GenomeNet

Database: UniProt
Entry: Q9QYM9
LinkDB: Q9QYM9
Original site: Q9QYM9 
ID   TEFF2_MOUSE             Reviewed;         374 AA.
AC   Q9QYM9; Q3UY20; Q8CDH1; Q9JJE3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-FEB-2019, entry version 140.
DE   RecName: Full=Tomoregulin-2;
DE            Short=TR-2;
DE   AltName: Full=Transmembrane protein with EGF-like and two follistatin-like domains;
DE   Flags: Precursor;
GN   Name=Tmeff2; ORFNames=MNCb-1026;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10903839; DOI=10.1006/geno.2000.6228;
RA   Horie M., Mitsumoto Y., Kyushiki H., Kanemoto N., Watanabe A.,
RA   Taniguchi Y., Nishino N., Okamoto T., Kondo M., Mori T., Noguchi K.,
RA   Nakamura Y., Takahashi E., Tanigami A.;
RT   "Identification and characterization of TMEFF2, a novel survival
RT   factor for hippocampal and mesencephalic neurons.";
RL   Genomics 67:146-152(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10600548; DOI=10.1006/bbrc.1999.1873;
RA   Uchida T., Wada K., Akamatsu T., Yonezawa M., Noguchi H.,
RA   Mizoguchi A., Kasuga M., Sakamoto C.;
RT   "A novel epidermal growth factor-like molecule containing two
RT   follistatin modules stimulates tyrosine phosphorylation of erbB-4 in
RT   MKN28 gastric cancer cells.";
RL   Biochem. Biophys. Res. Commun. 266:593-602(1999).
CC   -!- FUNCTION: May be a survival factor for hippocampal and
CC       mesencephalic neurons. The shedded form may up-regulate cell
CC       proliferation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QYM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYM9-2; Sequence=VSP_014314;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed in the brain. In the
CC       olfactory bulb expressed in mitral cell, granule, and glomerular
CC       layers. In the hippocampus expressed in hippocampal cornu ammonis,
CC       pyramidal layer, dentate gyrus, and substantia nigra pars
CC       compacta. {ECO:0000269|PubMed:10903839}.
CC   -!- DEVELOPMENTAL STAGE: First detected at 11 dpc, reaches a maximum
CC       at 15 dpc, and remains constant through 17 dpc.
CC       {ECO:0000269|PubMed:10600548}.
CC   -!- PTM: N-glycosylated. Contains chondroitin sulfate
CC       glycosaminoglycans (By similarity). {ECO:0000250}.
CC   -!- PTM: A soluble form (TMEFF2-ECD) is produced by proteolytic
CC       shedding. This shedding can be induced by phorbol ester or
CC       proinflammatory cytokines such as TNFalpha, and is mediated by a
CC       metalloproteinase ADAM (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA95049.1; Type=Frameshift; Positions=209; Evidence={ECO:0000305};
DR   EMBL; AB017270; BAA87898.1; -; mRNA.
DR   EMBL; AB041565; BAA95049.1; ALT_FRAME; mRNA.
DR   EMBL; AK029307; BAC26385.1; -; mRNA.
DR   EMBL; AK030053; BAC26760.1; -; mRNA.
DR   EMBL; AK076254; BAC36276.1; -; mRNA.
DR   EMBL; AK135038; BAE22393.1; -; mRNA.
DR   EMBL; BC034850; AAH34850.1; -; mRNA.
DR   CCDS; CCDS14939.1; -. [Q9QYM9-1]
DR   RefSeq; NP_062764.1; NM_019790.4. [Q9QYM9-1]
DR   UniGene; Mm.245154; -.
DR   UniGene; Mm.445120; -.
DR   ProteinModelPortal; Q9QYM9; -.
DR   SMR; Q9QYM9; -.
DR   IntAct; Q9QYM9; 1.
DR   STRING; 10090.ENSMUSP00000080533; -.
DR   MEROPS; I01.969; -.
DR   PhosphoSitePlus; Q9QYM9; -.
DR   PaxDb; Q9QYM9; -.
DR   PeptideAtlas; Q9QYM9; -.
DR   PRIDE; Q9QYM9; -.
DR   Ensembl; ENSMUST00000081851; ENSMUSP00000080533; ENSMUSG00000026109. [Q9QYM9-1]
DR   GeneID; 56363; -.
DR   KEGG; mmu:56363; -.
DR   UCSC; uc007axj.1; mouse. [Q9QYM9-1]
DR   CTD; 23671; -.
DR   MGI; MGI:1861735; Tmeff2.
DR   eggNOG; ENOG410IP0A; Eukaryota.
DR   eggNOG; ENOG4110TEU; LUCA.
DR   GeneTree; ENSGT00940000156056; -.
DR   HOGENOM; HOG000154541; -.
DR   HOVERGEN; HBG053816; -.
DR   InParanoid; Q9QYM9; -.
DR   OMA; NCSGFDD; -.
DR   OrthoDB; 773030at2759; -.
DR   PhylomeDB; Q9QYM9; -.
DR   TreeFam; TF330868; -.
DR   PRO; PR:Q9QYM9; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026109; Expressed in 213 organ(s), highest expression level in dorsal root ganglion.
DR   ExpressionAtlas; Q9QYM9; baseline and differential.
DR   Genevisible; Q9QYM9; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0045720; P:negative regulation of integrin biosynthetic process; ISO:MGI.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISO:MGI.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF07648; Kazal_2; 2.
DR   SMART; SM00280; KAZAL; 2.
DR   SUPFAM; SSF100895; SSF100895; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     40       {ECO:0000250}.
FT   CHAIN        41    374       Tomoregulin-2.
FT                                /FTId=PRO_0000016588.
FT   TOPO_DOM     41    320       Extracellular. {ECO:0000255}.
FT   TRANSMEM    321    341       Helical. {ECO:0000255}.
FT   TOPO_DOM    342    374       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       85    137       Kazal-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      176    229       Kazal-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      261    301       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      303    320       Required for shedding. {ECO:0000250}.
FT   COMPBIAS    231    235       Poly-Thr.
FT   CARBOHYD     55     55       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     91    121       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID     95    114       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    103    135       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    182    213       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    186    206       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    195    227       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    265    278       {ECO:0000250}.
FT   DISULFID    273    289       {ECO:0000250}.
FT   DISULFID    291    300       {ECO:0000250}.
FT   VAR_SEQ     147    262       VHEGSGETSQKETSTCDICQFGAECDEDAEDVWCVCNIDCS
FT                                QTNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRCQ
FT                                DNTTTTTKSEDGHYARTDYAENANKLEESAREHH -> EKF
FT                                SKVMLILKPCTASSLEETNSKEIILCNPSNTHLLKKNENAN
FT                                LTCWSEPFLQAYGLMRTWNSRQREAAKGITETRFLPPPSAY
FT                                CLGIFIGANVKINSEALFRQWTVLKGTIPVP (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014314.
SQ   SEQUENCE   374 AA;  41415 MW;  2C16FEF2C3A69385 CRC64;
     MVLWESPRQC SSWTLCEGFC WLLLLPVTLL IIARPVKLAA FPTSLSDCQT PTGWNCSGYD
     DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNSDYV PVCGSNGESY QNECYLRQAA
     CKQQSEILVV SEGSCATDTG SGSGDGVHEG SGETSQKETS TCDICQFGAE CDEDAEDVWC
     VCNIDCSQTN FNPLCASDGK SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG
     HYARTDYAEN ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC
     EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR IHRQKQNTGH
     YSSDNTTRAS TRLI
//
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