapiakvg vlaasmeaka ssqrereenk paetkklria wpppaeqgss
      541 gsapeegfkv skpkwppede vckteapedv dldlkklrrs sslkersrpf tvaasfrtss
      601 vkspkplsps lrkgwsepep eqseefgggt vtqtesprps rekesvgksr wqseeaeaea
      661 eeaprgrdgr sfelesesfi gngasiaedd vapaqrsple pespgwpgfg dtttakefnq
      721 ksqdvgfweg evvrelsvee qikrnryyde dedee
//
