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Q9EP52 (TWSG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twisted gastrulation protein homolog 1
Gene names
Name:Twsg1
Synonyms:Tsg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development. Ref.6 Ref.8 Ref.9 Ref.10

Subunit structure

Interacts with CHRD and/or BMP4. This interaction enhances CHRD/BMP4 complex formation. Interacts with BMP7. Ref.1 Ref.6 Ref.9

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed in lymph node, liver, kidney, and lung. Expression in the kidney was stronger in the medulla than in the cortex, particularly in the cells surrounding the medullary tubules. Expressed in growth plate cartilage of long bones, ribs, and digits and to a lesser extent also in the resting zone of the epiphysis, trabecular bone, and vertebral cartilage. Expression seems to be absent from other skeletal tissues including muscle, skin, and fibroblasts. Ref.10

Developmental stage

Expressed at all embryonic stages examined. Expression was low and distribution was diffuse. At the primitive streak stage, detected in the extraembryonic region. Signal first appeared in the embryo during the neural plate stage. Stronger and more localized expression is seen after embryonic turning. Higher expression is seen in the branchial arch mesenchyme, the endoderm of the developing pharynx, all levels of the developing gut, the myotome compartment of the somites, and some regions of surface ectoderm. At 8.25 and 9.0 dpc expressed in head mesenchyme and ventral mesoderm. Ref.6 Ref.9

Domain

The N-terminal domain is sufficient to interact with BMP4 By similarity.

Disruption phenotype

Embryonic lethality and sirenomelia were observed only in BMP null embryos in which one or two copies of TSG were also missing. When TSG and BMP7 are mutated, the siren phenotype results from the fusion of the limb buds in the ventroposterior midline owing to a paucity of posterior ventral mesoderm. Ref.9

Sequence similarities

Belongs to the twisted gastrulation protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 222198Twisted gastrulation protein homolog 1
PRO_0000278809

Regions

Compositional bias18 – 7659Cys-rich

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict61I → IA in AAG10080. Ref.3
Sequence conflict751M → R in AAG10080. Ref.3
Sequence conflict751M → R in AAH04850. Ref.5
Sequence conflict1681V → E in BAC28326. Ref.4
Sequence conflict203 – 2042IG → MR in AAG10080. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9EP52 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F9B0CEE2A8DF8CA7

FASTA22224,801
        10         20         30         40         50         60 
MKSHYIVLAL ASLTFLLCLP VSQSCNKALC ASDVSKCLIQ ELCQCRPGEG NCPCCKECML 

        70         80         90        100        110        120 
CLGALWDECC DCVGMCNPRN YSDTPPTSKS TVEELHEPIP SLFRALTEGD TQLNWNIVSF 

       130        140        150        160        170        180 
PVAEELSHHE NLVSFLETVN QLHHQNVSVP SNNVHAPFPS DKERMCTVVY FDDCMSIHQC 

       190        200        210        220 
KISCESMGAS KYRWFHNACC ECIGPECIDY GSKTVKCMNC MF 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary conservation, developmental expression, and genomic mapping of mammalian Twisted gastrulation."
Graf D., Timmons P.M., Hitchins M., Episkopou V., Moore G., Ito T., Fujiyama A., Fisher A.G., Merkenschlager M.
Mamm. Genome 12:554-560(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CHRD AND BMP4.
Tissue: Thymus.
[2]"Characterization of the mouse homolog of Twisted gastrulation."
Zakin L., Oelgeschlager M., Geissert D., De Robertis E.M.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Mouse twisted gastrulation protein: a new signal pathway of spermatogenesis."
Li J.M., Sha J.H., Zhou Z.M.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Colon, Liver and Spinal cord.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[6]"Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling."
Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y., Greenspan D.S.
Nature 410:475-478(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH CHRD AND BMP4.
[7]Erratum
Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y., Greenspan D.S.
Nature 411:720-720(2001)
[8]"The developmentally regulated expression of Twisted gastrulation reveals a role for bone morphogenetic proteins in the control of T cell development."
Graf D., Nethisinghe S., Palmer D.B., Fisher A.G., Merkenschlager M.
J. Exp. Med. 196:163-171(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Sirenomelia in Bmp7 and Tsg compound mutant mice: requirement for Bmp signaling in the development of ventral posterior mesoderm."
Zakin L., Reversade B., Kuroda H., Lyons K.M., De Robertis E.M.
Development 132:2489-2499(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, INTERACTION WITH BMP7.
[10]"Twisted gastrulation modulates bone morphogenetic protein-induced collagen II and X expression in chondrocytes in vitro and in vivo."
Schmidl M., Adam N., Surmann-Schmitt C., Hattori T., Stock M., Dietz U., de Crombrugghe B., Poeschl E., von der Mark K.
J. Biol. Chem. 281:31790-31800(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ297390 mRNA. Translation: CAC05586.1.
AF292033 mRNA. Translation: AAG00605.1.
AF295097 mRNA. Translation: AAG10080.1.
AK018524 mRNA. Translation: BAC25557.1.
AK033504 mRNA. Translation: BAC28326.1.
AK049646 mRNA. Translation: BAC33857.1.
AK168547 mRNA. Translation: BAE40422.1.
AK168633 mRNA. Translation: BAE40493.1.
BC004850 mRNA. Translation: AAH04850.1.
RefSeqNP_075540.1. NM_023053.3.
UniGeneMm.10153.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211157. 1 interaction.

Proteomic databases

PaxDbQ9EP52.
PRIDEQ9EP52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024906; ENSMUSP00000024906; ENSMUSG00000024098.
GeneID65960.
KEGGmmu:65960.
UCSCuc008dgq.2. mouse.

Organism-specific databases

CTD57045.
MGIMGI:2137520. Twsg1.

Phylogenomic databases

eggNOGNOG70213.
GeneTreeENSGT00390000007058.
HOGENOMHOG000044674.
HOVERGENHBG055753.
InParanoidQ9EP52.
OMANCTVAFM.
OrthoDBEOG7J70GN.
PhylomeDBQ9EP52.
TreeFamTF323922.

Gene expression databases

BgeeQ9EP52.
CleanExMM_TWSG1.
GenevestigatorQ9EP52.

Family and domain databases

InterProIPR006761. Tsg.
[Graphical view]
PANTHERPTHR12312. PTHR12312. 1 hit.
PfamPF04668. Tsg. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320380.
PROQ9EP52.
SOURCESearch...

Entry information

Entry nameTWSG1_MOUSE
AccessionPrimary (citable) accession number: Q9EP52
Secondary accession number(s): Q8CCB1 expand/collapse secondary AC list , Q8CEM6, Q99K77, Q9ERN7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot