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Q9Z0L0 (TPBG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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:
Trophoblast glycoprotein
Alternative name(s):
5T4 oncofetal trophoblast glycoprotein
Short name=5T4 oncotrophoblast glycoprotein
Gene names
Name:Tpbg
Synonyms:5t4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Highly expressed in embryo and placenta. In adult, expressed only in brain and ovary. Not detected in kidney small intestine, heart, spleen, testis, liver, lung, thymus and stomach. Ref.1

Sequence similarities

Contains 6 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 426395Trophoblast glycoprotein
PRO_0000019593

Regions

Topological domain32 – 361330Extracellular Potential
Transmembrane362 – 38221Helical; Potential
Topological domain383 – 42644Cytoplasmic Potential
Domain53 – 9139LRRNT
Repeat92 – 11322LRR 1
Repeat119 – 14022LRR 2
Repeat143 – 16422LRR 3
Repeat217 – 23822LRR 4
Repeat241 – 26222LRR 5
Repeat265 – 28622LRR 6
Domain300 – 35253LRRCT
Compositional bias32 – 5322Ser-rich

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Ref.4

Experimental info

Sequence conflict471A → D in CAA09931. Ref.1
Sequence conflict1611A → V in CAA09931. Ref.1
Sequence conflict2201R → C in AAH58198. Ref.3
Sequence conflict2881H → Q in CAA09931. Ref.1
Sequence conflict2881H → Q in AAH58198. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9Z0L0 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: A03A76377F68D2A4

FASTA42646,451
        10         20         30         40         50         60 
MPGAGSRGPS AGDGRLRLAR LALVLLGWVS ASAPSSSVPS SSTSPAAFLA SGSAQPPPAE 

        70         80         90        100        110        120 
RCPAACECSE AARTVKCVNR NLLEVPADLP PYVRNLFLTG NQMTVLPAGA FARQPPLADL 

       130        140        150        160        170        180 
EALNLSGNHL KEVCAGAFEH LPGLRRLDLS HNPLTNLSAF AFAGSNASVS APSPLEELIL 

       190        200        210        220        230        240 
NHIVPPEDQR QNGSFEGMVA FEGMVAAALR SGLALRGLTR LELASNHFLF LPRDLLAQLP 

       250        260        270        280        290        300 
SLRYLDLRNN SLVSLTYASF RNLTHLESLH LEDNALKVLH NSTLAEWHGL AHVKVFLDNN 

       310        320        330        340        350        360 
PWVCDCYMAD MVAWLKETEV VPDKARLTCA FPEKMRNRGL LDLNSSDLDC DAVLPQSLQT 

       370        380        390        400        410        420 
SYVFLGIVLA LIGAIFLLVL YLNRKGIKKW MHNIRDACRD HMEGYHYRYE INADPRLTNL 


SSNSDV 

« Hide

References

« Hide 'large scale' references
[1]"Organisation of the mouse and human 5T4 oncofetal leucine-rich glycoprotein gene and expression in foetal and adult murine tissues."
King K.W., Sheppard F.C., Westwater C., Stern P.L., Myers K.A.
Biochim. Biophys. Acta 1445:257-270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/Sv.
[2]"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: Spinal ganglion.
[3]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-281.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ012160 Genomic DNA. Translation: CAA09931.1.
AK051162 mRNA. Translation: BAC34540.1.
AK143519 mRNA. Translation: BAE25413.1.
BC058198 mRNA. Translation: AAH58198.1.
RefSeqNP_001158264.1. NM_001164792.1.
NP_035757.2. NM_011627.4.
UniGeneMm.20864.
Mm.484180.

3D structure databases

ProteinModelPortalQ9Z0L0.
SMRQ9Z0L0. Positions 62-352.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9Z0L0.

Proteomic databases

PaxDbQ9Z0L0.
PRIDEQ9Z0L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006559; ENSMUSP00000006559; ENSMUSG00000035274.
ENSMUST00000098500; ENSMUSP00000096101; ENSMUSG00000035274.
GeneID21983.
KEGGmmu:21983.
UCSCuc009qwz.2. mouse.

Organism-specific databases

CTD7162.
MGIMGI:1341264. Tpbg.

Phylogenomic databases

eggNOGNOG301461.
GeneTreeENSGT00620000088023.
HOGENOMHOG000013090.
HOVERGENHBG053843.
InParanoidQ3UPI2.
OMASFRNLTH.
OrthoDBEOG7QNVM8.
TreeFamTF351115.

Gene expression databases

ArrayExpressQ9Z0L0.
BgeeQ9Z0L0.
CleanExMM_TPBG.
GenevestigatorQ9Z0L0.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301700.
PROQ9Z0L0.
SOURCESearch...

Entry information

Entry nameTPBG_MOUSE
AccessionPrimary (citable) accession number: Q9Z0L0
Secondary accession number(s): Q3UPI2, Q6PE98, Q8BQA4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 3 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