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Q9QYM9 (TEFF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tomoregulin-2

Short name=TR-2
Alternative name(s):
Transmembrane protein with EGF-like and two follistatin-like domains
Gene names
Name:Tmeff2
ORF Names:MNCb-1026
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be a survival factor for hippocampal and mesencephalic neurons. The shedded form may up-regulate cell proliferation By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Widely expressed in the brain. In the olfactory bulb expressed in mitral cell, granule, and glomerular layers. In the hippocampus expressed in hippocampal cornu ammonis, pyramidal layer, dentate gyrus, and substantia nigra pars compacta. Ref.1

Developmental stage

First detected at E11, reaches a maximum at E15, and remains constant through E17. Ref.5

Post-translational modification

N-glycosylated. Contains chondroitin sulfate glycosaminoglycans By similarity.

A soluble form (TMEFF2-ECD) is produced by proteolytic shedding. This shedding can be induced by phorbol ester or proinflammatory cytokines such as TNFalpha, and is mediated by a metalloproteinase ADAM By similarity.

Sequence similarities

Belongs to the tomoregulin family.

Contains 1 EGF-like domain.

Contains 2 Kazal-like domains.

Sequence caution

The sequence BAA95049.1 differs from that shown. Reason: Frameshift at position 209.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9QYM9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9QYM9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     147-262: VHEGSGETSQ...KLEESAREHH → EKFSKVMLIL...TVLKGTIPVP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 By similarity
Chain41 – 374334Tomoregulin-2
PRO_0000016588

Regions

Topological domain41 – 320280Extracellular Potential
Transmembrane321 – 34121Helical; Potential
Topological domain342 – 37433Cytoplasmic Potential
Domain85 – 13753Kazal-like 1
Domain176 – 22954Kazal-like 2
Domain261 – 30141EGF-like
Region303 – 32018Required for shedding By similarity
Compositional bias231 – 2355Poly-Thr

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Disulfide bond265 ↔ 278 By similarity
Disulfide bond273 ↔ 289 By similarity
Disulfide bond291 ↔ 300 By similarity

Natural variations

Alternative sequence147 – 262116VHEGS…AREHH → EKFSKVMLILKPCTASSLEE TNSKEIILCNPSNTHLLKKN ENANLTCWSEPFLQAYGLMR TWNSRQREAAKGITETRFLP PPSAYCLGIFIGANVKINSE ALFRQWTVLKGTIPVP in isoform 2.
VSP_014314

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2C16FEF2C3A69385

FASTA37441,415
        10         20         30         40         50         60 
MVLWESPRQC SSWTLCEGFC WLLLLPVTLL IIARPVKLAA FPTSLSDCQT PTGWNCSGYD 

        70         80         90        100        110        120 
DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNSDYV PVCGSNGESY QNECYLRQAA 

       130        140        150        160        170        180 
CKQQSEILVV SEGSCATDTG SGSGDGVHEG SGETSQKETS TCDICQFGAE CDEDAEDVWC 

       190        200        210        220        230        240 
VCNIDCSQTN FNPLCASDGK SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG 

       250        260        270        280        290        300 
HYARTDYAEN ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC 

       310        320        330        340        350        360 
EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR IHRQKQNTGH 

       370 
YSSDNTTRAS TRLI 

« Hide

Isoform 2 [UniParc].

Checksum: F5F7B4619E1CCFCC
Show »

FASTA37441,603

References

« Hide 'large scale' references
[1]"Identification and characterization of TMEFF2, a novel survival factor for hippocampal and mesencephalic neurons."
Horie M., Mitsumoto Y., Kyushiki H., Kanemoto N., Watanabe A., Taniguchi Y., Nishino N., Okamoto T., Kondo M., Mori T., Noguchi K., Nakamura Y., Takahashi E., Tanigami A.
Genomics 67:146-152(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[3]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Head, Olfactory bulb and Skin.
[4]"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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Mammary gland.
[5]"A novel epidermal growth factor-like molecule containing two follistatin modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric cancer cells."
Uchida T., Wada K., Akamatsu T., Yonezawa M., Noguchi H., Mizoguchi A., Kasuga M., Sakamoto C.
Biochem. Biophys. Res. Commun. 266:593-602(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017270 mRNA. Translation: BAA87898.1.
AB041565 mRNA. Translation: BAA95049.1. Frameshift.
AK029307 mRNA. Translation: BAC26385.1.
AK030053 mRNA. Translation: BAC26760.1.
AK076254 mRNA. Translation: BAC36276.1.
AK135038 mRNA. Translation: BAE22393.1.
BC034850 mRNA. Translation: AAH34850.1.
IPIIPI00407251.
IPI00468627.
RefSeqNP_062764.1. NM_019790.4.
UniGeneMm.245154.
Mm.445120.

3D structure databases

ProteinModelPortalQ9QYM9.
SMRQ9QYM9. Positions 89-228, 272-304.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QYM9. 1 interaction.

Protein family/group databases

MEROPSI01.969.

PTM databases

PhosphoSiteQ9QYM9.

Proteomic databases

PaxDbQ9QYM9.
PRIDEQ9QYM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081851; ENSMUSP00000080533; ENSMUSG00000026109.
ENSMUST00000114565; ENSMUSP00000110212; ENSMUSG00000026109.
GeneID56363.
KEGGmmu:56363.
UCSCuc007axj.1. mouse.

Organism-specific databases

CTD23671.
MGIMGI:1861735. Tmeff2.

Phylogenomic databases

eggNOGNOG245393.
GeneTreeENSGT00530000062996.
HOGENOMHOG000154541.
HOVERGENHBG053816.
InParanoidQ9QYM9.
OMACPRTNRI.
OrthoDBEOG43BMNZ.

Gene expression databases

BgeeQ9QYM9.
GenevestigatorQ9QYM9.
GermOnlineENSMUSG00000026109. Mus musculus.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002350. Kazal_dom.
[Graphical view]
PfamPF12661. hEGF. 1 hit.
PF07648. Kazal_2. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 1 hit.
SM00280. KAZAL. 2 hits.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS51465. KAZAL_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio312394.
SOURCESearch...

Entry information

Entry nameTEFF2_MOUSE
AccessionPrimary (citable) accession number: Q9QYM9
Secondary accession number(s): Q3UY20, Q8CDH1, Q9JJE3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families