TEFF1_XENLA
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 25-MAY-2022, entry version 89.
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; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=8752111; DOI=10.1046/j.1471-4159.1996.67031047.x;
RA Eib D.W., Martens G.J.M.;
RT "A novel transmembrane protein with epidermal growth factor and follistatin
RT domains expressed in the hypothalamo-hypophysial axis of 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) through
RT 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 binding to
RT 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 type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, and at lower
CC levels in neuroendocrine tissues. Present in neurons from the
CC 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 stages.
CC {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};
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DR EMBL; U19879; AAB37751.1; ALT_INIT; mRNA.
DR EMBL; X83962; CAA58792.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q91590; -.
DR SMR; Q91590; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..370
FT /note="Tomoregulin-1"
FT /id="PRO_0000286059"
FT TOPO_DOM 36..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 83..135
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 174..227
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 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 89..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 93..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 101..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 180..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 184..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 193..225
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"
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
