GenomeNet

Database: UniProt
Entry: Q9QYV1
LinkDB: Q9QYV1
Original site: Q9QYV1 
ID   TEFF1_RAT               Reviewed;         373 AA.
AC   Q9QYV1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 113.
DE   RecName: Full=Tomoregulin-1;
DE            Short=TR-1;
DE   AltName: Full=Protein NC1;
DE   AltName: Full=Transmembrane protein with EGF-like and one follistatin-like domain;
DE   Flags: Precursor;
GN   Name=Tmeff1; Synonyms=Nc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Kugler S., Baehr M.;
RT   "Reverse transcription of a highly G+C rich mRNA 5'end by Tth
RT   polymerase resolved inversions and deletions which were generated by
RT   MMLV reverse transcriptase.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: May inhibit NODAL and BMP signaling during neural
CC       patterning. {ECO:0000250}.
CC   -!- SUBUNIT: May interact with ST14. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
DR   EMBL; AJ250730; CAB60131.1; -; mRNA.
DR   EMBL; BC129093; AAI29094.1; -; mRNA.
DR   RefSeq; NP_075409.1; NM_023020.2.
DR   UniGene; Rn.162809; -.
DR   ProteinModelPortal; Q9QYV1; -.
DR   SMR; Q9QYV1; -.
DR   BioGrid; 248901; 1.
DR   STRING; 10116.ENSRNOP00000063443; -.
DR   MEROPS; I01.974; -.
DR   SwissPalm; Q9QYV1; -.
DR   PaxDb; Q9QYV1; -.
DR   PRIDE; Q9QYV1; -.
DR   Ensembl; ENSRNOT00000065775; ENSRNOP00000063443; ENSRNOG00000008034.
DR   GeneID; 63845; -.
DR   KEGG; rno:63845; -.
DR   UCSC; RGD:62005; rat.
DR   CTD; 8577; -.
DR   RGD; 62005; Tmeff1.
DR   eggNOG; ENOG410KCWX; Eukaryota.
DR   eggNOG; ENOG410XQG4; LUCA.
DR   GeneTree; ENSGT00940000160714; -.
DR   HOGENOM; HOG000154541; -.
DR   HOVERGEN; HBG053816; -.
DR   InParanoid; Q9QYV1; -.
DR   OMA; INCSELN; -.
DR   OrthoDB; 773030at2759; -.
DR   PhylomeDB; Q9QYV1; -.
DR   PRO; PR:Q9QYV1; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000008034; Expressed in 7 organ(s), highest expression level in Ammon's horn.
DR   Genevisible; Q9QYV1; RN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Developmental protein;
KW   Disulfide bond; EGF-like domain; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36    373       Tomoregulin-1.
FT                                /FTId=PRO_0000286058.
FT   TOPO_DOM     46    323       Extracellular. {ECO:0000255}.
FT   TRANSMEM    324    344       Helical. {ECO:0000255}.
FT   TOPO_DOM    345    373       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       86    138       Kazal-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      177    230       Kazal-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      264    304       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS     42     45       Poly-Gly.
FT   DISULFID     92    122       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID     96    115       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    104    136       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    183    214       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    187    207       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    196    228       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    268    281       {ECO:0000250}.
FT   DISULFID    276    292       {ECO:0000250}.
FT   DISULFID    294    303       {ECO:0000250}.
SQ   SEQUENCE   373 AA;  40143 MW;  BDB8BC681B10280E CRC64;
     MGAQAPLRLP AAPPLAVCGY TSVLLLFAFC LPGSGASNQP AGGGGDCPGG RGKSINCSEL
     NLRESDIRAC DESSCKYGGV CKEDGDGLKC ACQFQCHTNY IPVCGSNGDT YQNECFLRRA
     ACKHQKDITV VARGPCYSDN GSGSGEGEEE GSGAGAHRKH SKCGPCKYKA ECDEDAENVG
     CVCNIDCSGY SFNPVCASDG SSYNNPCFVR EASCIRQEQI DIRHLGHCTD TDDTSLLGKK
     DDGLQYRPDV KDAGDQREDV YIGSHMPCPE NLNGYCIHGK CEFIYSTQKA SCRCESGYTG
     QHCEKTDFSI LYVVPSRQKL THVLIAAIIG AVQIAIIVAI VMCITRKCPK NNRGRRQKQN
     LGHFTSETSS RMV
//
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