TEFF2_BOVIN
ID TEFF2_BOVIN Reviewed; 374 AA.
AC Q17QD6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Tomoregulin-2;
DE Short=TR-2;
DE AltName: Full=Transmembrane protein with EGF-like and two follistatin-like domains;
DE Flags: Precursor;
GN Name=TMEFF2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be a survival factor for hippocampal and mesencephalic
CC neurons. The shedded form may up-regulate cell proliferation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. Contains chondroitin sulfate glycosaminoglycans
CC (By similarity). {ECO:0000250}.
CC -!- PTM: A soluble form (TMEFF2-ECD) is produced by proteolytic shedding.
CC This shedding can be induced by phorbol ester or pro-inflammatory
CC cytokines such as TNFalpha, and is mediated by a metalloproteinase ADAM
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
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DR EMBL; BC118420; AAI18421.1; -; mRNA.
DR RefSeq; NP_001069569.1; NM_001076101.2.
DR AlphaFoldDB; Q17QD6; -.
DR SMR; Q17QD6; -.
DR STRING; 9913.ENSBTAP00000019754; -.
DR PaxDb; Q17QD6; -.
DR Ensembl; ENSBTAT00000019754; ENSBTAP00000019754; ENSBTAG00000014832.
DR GeneID; 538354; -.
DR KEGG; bta:538354; -.
DR CTD; 23671; -.
DR VEuPathDB; HostDB:ENSBTAG00000014832; -.
DR VGNC; VGNC:35940; TMEFF2.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000156056; -.
DR HOGENOM; CLU_048579_1_0_1; -.
DR InParanoid; Q17QD6; -.
DR OMA; XCDAGYT; -.
DR OrthoDB; 773030at2759; -.
DR TreeFam; TF330868; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000014832; Expressed in floor plate of diencephalon and 78 other tissues.
DR ExpressionAtlas; Q17QD6; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0045720; P:negative regulation of integrin biosynthetic process; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..374
FT /note="Tomoregulin-2"
FT /id="PRO_0000286060"
FT TOPO_DOM 40..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..374
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 261..301
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 303..320
FT /note="Required for shedding"
FT /evidence="ECO:0000250"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
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 265..278
FT /evidence="ECO:0000250"
FT DISULFID 273..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 41385 MW; 1E5B80ABFFFC78E8 CRC64;
MVLWESPRQC SSWTLCEGFC WLLLLPVMLL IVARPVKLAA FPTSLSDCQT PTGWNCSGYD
DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNSDYV PVCGSNGESY QNECYLRQAA
CKQQSEILVV SEGSCATDAG SGSGDGVHEG SGETSQKETS TCDICQFGAE CDEDAEDVWC
VCNIDCSQTN FNPLCASDGK SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG
HYARTDFAEN ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC
EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR IHRQKQNTGH
YSSDNTTRAS TRLI
