ID   LMOD2_RAT               Reviewed;         549 AA.
AC   A1A5Q0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Leiomodin-2;
DE   AltName: Full=Cardiac leiomodin;
DE            Short=C-LMOD;
DE   AltName: Full=Leiomodin {ECO:0000303|PubMed:18403713};
GN   Name=Lmod2;
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 MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18403713; DOI=10.1126/science.1155313;
RA   Chereau D., Boczkowska M., Skwarek-Maruszewska A., Fujiwara I., Hayes D.B.,
RA   Rebowski G., Lappalainen P., Pollard T.D., Dominguez R.;
RT   "Leiomodin is an actin filament nucleator in muscle cells.";
RL   Science 320:239-243(2008).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20685966; DOI=10.1091/mbc.e10-02-0109;
RA   Skwarek-Maruszewska A., Boczkowska M., Zajac A.L., Kremneva E.,
RA   Svitkina T., Dominguez R., Lappalainen P.;
RT   "Different localizations and cellular behaviors of leiomodin and
RT   tropomodulin in mature cardiomyocyte sarcomeres.";
RL   Mol. Biol. Cell 21:3352-3361(2010).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-24 AND
RP   SER-406, AND 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).
CC   -!- FUNCTION: Mediates nucleation of actin filaments and thereby promotes
CC       actin polymerization (PubMed:18403713). Plays a role in the regulation
CC       of actin filament length (By similarity). Required for normal sarcomere
CC       organization in the heart, and for normal heart function
CC       (PubMed:18403713). {ECO:0000250|UniProtKB:Q6P5Q4,
CC       ECO:0000269|PubMed:18403713}.
CC   -!- SUBUNIT: Can bind at least three actin monomers and thereby provides a
CC       nucleus for actin filament formation. Interacts (via N-terminus) with
CC       tropomyosin alpha (TPM1) (via N-terminus). May also interact with TPM2
CC       (via N-terminus). {ECO:0000250|UniProtKB:Q6P5Q4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm,
CC       myofibril {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril,
CC       sarcomere, M line {ECO:0000269|PubMed:18403713}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:18403713}. Note=Colocalizes with actin
CC       filaments in sarcomeres. Detected close to the M line.
CC       {ECO:0000269|PubMed:18403713}.
CC   -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR   EMBL; BC128755; AAI28756.1; -; mRNA.
DR   RefSeq; NP_001094434.1; NM_001100964.1.
DR   AlphaFoldDB; A1A5Q0; -.
DR   SMR; A1A5Q0; -.
DR   BioGRID; 255509; 1.
DR   STRING; 10116.ENSRNOP00000067847; -.
DR   iPTMnet; A1A5Q0; -.
DR   PhosphoSitePlus; A1A5Q0; -.
DR   jPOST; A1A5Q0; -.
DR   PaxDb; 10116-ENSRNOP00000064921; -.
DR   PeptideAtlas; A1A5Q0; -.
DR   GeneID; 296935; -.
DR   KEGG; rno:296935; -.
DR   AGR; RGD:1592092; -.
DR   CTD; 442721; -.
DR   RGD; 1592092; Lmod2.
DR   eggNOG; KOG3735; Eukaryota.
DR   InParanoid; A1A5Q0; -.
DR   OrthoDB; 2883785at2759; -.
DR   PhylomeDB; A1A5Q0; -.
DR   PRO; PR:A1A5Q0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0097512; C:cardiac myofibril; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0030016; C:myofibril; ISO:RGD.
DR   GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR   GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR   GO; GO:0005523; F:tropomyosin binding; ISO:RGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR   GO; GO:0045010; P:actin nucleation; ISS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR   GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR004934; TMOD.
DR   PANTHER; PTHR10901:SF12; LEIOMODIN-2; 1.
DR   PANTHER; PTHR10901; TROPOMODULIN; 1.
DR   Pfam; PF03250; Tropomodulin; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..549
FT                   /note="Leiomodin-2"
FT                   /id="PRO_0000311342"
FT   DOMAIN          523..542
FT                   /note="WH2"
FT   REGION          1..164
FT                   /note="Interaction with actin 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT   REGION          1..47
FT                   /note="Interaction with tropomyosin alpha"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT   REGION          1..42
FT                   /note="Tropomyosin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          91..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..499
FT                   /note="Interaction with actin 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT   REGION          179..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..542
FT                   /note="Interaction with actin 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT   COILED          457..515
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        95..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..453
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   549 AA;  61717 MW;  3494F88AEA5C395C CRC64;
     MSTFGYRRGL SKYESIDEDE LLASLTAEEL KELERELEDI EPDRNLPVGL RQKSLTEKTP
     TGNFSREALM AYWEKESQKL LEKERLGECG KLAEEDKEES EEELIFTESN SEVSEEVCTE
     EEEESTEEEE EEEEEDSEEE EVTTEVTKHI NGTVSHNGVN PDNSKPKTFK SQIENINLTN
     GNSGGTQRNT ESPAAIHPCG NPTVIEDALE KIKNNDPDTT EVNLNNIENI TTQTLSRFAE
     ALKENTVVKT FSLANTHADD AAAIAIAEML KVNEHITSVN VESNFITGKG ILAIMRALQH
     NTVLTELRFH NQRHIMGSQV EMEIVKLLKE NTTLLRLGYH FELPGPRMSM TSILTRNMDK
     QRQKRMQEQK QQEGHDGGAT LRTKVWQRGT PGSSPYASPR QSPWSSPKVS KKVHTGRSRP
     PSPVAPPPPP PPPPLPPHML PPPPPPPAPP LPGKKLITRN IAEVIKQQES AQRALQNGQR
     KKKGKKVKKQ PNNILKEIKN SLRSVQEKKM EESSRPSTPQ RSAHENLMEA IRGSSIRQLR
     RVEVPEALR
//