LOCUS       NP_001001515            1729 aa            linear   ROD 22-SEP-2024
DEFINITION  LIM domain only protein 7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001001515 XP_341369
VERSION     NP_001001515.2
DBSOURCE    REFSEQ: accession NM_001001515.2
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 1729)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1729)
  AUTHORS   Dada,L.A., Trejo Bittar,H.E., Welch,L.C., Vagin,O.,
            Deiss-Yehiely,N., Kelly,A.M., Baker,M.R., Capri,J., Cohn,W.,
            Whitelegge,J.P., Vadasz,I., Gruenbaum,Y. and Sznajder,J.I.
  TITLE     High CO2 Leads to Na,K-ATPase Endocytosis via c-Jun Amino-Terminal
            Kinase-Induced LMO7b Phosphorylation
  JOURNAL   Mol Cell Biol 35 (23), 3962-3973 (2015)
   PUBMED   26370512
  REMARK    GeneRIF: JNK-dependent LMO7b phosphorylation is required for
            hypercapnia-mediated Na,K-ATPase endocytosis.
REFERENCE   3  (residues 1 to 1729)
  AUTHORS   Dedeic,Z., Cetera,M., Cohen,T.V. and Holaska,J.M.
  TITLE     Emerin inhibits Lmo7 binding to the Pax3 and MyoD promoters and
            expression of myoblast proliferation genes
  JOURNAL   J Cell Sci 124 (Pt 10), 1691-1702 (2011)
   PUBMED   21525034
REFERENCE   4  (residues 1 to 1729)
  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   5  (residues 1 to 1729)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 1729)
  AUTHORS   Tanaka-Okamoto,M., Hori,K., Ishizaki,H., Hosoi,A., Itoh,Y., Wei,M.,
            Wanibuchi,H., Mizoguchi,A., Nakamura,H. and Miyoshi,J.
  TITLE     Increased susceptibility to spontaneous lung cancer in mice lacking
            LIM-domain only 7
  JOURNAL   Cancer Sci 100 (4), 608-616 (2009)
   PUBMED   19215226
REFERENCE   7  (residues 1 to 1729)
  AUTHORS   Holaska,J.M., Rais-Bahrami,S. and Wilson,K.L.
  TITLE     Lmo7 is an emerin-binding protein that regulates the transcription
            of emerin and many other muscle-relevant genes
  JOURNAL   Hum Mol Genet 15 (23), 3459-3472 (2006)
   PUBMED   17067998
REFERENCE   8  (residues 1 to 1729)
  AUTHORS   Nakamura,H., Mukai,M., Komatsu,K., Tanaka-Okamoto,M., Itoh,Y.,
            Ishizaki,H., Tatsuta,M., Inoue,M. and Miyoshi,J.
  TITLE     Transforming growth factor-beta1 induces LMO7 while enhancing the
            invasiveness of rat ascites hepatoma cells
  JOURNAL   Cancer Lett 220 (1), 95-99 (2005)
   PUBMED   15737692
REFERENCE   9  (residues 1 to 1729)
  AUTHORS   Ooshio,T., Irie,K., Morimoto,K., Fukuhara,A., Imai,T. and Takai,Y.
