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Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)

 LFTY2_HUMAN             Reviewed;         366 AA.
O00292; B3KNH4; B4E332; E9PDM4; O75611; Q5TE89; Q8NBQ9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
20-DEC-2017, entry version 176.
RecName: Full=Left-right determination factor 2;
AltName: Full=Endometrial bleeding-associated factor;
AltName: Full=Left-right determination factor A;
AltName: Full=Protein lefty-2;
AltName: Full=Protein lefty-A;
AltName: Full=Transforming growth factor beta-4;
Short=TGF-beta-4;
Flags: Precursor;
Name=LEFTY2; Synonyms=EBAF, LEFTA, LEFTYA, TGFB4; ORFNames=PSEC0024;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9153275; DOI=10.1172/JCI119415;
Kothapalli R., Buyuksal I., Wu S.-Q., Chegini N., Tabibzadeh S.;
"Detection of ebaf, a novel human gene of the transforming growth
factor beta superfamily association of gene expression with
endometrial bleeding.";
J. Clin. Invest. 99:2342-2350(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LRAM ASN-342.
TISSUE=Placenta;
PubMed=10053005; DOI=10.1086/302289;
Kosaki K., Bassi M.T., Kosaki R., Lewin M., Belmont J., Schauer G.,
Casey B.;
"Characterization and mutation analysis of human LEFTY A and LEFTY B,
homologues of murine genes implicated in left-right axis
development.";
Am. J. Hum. Genet. 64:712-721(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Required for left-right (L-R) asymmetry determination of
organ systems in mammals. May play a role in endometrial bleeding.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00292-1; Sequence=Displayed;
Name=2;
IsoId=O00292-2; Sequence=VSP_045264;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mesenchymal cells of the endometrial stroma.
-!- DEVELOPMENTAL STAGE: Transiently expressed before and during
menstrual bleeding.
-!- PTM: The processing of the protein may also occur at the second R-
X-X-R site located at AA 132-135. Processing appears to be
regulated in a cell-type specific manner.
-!- DISEASE: Left-right axis malformations (LRAM) [MIM:601877]: The
defect includes left pulmonary isomerism, with cardiac anomalies
characterized by complete atrioventricular canal defect and
hypoplastic left ventricle, and interrupted inferior vena cava.
{ECO:0000269|PubMed:10053005}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB53269.1; Type=Miscellaneous discrepancy; Note=Authors have revised their sequence, but have not submitted the revised DNA sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U81523; AAB53269.1; ALT_SEQ; mRNA.
EMBL; AF081511; AAC32600.1; -; Genomic_DNA.
EMBL; AF081508; AAC32600.1; JOINED; Genomic_DNA.
EMBL; AF081509; AAC32600.1; JOINED; Genomic_DNA.
EMBL; AF081510; AAC32600.1; JOINED; Genomic_DNA.
EMBL; AF081513; AAD48145.1; -; mRNA.
EMBL; AK027520; BAG51336.1; -; mRNA.
EMBL; AK075344; BAC11556.1; -; mRNA.
EMBL; AK304549; BAG65344.1; -; mRNA.
EMBL; AL117348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035718; AAH35718.1; -; mRNA.
CCDS; CCDS1549.1; -. [O00292-1]
CCDS; CCDS53479.1; -. [O00292-2]
RefSeq; NP_001165896.1; NM_001172425.2. [O00292-2]
RefSeq; NP_003231.2; NM_003240.4. [O00292-1]
UniGene; Hs.520187; -.
ProteinModelPortal; O00292; -.
SMR; O00292; -.
BioGrid; 112902; 3.
IntAct; O00292; 2.
STRING; 9606.ENSP00000355785; -.
iPTMnet; O00292; -.
PhosphoSitePlus; O00292; -.
BioMuta; LEFTY2; -.
EPD; O00292; -.
PaxDb; O00292; -.
PeptideAtlas; O00292; -.
