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MTD1_CAEEL
ID   MTD1_CAEEL              Reviewed;         278 AA.
AC   G5ECI1;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein mtd-1 {ECO:0000305};
DE   AltName: Full=Mec three-dependent expression protein 1 {ECO:0000303|PubMed:12385749, ECO:0000312|WormBase:ZK337.5};
DE   Flags: Precursor;
GN   Name=mtd-1 {ECO:0000303|PubMed:12385749, ECO:0000312|WormBase:ZK337.5};
GN   ORFNames=ZK337.5 {ECO:0000312|WormBase:ZK337.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=12385749; DOI=10.1016/s0925-4773(02)00293-9;
RA   Zhang Y., Chalfie M.;
RT   "MTD-1, a touch-cell-specific membrane protein with a subtle effect on
RT   touch sensitivity.";
RL   Mech. Dev. 119:3-7(2002).
CC   -!- FUNCTION: Plays a role in mechanosensory transduction (touch
CC       sensitivity). {ECO:0000269|PubMed:12385749}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12385749};
CC       Single-pass type I membrane protein {ECO:0000255}; Extracellular side
CC       {ECO:0000305|PubMed:12385749}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos and larva (PubMed:12385749).
CC       In L2 and L3 stage larva, expressed in the six touch receptor neurons
CC       (PubMed:12385749). {ECO:0000269|PubMed:12385749}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in no visible
CC       phenotype (PubMed:12385749). RNAi-mediated knockdown enhances the
CC       touch-insensitive phenotype (the inability to respond to more than two
CC       of four touches) of mec-6 u247ts mutants at 15 degrees Celsius
CC       (PubMed:12385749). {ECO:0000269|PubMed:12385749}.
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DR   EMBL; BX284601; CAB51468.1; -; Genomic_DNA.
DR   PIR; T21718; T21718.
DR   RefSeq; NP_493615.1; NM_061214.6.
DR   AlphaFoldDB; G5ECI1; -.
DR   STRING; 6239.ZK337.5; -.
DR   PaxDb; G5ECI1; -.
DR   PeptideAtlas; G5ECI1; -.
DR   EnsemblMetazoa; ZK337.5.1; ZK337.5.1; WBGene00003471.
DR   GeneID; 191285; -.
DR   KEGG; cel:CELE_ZK337.5; -.
DR   CTD; 191285; -.
DR   WormBase; ZK337.5; CE24721; WBGene00003471; mtd-1.
DR   eggNOG; ENOG502TGU6; Eukaryota.
DR   HOGENOM; CLU_991237_0_0_1; -.
DR   InParanoid; G5ECI1; -.
DR   OMA; CQGHNIW; -.
DR   OrthoDB; 1112437at2759; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003471; Expressed in larva and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:1905789; P:positive regulation of detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..278
FT                   /note="Protein mtd-1"
FT                   /id="PRO_5003475913"
FT   TOPO_DOM        18..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        255..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   278 AA;  31379 MW;  342FF46610ACA3AE CRC64;
     MRSSLLLLVF FLSIGWARYC VHNEKSWCQG HNIWGWCFHN KSSGVFNCDD NAFCVSQEQL
     KNKKSSGCFL RDNSSICCCN DADGCNLGFI GVQPKYAHGQ QCTNSMEVPN EDIRQFRPCD
     DPFCYSVLTA EDDGGPTTVT RGCHSRKMVM HHMSKNEDDK YQNNTKWRET KQIAEMPSCA
     EILKDQPKVN GTTSMCVDFT YDQEAEDGEE VDEPIKMKGR LCCCAGSNKC NEHAMWADEG
     ISLTEMLEEI EARKVPVDSS APVNIILSIA FSIFLIHF
 
 
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