TEFF1_RAT
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 03-AUG-2022, entry version 126.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 polymerase
RT resolved inversions and deletions which were generated by MMLV reverse
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
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DR EMBL; AJ250730; CAB60131.1; -; mRNA.
DR EMBL; BC129093; AAI29094.1; -; mRNA.
DR RefSeq; NP_075409.1; NM_023020.2.
DR AlphaFoldDB; Q9QYV1; -.
DR SMR; Q9QYV1; -.
DR BioGRID; 248901; 1.
DR STRING; 10116.ENSRNOP00000063443; -.
DR MEROPS; I01.974; -.
DR MEROPS; I01.978; -.
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; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000160714; -.
DR HOGENOM; CLU_048579_1_0_1; -.
DR InParanoid; Q9QYV1; -.
DR OMA; DSTCRYG; -.
DR OrthoDB; 773030at2759; -.
DR PhylomeDB; Q9QYV1; -.
DR PRO; PR:Q9QYV1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008034; Expressed in Ammon's horn and 15 other tissues.
DR Genevisible; Q9QYV1; RN.
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; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; 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 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..373
FT /note="Tomoregulin-1"
FT /id="PRO_0000286058"
FT TOPO_DOM 46..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 86..138
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 177..230
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 264..304
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 92..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 96..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 104..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 183..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 187..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 196..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 268..281
FT /evidence="ECO:0000250"
FT DISULFID 276..292
FT /evidence="ECO:0000250"
FT DISULFID 294..303
FT /evidence="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