PRIDE; O00292; -.
Ensembl; ENST00000366820; ENSP00000355785; ENSG00000143768. [O00292-1]
Ensembl; ENST00000420304; ENSP00000388009; ENSG00000143768. [O00292-2]
GeneID; 7044; -.
KEGG; hsa:7044; -.
UCSC; uc001hpt.3; human. [O00292-1]
CTD; 7044; -.
DisGeNET; 7044; -.
EuPathDB; HostDB:ENSG00000143768.11; -.
GeneCards; LEFTY2; -.
HGNC; HGNC:3122; LEFTY2.
HPA; CAB025801; -.
HPA; HPA047883; -.
HPA; HPA056210; -.
MalaCards; LEFTY2; -.
MIM; 601877; gene+phenotype.
neXtProt; NX_O00292; -.
OpenTargets; ENSG00000143768; -.
Orphanet; 157769; Situs ambiguus.
PharmGKB; PA27580; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00390000010056; -.
HOGENOM; HOG000113317; -.
HOVERGEN; HBG074429; -.
InParanoid; O00292; -.
KO; K04668; -.
OMA; ETGWKSF; -.
PhylomeDB; O00292; -.
TreeFam; TF106462; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
SIGNOR; O00292; -.
ChiTaRS; LEFTY2; human.
GenomeRNAi; 7044; -.
PRO; PR:O00292; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143768; -.
CleanEx; HS_LEFTY2; -.
ExpressionAtlas; O00292; baseline and differential.
Genevisible; O00292; HS.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016049; P:cell growth; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR003942; LRDF.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF037402; TGFb4; 1.
PRINTS; PR01427; TGFBETA4.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytokine;
Developmental protein; Disease mutation; Disulfide bond; Glycoprotein;
Growth factor; Heterotaxy; Polymorphism; Reference proteome; Secreted;
Signal.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 76 Or 135. {ECO:0000255}.
/FTId=PRO_0000033806.
CHAIN 77 366 Left-right determination factor 2.
/FTId=PRO_0000033807.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 251 264 {ECO:0000250}.
DISULFID 263 316 {ECO:0000250}.
DISULFID 293 351 {ECO:0000250}.
DISULFID 297 353 {ECO:0000250}.
VAR_SEQ 94 127 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045264.
VARIANT 92 92 S -> L (in dbSNP:rs366439).
/FTId=VAR_021980.
VARIANT 286 286 P -> L (in dbSNP:rs2295418).
/FTId=VAR_021981.
VARIANT 342 342 S -> N (in LRAM; dbSNP:rs121909126).
{ECO:0000269|PubMed:10053005}.
/FTId=VAR_010385.
CONFLICT 132 132 R -> G (in Ref. 3; BAG65344).
{ECO:0000305}.
CONFLICT 183 183 A -> P (in Ref. 4; BAC11556).
{ECO:0000305}.
SEQUENCE 366 AA; 40920 MW; 63A416CAE30F7A39 CRC64;
MWPLWLCWAL WVLPLAGPGA ALTEEQLLGS LLRQLQLSEV PVLDRADMEK LVIPAHVRAQ
YVVLLRRSHG DRSRGKRFSQ SFREVAGRFL ASEASTHLLV FGMEQRLPPN SELVQAVLRL
FQEPVPKAAL HRHGRLSPRS AQARVTVEWL RVRDDGSNRT SLIDSRLVSV HESGWKAFDV
TEAVNFWQQL SRPRQPLLLQ VSVQREHLGP LASGAHKLVR FASQGAPAGL GEPQLELHTL
DLRDYGAQGD CDPEAPMTEG TRCCRQEMYI DLQGMKWAKN WVLEPPGFLA YECVGTCQQP
PEALAFNWPF LGPRQCIASE TASLPMIVSI KEGGRTRPQV VSLPNMRVQK CSCASDGALV
PRRLQP


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