GenomeNet

Database: UniProt
Entry: Q91590
LinkDB: Q91590
Original site: Q91590 
ID   TEFF1_XENLA             Reviewed;         370 AA.
AC   Q91590;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   23-MAY-2018, entry version 79.
DE   RecName: Full=Tomoregulin-1;
DE            Short=TR-1;
DE   AltName: Full=Transmembrane protein with EGF-like and one follistatin-like domain;
DE   AltName: Full=X7365;
DE   Flags: Precursor;
GN   Name=tmeff1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Pituitary;
RX   PubMed=8752111;
RA   Eib D.W., Martens G.J.M.;
RT   "A novel transmembrane protein with epidermal growth factor and
RT   follistatin domains expressed in the hypothalamo-hypophysial axis of
RT   Xenopus laevis.";
RL   J. Neurochem. 67:1047-1055(1996).
RN   [2]
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
RX   PubMed=12618130; DOI=10.1016/S0012-1606(02)00075-1;
RA   Chang C., Eggen B.J.L., Weinstein D.C., Brivanlou A.H.;
RT   "Regulation of nodal and BMP signaling by tomoregulin-1 (X7365)
RT   through novel mechanisms.";
RL   Dev. Biol. 255:1-11(2003).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH CRIPTO.
RX   PubMed=14563676; DOI=10.1101/gad.1127703;
RA   Harms P.W., Chang C.;
RT   "Tomoregulin-1 (TMEFF1) inhibits nodal signaling through direct
RT   binding to the nodal coreceptor Cripto.";
RL   Genes Dev. 17:2624-2629(2003).
CC   -!- FUNCTION: Inhibits nodal/nr-1 and bmp signaling during neural
CC       patterning through interaction with cripto.
CC       {ECO:0000269|PubMed:12618130, ECO:0000269|PubMed:14563676}.
CC   -!- SUBUNIT: Interacts with cripto. {ECO:0000269|PubMed:14563676}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, and at
CC       lower levels in neuroendocrine tissues. Present in neurons from
CC       the diencephalon (at protein level). {ECO:0000269|PubMed:8752111}.
CC   -!- DEVELOPMENTAL STAGE: First expressed at stage 10.5. Expression
CC       increases during neurula stages and remains at least to tadpole
CC       stages. {ECO:0000269|PubMed:12618130}.
CC   -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB37751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA58792.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; U19879; AAB37751.1; ALT_INIT; mRNA.
DR   EMBL; X83962; CAA58792.1; ALT_INIT; mRNA.
DR   UniGene; Xl.77; -.
DR   ProteinModelPortal; Q91590; -.
DR   PRIDE; Q91590; -.
DR   HOVERGEN; HBG053816; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Disulfide bond; EGF-like domain;
KW   Membrane; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36    370       Tomoregulin-1.
FT                                /FTId=PRO_0000286059.
FT   TOPO_DOM     36    320       Extracellular. {ECO:0000255}.
FT   TRANSMEM    321    341       Helical. {ECO:0000255}.
FT   TOPO_DOM    342    370       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       83    135       Kazal-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      174    227       Kazal-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      261    301       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID     89    119       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID     93    112       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    101    133       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    180    211       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    184    204       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    193    225       {ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   DISULFID    265    278       {ECO:0000250}.
FT   DISULFID    273    289       {ECO:0000250}.
FT   DISULFID    291    300       {ECO:0000250}.
SQ   SEQUENCE   370 AA;  40330 MW;  782E3BE4E0E9D6E9 CRC64;
     MDGLHPASWM LLLGSLAFWS ASSLLLFSLA LPGARASNQL LSECHNGKGK GINCSELTVR
     ESEVRVCDES SCKYGGVCKE EGDVLKCICQ FQCQTNYAPV CGSNGDTYQN ECFLRRSACK
     QQKDITVVAR GPCFSDIASG SGEGEYEGSG GEVHKKHSKC GVCKFGAECD EDAGDVGCVC
     NIDCSGHNFN PVCATDGSSY SNPCLVREAS CLRQEQIDVK HIRSCIETDE TSIMGKKDEG
     LQNRPEVKDS TDQREGDFMG NYIPCSENYN GYCVHGKCEL SYSSQKASCR CDSGYTGQYC
     DKTDFNILYV VPSRQKLTHV LIAAIIGAVQ IAIIVAIVMC ITRKCPKNNR GRRQKQNLGH
     FSSDTSSRMV
//
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