TEFF2_MOUSE
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 03-AUG-2022, entry version 156.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 factor for
RT 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., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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., Mizoguchi A.,
RA Kasuga M., Sakamoto C.;
RT "A novel epidermal growth factor-like molecule containing two follistatin
RT modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric
RT cancer cells.";
RL Biochem. Biophys. Res. Commun. 266:593-602(1999).
CC -!- FUNCTION: May be a survival factor for hippocampal and mesencephalic
CC neurons. The shedded form may up-regulate cell proliferation (By
CC 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 -!- TISSUE SPECIFICITY: Widely expressed in the brain. In the olfactory
CC bulb expressed in mitral cell, granule, and glomerular layers. In the
CC hippocampus expressed in hippocampal cornu ammonis, pyramidal layer,
CC dentate gyrus, and substantia nigra pars compacta.
CC {ECO:0000269|PubMed:10903839}.
CC -!- DEVELOPMENTAL STAGE: First detected at 11 dpc, reaches a maximum at 15
CC dpc, and remains constant through 17 dpc.
CC {ECO:0000269|PubMed:10600548}.
CC -!- PTM: N-glycosylated. Contains chondroitin sulfate glycosaminoglycans
CC (By similarity). {ECO:0000250}.
CC -!- PTM: A soluble form (TMEFF2-ECD) is produced by proteolytic shedding.
CC This shedding can be induced by phorbol ester or pro-inflammatory
CC cytokines such as TNFalpha, and is mediated by a metalloproteinase ADAM
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95049.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q9QYM9; -.
DR SMR; Q9QYM9; -.
DR IntAct; Q9QYM9; 1.
DR STRING; 10090.ENSMUSP00000080533; -.
DR MEROPS; I01.969; -.
DR MEROPS; I01.978; -.
DR GlyGen; Q9QYM9; 2 sites.
DR PhosphoSitePlus; Q9QYM9; -.
DR MaxQB; Q9QYM9; -.
DR PaxDb; Q9QYM9; -.
DR PeptideAtlas; Q9QYM9; -.
DR PRIDE; Q9QYM9; -.
DR ProteomicsDB; 263159; -. [Q9QYM9-1]
DR ProteomicsDB; 263160; -. [Q9QYM9-2]
DR Antibodypedia; 2895; 369 antibodies from 31 providers.
DR DNASU; 56363; -.
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 VEuPathDB; HostDB:ENSMUSG00000026109; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000156056; -.
DR HOGENOM; CLU_048579_1_0_1; -.
DR InParanoid; Q9QYM9; -.
DR OMA; XCDAGYT; -.
DR OrthoDB; 773030at2759; -.
DR PhylomeDB; Q9QYM9; -.
DR TreeFam; TF330868; -.
DR BioGRID-ORCS; 56363; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9QYM9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QYM9; protein.
DR Bgee; ENSMUSG00000026109; Expressed in ventral horn of spinal cord and 195 other tissues.
DR ExpressionAtlas; Q9QYM9; baseline and differential.
DR Genevisible; Q9QYM9; MM.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
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:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO:MGI.
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; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000250"
FT CHAIN 41..374
FT /note="Tomoregulin-2"
FT /id="PRO_0000016588"
FT TOPO_DOM 41..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..137
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 176..229
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 261..301
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 303..320
FT /note="Required for shedding"
FT /evidence="ECO:0000250"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 95..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 103..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 182..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 186..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 195..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 265..278
FT /evidence="ECO:0000250"
FT DISULFID 273..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT VAR_SEQ 147..262
FT /note="VHEGSGETSQKETSTCDICQFGAECDEDAEDVWCVCNIDCSQTNFNPLCASD
FT GKSYDNACQIKEASCQKQEKIEVMSLGRCQDNTTTTTKSEDGHYARTDYAENANKLEES
FT AREHH -> EKFSKVMLILKPCTASSLEETNSKEIILCNPSNTHLLKKNENANLTCWSE
FT PFLQAYGLMRTWNSRQREAAKGITETRFLPPPSAYCLGIFIGANVKINSEALFRQWTVL
FT KGTIPVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="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
