MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Transmembrane protein 100; |
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| MyHits synonyms | TM100_RAT , Q569C0 , DB6481BE3194641F |
 Legends: 1, Phosphoserine. {ECO:0000244|PubMed:22673903}; 2, TRANSMEM Helical. {ECO:0000255}.
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ID TM100_RAT Reviewed; 134 AA.
AC Q569C0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 10-MAY-2017, entry version 69.
DE RecName: Full=Transmembrane protein 100;
GN Name=Tmem100;
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA Lundby C., Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14
RT different rat organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role during embryonic arterial endothelium
CC differentiation and vascular morphogenesis through the ACVRL1
CC receptor-dependent signaling pathway upon stimulation by bone
CC morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in
CC the regulation of nociception, acting as a modulator of the
CC interaction between TRPA1 and TRPV1, two molecular sensors and
CC mediators of pain signals in dorsal root ganglia (DRG) neurons.
CC Mechanistically, it weakens their interaction, thereby releasing
CC the inhibition of TRPA1 by TRPV1 and increasing the single-channel
CC open probability of the TRPA1-TRPV1 complex.
CC {ECO:0000250|UniProtKB:Q9CQG9}.
CC -!- SUBUNIT: Interacts (via C-terminus) with TRPA1 and TRPV1.
CC {ECO:0000250|UniProtKB:Q9CQG9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane
CC {ECO:0000250|UniProtKB:Q9CQG9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9CQG9}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Perikaryon {ECO:0000250}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic
CC reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in
CC neural cell bodies and neural fibers of the enteric nervous system
CC (By similarity). {ECO:0000250}.
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DR EMBL; BC092577; AAH92577.1; -; mRNA.
DR RefSeq; NP_001017479.1; NM_001017479.1.
DR RefSeq; XP_008766324.1; XM_008768102.2.
DR UniGene; Rn.18850; -.
DR iPTMnet; Q569C0; -.
DR PhosphoSitePlus; Q569C0; -.
DR PaxDb; Q569C0; -.
DR Ensembl; ENSRNOT00000003297; ENSRNOP00000003297; ENSRNOG00000002434.
DR GeneID; 497979; -.
DR KEGG; rno:497979; -.
DR CTD; 55273; -.
DR RGD; 1560541; Tmem100.
DR eggNOG; ENOG410IY9U; Eukaryota.
DR eggNOG; ENOG410YJ77; LUCA.
DR GeneTree; ENSGT00390000018520; -.
DR HOGENOM; HOG000154600; -.
DR HOVERGEN; HBG054506; -.
DR InParanoid; Q569C0; -.
DR OMA; PLVSECQ; -.
DR OrthoDB; EOG091G0X1R; -.
DR PhylomeDB; Q569C0; -.
DR TreeFam; TF332068; -.
DR PRO; PR:Q569C0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002434; -.
DR Genevisible; Q569C0; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0060842; P:arterial endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR InterPro; IPR032536; TMEM100.
DR PANTHER; PTHR16100:SF7; PTHR16100:SF7; 1.
DR Pfam; PF16311; TMEM100; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
KW Differentiation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 134 Transmembrane protein 100.
FT /FTId=PRO_0000240848.
FT TRANSMEM 56 76 Helical. {ECO:0000255}.
FT TRANSMEM 84 104 Helical. {ECO:0000255}.
FT MOD_RES 15 15 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 121 121 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 133 ipfam:TMEM100 [T]
SQ SEQUENCE 134 AA; 14352 MW; DB6481BE3194641F CRC64;
MTEEPTKENL GGPKSPTPVT MEKSPKSEVV VTTVPLVSEV QLTAATGGAE LSCYRCIIPF
AVVVFITGIV VTAVAYSFNS HGSVISILGL VLLSSGLFLL ASSALCWKVR QRNKKVKRRE
SQTALVVNQR SLFA
//
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