LFTY1_MOUSE
ID LFTY1_MOUSE Reviewed; 368 AA.
AC Q64280; Q3V2A9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Left-right determination factor 1;
DE AltName: Full=Protein lefty-1;
DE Short=Lefty protein;
DE AltName: Full=Stimulated by retinoic acid gene 3 protein;
DE AltName: Full=Transforming growth factor beta-4;
DE Short=TGF-beta-4;
DE Flags: Precursor;
GN Name=Lefty1; Synonyms=Ebaf, Lefty, Stra3, Tgfb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8610011; DOI=10.1038/381151a0;
RA Meno C., Saijoh Y., Fujii H., Ikeda M., Yokoyama T., Yokoyama M.,
RA Toyoda Y., Hamada H.;
RT "Left-right asymmetric expression of the TGF beta-family member lefty in
RT mouse embryos.";
RL Nature 381:151-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bouillet P.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9496783;
RA Oulad-Abdelghani M., Chazaud C., Bouillet P., Mattei M.-G., Dolle P.,
RA Chambon P.;
RT "Stra3/lefty, a retinoic acid-inducible novel member of the transforming
RT growth factor-beta superfamily.";
RL Int. J. Dev. Biol. 42:23-32(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic stem cell;
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 [6]
RP FUNCTION.
RX PubMed=9708731; DOI=10.1016/s0092-8674(00)81472-5;
RA Meno C., Shimono A., Saijoh Y., Yashiro K., Mochida K., Ohishi S., Noji S.,
RA Kondoh H., Hamada H.;
RT "Lefty-1 is required for left-right determination as a regulator of lefty-2
RT and nodal.";
RL Cell 94:287-297(1998).
CC -!- FUNCTION: Required for left-right axis determination as a regulator of
CC LEFTY2 and NODAL. {ECO:0000269|PubMed:9708731}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: By 8.0 dpc, expressed exclusively on the left side
CC of developing embryos with expression predominantly in the prospective
CC floor plate (PFP). Weak expression in the lateral-plate mesoderm (LPM).
CC -!- PTM: The processing of the protein may also occur at the second R-X-X-R
CC site located at AA 132-135. Processing appears to be regulated in a
CC cell-type specific manner.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; D83921; BAA12121.1; -; mRNA.
DR EMBL; Z73151; CAA97497.1; -; mRNA.
DR EMBL; AJ000082; CAA03909.1; -; mRNA.
DR EMBL; AJ000083; CAA03910.1; -; Genomic_DNA.
DR EMBL; AK131943; BAE20889.1; -; mRNA.
DR EMBL; BC050221; AAH50221.1; -; mRNA.
DR CCDS; CCDS15577.1; -.
DR PIR; S67507; S67507.
DR RefSeq; NP_034224.1; NM_010094.4.
DR AlphaFoldDB; Q64280; -.
DR DIP; DIP-46067N; -.
DR IntAct; Q64280; 1.
DR STRING; 10090.ENSMUSP00000041427; -.
DR GlyGen; Q64280; 1 site.
DR PhosphoSitePlus; Q64280; -.
DR PaxDb; Q64280; -.
DR PeptideAtlas; Q64280; -.
DR PRIDE; Q64280; -.
DR DNASU; 13590; -.
DR Ensembl; ENSMUST00000037361; ENSMUSP00000041427; ENSMUSG00000038793.
DR GeneID; 13590; -.
DR KEGG; mmu:13590; -.
DR UCSC; uc007dww.1; mouse.
DR CTD; 10637; -.
DR MGI; MGI:107405; Lefty1.
DR VEuPathDB; HostDB:ENSMUSG00000038793; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000010056; -.
DR HOGENOM; CLU_064098_0_0_1; -.
DR InParanoid; Q64280; -.
DR OMA; VSVYWVQ; -.
DR OrthoDB; 751948at2759; -.
DR PhylomeDB; Q64280; -.
DR TreeFam; TF106462; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 13590; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q64280; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q64280; protein.
DR Bgee; ENSMUSG00000038793; Expressed in neural plate and 78 other tissues.
DR Genevisible; Q64280; MM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0038100; F:nodal binding; IPI:UniProtKB.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; IGI:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IDA:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:1900124; P:negative regulation of nodal receptor complex assembly; IDA:UniProtKB.
DR GO; GO:1900108; P:negative regulation of nodal signaling pathway; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR003942; LRDF.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PIRSF; PIRSF037402; TGFb4; 1.
DR PRINTS; PR01427; TGFBETA4.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Developmental protein; Disulfide bond; Glycoprotein;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..76
FT /note="Or 135"
FT /evidence="ECO:0000255"
FT /id="PRO_0000033808"
FT CHAIN 77..368
FT /note="Left-right determination factor 1"
FT /id="PRO_0000033809"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..266
FT /evidence="ECO:0000250"
FT DISULFID 265..318
FT /evidence="ECO:0000250"
FT DISULFID 295..353
FT /evidence="ECO:0000250"
FT DISULFID 299..355
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 41498 MW; 821DAE663C546B5F CRC64;
MPFLWLCWAL WALSLVSLRE ALTGEQILGS LLQQLQLDQP PVLDKADVEG MVIPSHVRTQ
YVALLQHSHA SRSRGKRFSQ NLREVAGRFL VSETSTHLLV FGMEQRLPPN SELVQAVLRL
FQEPVPRTAL RRQKRLSPHS ARARVTIEWL RFRDDGSNRT ALIDSRLVSI HESGWKAFDV
TEAVNFWQQL SRPRQPLLLQ VSVQREHLGP GTWSSHKLVR FAAQGTPDGK GQGEPQLELH
TLDLKDYGAQ GNCDPEAPVT EGTRCCRQEM YLDLQGMKWA ENWILEPPGF LTYECVGSCL
QLPESLTSRW PFLGPRQCVA SEMTSLPMIV SVKEGGRTRP QVVSLPNMRV QTCSCASDGA
LIPRRLQP
