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TEFF1_MOUSE
ID   TEFF1_MOUSE             Reviewed;         372 AA.
AC   Q6PFE7; A2AJN3; Q8BRP7; Q8C536; Q9JJS1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Tomoregulin-1;
DE            Short=TR-1;
DE   AltName: Full=M7365;
DE   AltName: Full=Transmembrane protein with EGF-like and one follistatin-like domain;
DE   Flags: Precursor;
GN   Name=Tmeff1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-372 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=11025219; DOI=10.1016/s0925-4773(00)00426-3;
RA   Eib D.W., Holling T.M., Zwijsen A., Dewulf N., de Groot E.,
RA   van den Eijnden-van Raaij A.J.M., Huylebroeck D., Martens G.J.M.;
RT   "Expression of the follistatin/EGF-containing transmembrane protein M7365
RT   (tomoregulin-1) during mouse development.";
RL   Mech. Dev. 97:167-171(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-372 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-372 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal cord;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11165370; DOI=10.1016/s0169-328x(00)00257-6;
RA   Kanemoto N., Horie M., Omori K., Nishino N., Kondo M., Noguchi K.,
RA   Tanigami A.;
RT   "Expression of TMEFF1 mRNA in the mouse central nervous system: precise
RT   examination and comparative studies of TMEFF1 and TMEFF2.";
RL   Brain Res. Mol. Brain Res. 86:48-55(2001).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11404089; DOI=10.1016/s0925-4773(01)00362-8;
RA   Morais da Silva S., Gates P.B., Eib D.W., Martens G.J.M., Brockes J.P.;
RT   "The expression pattern of tomoregulin-1 in urodele limb regeneration and
RT   mouse limb development.";
RL   Mech. Dev. 104:125-128(2001).
CC   -!- FUNCTION: May inhibit NODAL and BMP signaling during neural patterning.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: May interact with ST14. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PFE7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PFE7-2; Sequence=VSP_024960;
CC       Name=3;
CC         IsoId=Q6PFE7-3; Sequence=VSP_024960, VSP_024961;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, neurointermediate lobe, pars
CC       distalis, pancreas, ovary and testis. {ECO:0000269|PubMed:11025219,
CC       ECO:0000269|PubMed:11165370}.
CC   -!- DEVELOPMENTAL STAGE: At 8.5 dpc, highly expressed in the first
CC       branchial arch, somites, splanchnic mesoderm and ventral foregut
CC       epithelium. At 9.5 dpc, highly expressed in motor neurons and
CC       superficial neurons from the neural tube, and in the dorsal part of
CC       diencephalon and mesencephalon. At 11.5 dpc and 12.5 dpc, expressed in
CC       limbs. At 15.5 dpc, highly expressed in brain and spinal cord.
CC       {ECO:0000269|PubMed:11025219, ECO:0000269|PubMed:11404089}.
CC   -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB90827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL772151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC057598; AAH57598.1; -; mRNA.
DR   EMBL; AJ400622; CAB90827.1; ALT_INIT; mRNA.
DR   EMBL; AK043792; BAC31655.1; -; mRNA.
DR   EMBL; AK079633; BAC37709.1; -; mRNA.
DR   CCDS; CCDS18168.1; -. [Q6PFE7-1]
DR   RefSeq; NP_067411.1; NM_021436.2. [Q6PFE7-1]
DR   RefSeq; XP_006537899.1; XM_006537836.1.
DR   RefSeq; XP_006537900.1; XM_006537837.1. [Q6PFE7-3]
DR   AlphaFoldDB; Q6PFE7; -.
DR   STRING; 10090.ENSMUSP00000030032; -.
DR   MEROPS; I01.974; -.
DR   MEROPS; I01.978; -.
DR   GlyConnect; 2434; 1 N-Linked glycan (1 site). [Q6PFE7-2]
DR   GlyGen; Q6PFE7; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q6PFE7; -.
DR   PhosphoSitePlus; Q6PFE7; -.
DR   MaxQB; Q6PFE7; -.
DR   PaxDb; Q6PFE7; -.
DR   PeptideAtlas; Q6PFE7; -.
DR   PRIDE; Q6PFE7; -.
DR   ProteomicsDB; 263156; -. [Q6PFE7-1]
DR   ProteomicsDB; 263157; -. [Q6PFE7-2]
DR   ProteomicsDB; 263158; -. [Q6PFE7-3]
DR   Antibodypedia; 34902; 215 antibodies from 22 providers.
DR   DNASU; 230157; -.
DR   Ensembl; ENSMUST00000030032; ENSMUSP00000030032; ENSMUSG00000028347. [Q6PFE7-1]
DR   Ensembl; ENSMUST00000123476; ENSMUSP00000115841; ENSMUSG00000028347. [Q6PFE7-1]
DR   GeneID; 230157; -.
DR   KEGG; mmu:230157; -.
DR   UCSC; uc008svk.1; mouse. [Q6PFE7-1]
DR   UCSC; uc008svl.1; mouse. [Q6PFE7-2]
DR   CTD; 8577; -.
DR   MGI; MGI:1926810; Tmeff1.
DR   VEuPathDB; HostDB:ENSMUSG00000028347; -.
DR   eggNOG; KOG3649; Eukaryota.
DR   GeneTree; ENSGT00940000160714; -.
DR   InParanoid; Q6PFE7; -.
DR   OMA; DSTCRYG; -.
DR   OrthoDB; 773030at2759; -.
DR   PhylomeDB; Q6PFE7; -.
DR   TreeFam; TF330868; -.
DR   BioGRID-ORCS; 230157; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Tmeff1; mouse.
DR   PRO; PR:Q6PFE7; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q6PFE7; protein.
DR   Bgee; ENSMUSG00000028347; Expressed in cortical plate and 243 other tissues.
DR   ExpressionAtlas; Q6PFE7; baseline and differential.
DR   Genevisible; Q6PFE7; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
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; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..372
FT                   /note="Tomoregulin-1"
FT                   /id="PRO_0000286057"
FT   TOPO_DOM        36..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..372
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          263..303
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          139..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
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   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        267..280
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..291
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..302
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         146
FT                   /note="G -> GA (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11025219,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024960"
FT   VAR_SEQ         251..252
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024961"
FT   CONFLICT        235
FT                   /note="L -> S (in Ref. 4; CAB90827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="D -> P (in Ref. 4; CAB90827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="Q -> L (in Ref. 4; CAB90827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="R -> K (in Ref. 4; CAB90827)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  40114 MW;  BB3DA6710B78A530 CRC64;
     MGAQAPLRLP AAPPLAVCGY TSVLLLFAFC LPGSRASNQP AGGGGDCPGG RGKSNCSELN
     LRESDIRVCD ESSCKYGGVC KEDGDGLKCA CQFQCHTNYI PVCGSNGDTY QNECFLRRAA
     CKHQKDITVV ARGPCYSDNG SGSGEGEEEG SGAGAHRKHS KCGPCKYKAE CDEDAENVGC
     VCNIDCSGYS FNPVCASDGS SYNNPCFVRE ASCIKQEQID IRHLGHCTDT DDVSLLGKKD
     DGLQYRPDVK DAGDEREDVY IGSHMPCPEN LNGYCIHGKC EFIYSTQKAS CRCESGYTGQ
     HCEKTDFSIL YVVPSRQKLT HVLIAAIIGA VQIAIIVAIV MCITRKCPKN NRGRRQKQNL
     GHFTSDTSSR MV
 
 
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