  TITLE     Involvement of LMO7 in the association of two cell-cell adhesion
            molecules, nectin and E-cadherin, through afadin and alpha-actinin
            in epithelial cells
  JOURNAL   J Biol Chem 279 (30), 31365-31373 (2004)
   PUBMED   15140894
  REMARK    GeneRIF: LMO7 is an afadin- and alpha-actinin-binding protein that
            connects the nectin-afadin and E-cadherin-catenin systems through
            alpha-actinin.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Sep 14, 2022 this sequence version replaced NP_001001515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY533473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1729
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..1729
                     /product="LIM domain only protein 7 isoform 1"
                     /EC_number="3.4.19.12"
                     /note="LIM domain only protein 7; TGF-beta induced
                     protein; LIM domain only 7"
                     /calculated_mol_wt=195556
     Region          14..129
                     /region_name="CH_LMO7"
                     /note="calponin homology (CH) domain found in LIM domain
                     only protein 7; cd21277"
                     /db_xref="CDD:409126"
     Site            order(14,18,68,70..71,74..75,77,87..95,113,115..116,
                     118..119,122..123,126)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409126"
     Region          242..>304
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          588..735
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          1082..1150
                     /region_name="PDZ"
                     /note="Domain present in PSD-95, Dlg, and ZO-1/2;
                     smart00228"
                     /db_xref="CDD:214570"
     Region          1660..1718
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cd08368"
                     /db_xref="CDD:259829"
     Site            order(1660,1663,1683,1686,1689,1692,1714,1717)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..1729
                     /gene="Lmo7"
                     /coded_by="NM_001001515.2:215..5404"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361084"
                     /db_xref="RGD:1302984"
ORIGIN      
        1 megmedaead csvafaeaqr wveavteknf etrdfrasle ngvllcdlin klkpgvvrki
       61 nrlstpiagl dninvflkac eqiglkeaql fhpgdlqdls nrvtvkqeet drrlknvlit
      121 lywlgrkaqn npyyhgpyln lkafetllgq altkaledss clkrsgrdsg ygdiwcpdrg
      181 dfpappgshr redsfeslds lgsrsltscs sdltlrggre gcesdndwef tfkmqdynkd
      241 dmsyrrisai epksalpfnr flpnkskqps yvpaplrkkr pdknednrrs waspvytete
      301 gtfsstqrra wgpkmenwht vqetstsswc leeeeekvtr lpnvvkddly vrklspvmps
      361 pgssfdqflp kgwtpedmnw kkikretykp wykefqglsq flllqalqty sddilssetn
      421 vkldptsgpr litrrknfsp tpgyrahdle pqsldpdlen ddffvrktra fhanpcvlra
      481 fedfrrfsep ddaverdiil qcregelvlp dlekddmivr ripaqkkevp lsgapdryqp
      541 vpfpepwtlp peiqakflsv lertcppkdk psscrvlvps hrlkkddmlt rkiqswklgt
      601 avppisfrpg pcseadlrkw eaireasrlr hrkrlmverl fqkiygengs kslsdvsaed
      661 vqslrqlrye emqkiksqlk eqdqkwqddl akwkdrrksy tsdlqkkkee reeiekqale
      721 ksdrssktfr emlqdresqs stttsrrriy ssddilddgv lpptvtlset syqserledk
      781 arahpaempk edsttfasre dgiaaeipla shipeerrqa pwpsaetrqa ssssaeshqa
      841 slpstesdqa rlpsaephqa sfssaeprqv plvsaephqa ssfsstephq aslssalqrp
      901 sslsssqqsw strgestris aslprsyqrs dtarltsvvt arpfgtssrg isslprsytm
      961 ddgwkyngdv evvkreqhds graagmkpds shfilgssse kevatgedva slssfvlpss
     1021 sslshdqaas skatfsstsg ldsvsdsgeg rssslrevsr spdqfsdmri sinqtpgtkh
     1081 dfgftikwdv sgisvasvek gspaefsqlq vddeilainn tkfsykdtkk weeamanaqe
     1141 tgnlvmdvrr ygksgspetk widttsgiys tekssslsvt tdfseslqsp yseskeingi
     1201 heesnafdsk asesislknl krrsqffeqg ssdsvapdlp vptlsapsrw awdqeeerrr
     1261 qerwqkeqdr llqekyqreq eklreewqra qqeaerensk yldeelmvln snsisltsre
     1321 svtaswepsw segsksldre gtragdedrg qleddavyed qsqklqerlm lehekkrkeq
     1381 eaqeeelrkq reaeaqarae aeaqaraeaq araeaqaqae aearkraeaq klqaereret
     1441 svkiyqyrrp idsydlpkre eessgllpid rsksrsttel ndplieksgs skysdrigtt
     1501 sfsqrsskkd qgpseaeler qqilqemrkk tslhndnswi rqrsasvnke picltgimrr
     1561 gesldnldsq rpgswrqssw hsqpagvyas ssvqdfsrlp pqllstsnra ymrnpssavp
     1621 plagsvktsp gspsprshsp smsqsgsqlr nrsvsgkrvc sycnsilgkg aamiietlgl
     1681 cyhlhcfkcv scerdlggss sgaevrirnh qlycndcylr fksgrptam
//
