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MP83_MYCTU
ID   MP83_MYCTU              Reviewed;         220 AA.
AC   P9WNF3; L0TAW5; P0A670; P71493; Q10790;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Cell surface glycolipoprotein MPT83;
DE   AltName: Full=Lipoprotein p23;
DE   Flags: Precursor;
GN   Name=mpt83; OrderedLocusNames=Rv2873; ORFNames=MTCY274.04;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=8633206; DOI=10.1046/j.1365-3083.1996.d01-78.x;
RA   Hewinson R.G., Michell S., Russell W.P., McAdam R.A., Jacobs W.R. Jr.;
RT   "Molecular characterization of MPT83: a seroreactive antigen of
RT   Mycobacterium tuberculosis with homology to MPT70.";
RL   Scand. J. Immunol. 43:490-499(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HOST TLR2.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=22174456; DOI=10.4049/jimmunol.1102177;
RA   Chen S.T., Li J.Y., Zhang Y., Gao X., Cai H.;
RT   "Recombinant MPT83 derived from Mycobacterium tuberculosis induces cytokine
RT   production and upregulates the function of mouse macrophages through
RT   TLR2.";
RL   J. Immunol. 188:668-677(2012).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=22567094; DOI=10.1371/journal.pone.0034991;
RA   Kao F.F., Mahmuda S., Pinto R., Triccas J.A., West N.P., Britton W.J.;
RT   "The secreted lipoprotein, MPT83, of Mycobacterium tuberculosis is
RT   recognized during human tuberculosis and stimulates protective immunity in
RT   mice.";
RL   PLoS ONE 7:E34991-E34991(2012).
CC   -!- FUNCTION: Recombinant, non-modified protein stimulates secretion of
CC       cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines
CC       in a TLR2-dependent fashion, which leads to increased host innate
CC       immunity responses against the bacterium (PubMed:22174456). Serves as a
CC       strong human and mouse antigen T cell antigen during M.tuberculosis
CC       infection, inducing strong IFN-gamma expression (PubMed:22567094).
CC       {ECO:0000269|PubMed:22174456, ECO:0000269|PubMed:22567094}.
CC   -!- SUBUNIT: Interacts with host TLR2 (tested in mouse) (PubMed:22174456).
CC       {ECO:0000269|PubMed:22174456}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000305|PubMed:22567094,
CC       ECO:0000305|PubMed:8633206}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}. Secreted, cell wall {ECO:0000305|PubMed:22567094}.
CC       Secreted {ECO:0000250|UniProtKB:P0CAX7}.
CC   -!- INDUCTION: Highly expressed and immunogenic during infection of mice
CC       with live bacteria (at protein level). {ECO:0000269|PubMed:8633206}.
CC   -!- PTM: O-glycosylated. Contains 0-3 mannose residues attached to residues
CC       48-49 in various configurations; the dominant glycoform is Thr-
CC       48(Man)/Thr-49(Man2) with an unusual Man(1->3)Man linkage, but
CC       Thr48(Man3)/Thr49(Man0) through to Thr48(Man0/)Thr49(Man3) are also
CC       seen (By similarity). {ECO:0000250|UniProtKB:P0CAX7}.
CC   -!- BIOTECHNOLOGY: Could be used in vaccine production; both recombinant
CC       protein and DNA vaccines stimulate antigen-specific T cell responses in
CC       mice (PubMed:22567094). {ECO:0000269|PubMed:22567094}.
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DR   EMBL; X94597; CAA64290.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45675.1; -; Genomic_DNA.
DR   PIR; D70923; D70923.
DR   RefSeq; NP_217389.1; NC_000962.3.
DR   RefSeq; WP_003414630.1; NZ_NVQJ01000006.1.
DR   AlphaFoldDB; P9WNF3; -.
DR   SMR; P9WNF3; -.
DR   STRING; 83332.Rv2873; -.
DR   PaxDb; P9WNF3; -.
DR   DNASU; 887155; -.
DR   GeneID; 887155; -.
DR   KEGG; mtu:Rv2873; -.
DR   TubercuList; Rv2873; -.
DR   eggNOG; COG2335; Bacteria.
DR   OMA; ICGGVQT; -.
DR   PhylomeDB; P9WNF3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR   Gene3D; 2.30.180.10; -; 1.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   Pfam; PF02469; Fasciclin; 1.
DR   SMART; SM00554; FAS1; 1.
DR   SUPFAM; SSF82153; SSF82153; 1.
DR   PROSITE; PS50213; FAS1; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           25..220
FT                   /note="Cell surface glycolipoprotein MPT83"
FT                   /id="PRO_0000008788"
FT   DOMAIN          83..215
FT                   /note="FAS1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   LIPID           25
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           25
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CARBOHYD        48
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0CAX7"
FT   CARBOHYD        49
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0CAX7"
SQ   SEQUENCE   220 AA;  22070 MW;  5CB99A4B51852A98 CRC64;
     MINVQAKPAA AASLAAIAIA FLAGCSSTKP VSQDTSPKPA TSPAAPVTTA AMADPAADLI
     GRGCAQYAAQ NPTGPGSVAG MAQDPVATAA SNNPMLSTLT SALSGKLNPD VNLVDTLNGG
     EYTVFAPTNA AFDKLPAATI DQLKTDAKLL SSILTYHVIA GQASPSRIDG THQTLQGADL
     TVIGARDDLM VNNAGLVCGG VHTANATVYM IDTVLMPPAQ
 
 
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