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TMC2_CAEEL
ID   TMC2_CAEEL              Reviewed;        1203 AA.
AC   Q11069;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Transmembrane channel-like protein 2;
GN   Name=tmc-2; ORFNames=B0416.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225 AND ASN-748, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Probable ion channel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TMC family. {ECO:0000305}.
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DR   EMBL; FO080200; CCD61919.1; -; Genomic_DNA.
DR   PIR; H89606; H89606.
DR   RefSeq; NP_001335510.1; NM_001348601.1.
DR   AlphaFoldDB; Q11069; -.
DR   BioGRID; 46077; 2.
DR   STRING; 6239.B0416.1; -.
DR   TCDB; 1.A.17.4.8; the calcium-dependent chloride channel (ca-clc) family.
DR   iPTMnet; Q11069; -.
DR   EPD; Q11069; -.
DR   PaxDb; Q11069; -.
DR   PeptideAtlas; Q11069; -.
DR   PRIDE; Q11069; -.
DR   EnsemblMetazoa; B0416.1a.1; B0416.1a.1; WBGene00015177.
DR   GeneID; 181161; -.
DR   KEGG; cel:CELE_B0416.1; -.
DR   UCSC; B0416.1; c. elegans.
DR   CTD; 181161; -.
DR   WormBase; B0416.1a; CE51844; WBGene00015177; tmc-2.
DR   eggNOG; ENOG502QQGX; Eukaryota.
DR   GeneTree; ENSGT01050000244942; -.
DR   HOGENOM; CLU_272172_0_0_1; -.
DR   InParanoid; Q11069; -.
DR   OMA; CIGWADP; -.
DR   OrthoDB; 124678at2759; -.
DR   PhylomeDB; Q11069; -.
DR   PRO; PR:Q11069; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00015177; Expressed in embryo and 3 other tissues.
DR   ExpressionAtlas; Q11069; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR   InterPro; IPR038900; TMC.
DR   InterPro; IPR012496; TMC_dom.
DR   PANTHER; PTHR23302; PTHR23302; 1.
DR   Pfam; PF07810; TMC; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1203
FT                   /note="Transmembrane channel-like protein 2"
FT                   /id="PRO_0000185388"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        665..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        714..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        780..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        748
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   1203 AA;  136060 MW;  1B96886F827CC206 CRC64;
     MPKSGAHQPL VRHDTDDGGE TGQSVKSLAD VSEEEIDSRM SRRSSVIADL LSLFRRSSSV
     LVRPHTRLGN PNFDDDDDEF DEEDDKEASK DRILKKIQQK KEIIQKLRGQ PWYMKRKRRT
     LKVAQKHLQQ QEAKVSKARL YKAEAGRRLT QASRWLDNLK IYLIPWEAKI RKIESHFGSV
     VSSYFTFHRW VLGVNITITF IMCMFVVIPE WLADSRTQFG DDRYNKTKAI KVMPPAVRAR
     ADELSTVWDF GGYFQYSLLF YGFYSKETFF GETIKYRVPV AYFFCNIFIL GFSLFIILRK
     MAANNRRGTL SSGKTQQYLF NWKAFTGWDY TIGNPETAGN VYMANVIKFR EAINDDKQKP
     SDKHPWIRFV ARVLTNLFIC AMYVFSIWAI MQCGTLKGEH FFAQNATAIT ISLITLVFPN
     IFDLLGKIEK LHPRNALRFQ LGRVLVLYIL NYYTLIYSLM LQLEHLQKEK NASDNPISAL
     GHPGDAIGRT IRETVLPRYP VDNNPHTYYS YAPVTTTPIP ATSSWTTVLP DFGPFGVYNP
     KASVTKDDTV FSSPVVETHM FGPNSDWNET TVNAASPTGA TTRASLRMSQ GGLCWETIIG
     QEITKLVTMD LYMTVASIFL IDFLRGLACR YLNLYWPWDL ERTFPEYGEF KVAENVLHLV
     NNQGMIWLGL FFVPLLPMLN NIKLIILMYI RGWAAMTCNV PASQIFRASR SSNFFFALLI
     LFLFLCTLPV GFVIASKTPS KSCGPFGNQS FFYSVITDVL HENLDKTLVN GIKYSLSPGI
     IIPVLVLLSL VIYFLIAMVT GLSQANQDLS FQLMVERTEE KKKIFELAGG KKKKSKDNTF
     GKQKPKQLLP PPTKGVSSDD DSQHNRSTAK SVSGRQFVPS LGSVSEVDHS TGEEQSSDSE
     STTSSLPPKL SLRQRFLVCI GWADPNKYGR HDDIEMEEGG GRLRELSTGS ETDSDDEDSE
     KSNRDMSYRT AIQSFDQNSQ SASASSSKST TTAPSNSEMR IEITENPLHT YITPLRIEKK
     SSASSSSSSH QPSSSIEKQA ARRLLQPIST THNIRYGVAT VENSSQDPTR PPSTDDSLGD
     PALHEPLWAN LNPHSSYTSA MMSPIMNEVM SNDETTDDEK GRLIPDRPPI PHSPRELKRL
     KREKDQQSES GSKPSTPRPP RFRISMSPPR KPPSEKNDSD SSNRKYEMRV EKSPKKPKKS
     DND
 
 
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