LMOD2_CHICK
ID LMOD2_CHICK Reviewed; 552 AA.
AC E1BTG2;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Leiomodin-2 {ECO:0000303|PubMed:20736303};
DE AltName: Full=Cardiac leiomodin;
DE Short=C-LMOD;
GN Name=LMOD2 {ECO:0000312|Ensembl:ENSGALP00000014297};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND ACTIN-BINDING.
RX PubMed=20736303; DOI=10.1242/jcs.071837;
RA Tsukada T., Pappas C.T., Moroz N., Antin P.B., Kostyukova A.S.,
RA Gregorio C.C.;
RT "Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the
RT thin filaments in cardiac muscle.";
RL J. Cell Sci. 123:3136-3145(2010).
CC -!- FUNCTION: Mediates nucleation of actin filaments and thereby promotes
CC actin polymerization (By similarity). Plays a role in the regulation of
CC actin filament length (PubMed:20736303). Required for normal sarcomere
CC organization in the heart, and for normal heart function (By
CC similarity). {ECO:0000250|UniProtKB:Q3UHZ5,
CC ECO:0000250|UniProtKB:Q6P5Q4, ECO:0000269|PubMed:20736303}.
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:20736303}. Cytoplasm, myofibril
CC {ECO:0000269|PubMed:20736303}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:20736303}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20736303}. Note=Colocalizes with actin filament
CC pointed ends in sarcomeres. Detected close to the M line.
CC {ECO:0000269|PubMed:20736303}.
CC -!- DEVELOPMENTAL STAGE: First detected in myocardium at HH stage 14.
CC Detected in myocardium and somites at HH stage 17 and 19.
CC {ECO:0000269|PubMed:20736303}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; AADN03000706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001186644.2; NM_001199715.2.
DR AlphaFoldDB; E1BTG2; -.
DR SMR; E1BTG2; -.
DR STRING; 9031.ENSGALP00000014297; -.
DR PaxDb; E1BTG2; -.
DR Ensembl; ENSGALT00000014313; ENSGALP00000014297; ENSGALG00000008805.
DR GeneID; 417751; -.
DR KEGG; gga:417751; -.
DR CTD; 442721; -.
DR VEuPathDB; HostDB:geneid_417751; -.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000156567; -.
DR HOGENOM; CLU_031052_4_0_1; -.
DR InParanoid; E1BTG2; -.
DR OMA; EECFTES; -.
DR OrthoDB; 1025132at2759; -.
DR TreeFam; TF315841; -.
DR PRO; PR:E1BTG2; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000008805; Expressed in heart and 2 other tissues.
DR GO; GO:0005884; C:actin filament; 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; IBA:GO_Central.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IMP: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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR030132; LMOD2.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF12; PTHR10901:SF12; 1.
DR Pfam; PF03250; Tropomodulin; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..552
FT /note="Leiomodin-2"
FT /id="PRO_0000437123"
FT DOMAIN 526..545
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..169
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 33..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..498
FT /note="Interaction with actin 2"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT REGION 364..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Interaction with actin 3"
FT /evidence="ECO:0000250|UniProtKB:Q6P5Q4"
FT COILED 13..46
FT /evidence="ECO:0000255"
FT COILED 86..151
FT /evidence="ECO:0000255"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 62373 MW; F23C7DE013A83CD6 CRC64;
MSTFGYRREL SKYEDIDEDE LLASLTEEEL KELERELEDI EPDRNLPVGQ RQKSLTEKTP
TGTFSREALM AYWERETRKL LEKERLGACE KDSEQEEDNS EDIQEECFTE SNSEVSEEAY
TEEDDEEEEE EEEEEEDEDD SDDEDEEKQN SAASERPVNC EDGRSSSHVR HKKCSNAKNS
ENLFNGHDGK DTENLSFKSS AIHPCGNPTV IEDALEKVRS NDPETTEVNL NNIENITSQM
LIQFSQALRD NTVVKSFSLA NTHADDNVAI AIAGMLKVNQ HITSLNIESN FITGKGVLAI
MRALQHNKVL TELRFHNQRH IMGSQVEMDI VKLLKENTTL VKLGYHFDLA GPRMSMTSIL
TRNMDKQRQK RMQEQRQQEY GCDGAINPKT KVLQKGTPRS SPYTSPKSSP WSSPKLPRKS
APAKSQPPAP APPPPPPPPP PPPPPPPPVI PDKKAPTRNI AEVIKQQESS RKALQNGQKK
KKGKKGKKHE NSILKEIKDS LKSVSDRKSE EGSRPSTRPS TPQRSLHDNL MEAIRASSIK
QLRRVEVPEA LR
