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Protein

Tomoregulin-2

Gene

Tmeff2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Biological processi

Complete GO annotation...

Protein family/group databases

MEROPSiI01.969.

Names & Taxonomyi

Protein namesi
Recommended name:
Tomoregulin-2
Short name:
TR-2
Alternative name(s):
Transmembrane protein with EGF-like and two follistatin-like domains
Gene namesi
Name:Tmeff2
ORF Names:MNCb-1026
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1861735. Tmeff2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 320280ExtracellularSequence analysisAdd
BLAST
Transmembranei321 – 34121HelicalSequence analysisAdd
BLAST
Topological domaini342 – 37433CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040By similarityAdd
BLAST
Chaini41 – 374334Tomoregulin-2PRO_0000016588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi265 ↔ 278By similarity
Disulfide bondi273 ↔ 289By similarity
Disulfide bondi291 ↔ 300By similarity

Post-translational modificationi

N-glycosylated. Contains chondroitin sulfate glycosaminoglycans (By similarity).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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9QYM9.
PaxDbiQ9QYM9.
PRIDEiQ9QYM9.

PTM databases

PhosphoSiteiQ9QYM9.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

First detected at E11, reaches a maximum at E15, and remains constant through E17.1 Publication

Gene expression databases

BgeeiQ9QYM9.
GenevisibleiQ9QYM9. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9QYM9. 1 interaction.
STRINGi10090.ENSMUSP00000080533.

Structurei

3D structure databases

ProteinModelPortaliQ9QYM9.
SMRiQ9QYM9. Positions 86-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 13753Kazal-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini176 – 22954Kazal-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 30141EGF-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni303 – 32018Required for sheddingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 2355Poly-Thr

Sequence similaritiesi

Belongs to the tomoregulin family.Curated
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 2 Kazal-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IP0A. Eukaryota.
ENOG4110TEU. LUCA.
GeneTreeiENSGT00730000110884.
HOGENOMiHOG000154541.
HOVERGENiHBG053816.
InParanoidiQ9QYM9.
OMAiENTMRAS.
OrthoDBiEOG7JT6WK.
PhylomeDBiQ9QYM9.
TreeFamiTF330868.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002350. Kazal_dom.
[Graphical view]
PfamiPF12661. hEGF. 1 hit.
PF07648. Kazal_2. 2 hits.
[Graphical view]
SMARTiSM00280. KAZAL. 2 hits.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS51465. KAZAL_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QYM9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVLWESPRQC SSWTLCEGFC WLLLLPVTLL IIARPVKLAA FPTSLSDCQT
60 70 80 90 100
PTGWNCSGYD DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNSDYV
110 120 130 140 150
PVCGSNGESY QNECYLRQAA CKQQSEILVV SEGSCATDTG SGSGDGVHEG
160 170 180 190 200
SGETSQKETS TCDICQFGAE CDEDAEDVWC VCNIDCSQTN FNPLCASDGK
210 220 230 240 250
SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG HYARTDYAEN
260 270 280 290 300
ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC
310 320 330 340 350
EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR
360 370
IHRQKQNTGH YSSDNTTRAS TRLI
Length:374
Mass (Da):41,415
Last modified:May 1, 2000 - v1
Checksum:i2C16FEF2C3A69385
GO
Isoform 2 (identifier: Q9QYM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-262: VHEGSGETSQ...KLEESAREHH → EKFSKVMLIL...TVLKGTIPVP

Note: No experimental confirmation available.
Show »
Length:374
Mass (Da):41,603
Checksum:iF5F7B4619E1CCFCC
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei147 – 262116VHEGS…AREHH → EKFSKVMLILKPCTASSLEE TNSKEIILCNPSNTHLLKKN ENANLTCWSEPFLQAYGLMR TWNSRQREAAKGITETRFLP PPSAYCLGIFIGANVKINSE ALFRQWTVLKGTIPVP in isoform 2. 1 PublicationVSP_014314Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14939.1. [Q9QYM9-1]
RefSeqiNP_062764.1. NM_019790.4. [Q9QYM9-1]
XP_011236864.1. XM_011238562.1. [Q9QYM9-1]
UniGeneiMm.245154.
Mm.445120.

Genome annotation databases

EnsembliENSMUST00000081851; ENSMUSP00000080533; ENSMUSG00000026109. [Q9QYM9-1]
GeneIDi56363.
KEGGimmu:56363.
UCSCiuc007axj.1. mouse. [Q9QYM9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14939.1. [Q9QYM9-1]
RefSeqiNP_062764.1. NM_019790.4. [Q9QYM9-1]
XP_011236864.1. XM_011238562.1. [Q9QYM9-1]
UniGeneiMm.245154.
Mm.445120.

3D structure databases

ProteinModelPortaliQ9QYM9.
SMRiQ9QYM9. Positions 86-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QYM9. 1 interaction.
STRINGi10090.ENSMUSP00000080533.

Protein family/group databases

MEROPSiI01.969.

PTM databases

PhosphoSiteiQ9QYM9.

Proteomic databases

MaxQBiQ9QYM9.
PaxDbiQ9QYM9.
PRIDEiQ9QYM9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081851; ENSMUSP00000080533; ENSMUSG00000026109. [Q9QYM9-1]
GeneIDi56363.
KEGGimmu:56363.
UCSCiuc007axj.1. mouse. [Q9QYM9-1]

Organism-specific databases

CTDi23671.
MGIiMGI:1861735. Tmeff2.

Phylogenomic databases

eggNOGiENOG410IP0A. Eukaryota.
ENOG4110TEU. LUCA.
GeneTreeiENSGT00730000110884.
HOGENOMiHOG000154541.
HOVERGENiHBG053816.
InParanoidiQ9QYM9.
OMAiENTMRAS.
OrthoDBiEOG7JT6WK.
PhylomeDBiQ9QYM9.
TreeFamiTF330868.

Miscellaneous databases

PROiQ9QYM9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYM9.
GenevisibleiQ9QYM9. MM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002350. Kazal_dom.
[Graphical view]
PfamiPF12661. hEGF. 1 hit.
PF07648. Kazal_2. 2 hits.
[Graphical view]
SMARTiSM00280. KAZAL. 2 hits.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS51465. KAZAL_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/6J.
    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.
    , 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.

Entry informationi

Entry nameiTEFF2_MOUSE
AccessioniPrimary (citable) accession number: Q9QYM9
Secondary accession number(s): Q3UY20, Q8CDH1, Q9JJE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.