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Alanine and proline-rich secreted protein Apa (45 kDa glycoprotein) (45/47 kDa antigen) (Antigen MPT-32) (FAP-B) (Fibronectin attachment protein) (Immunogenic protein MPT32)

 APA_MYCTU               Reviewed;         325 AA.
P9WIR7; L0T9G7; O08062; Q50906;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
20-DEC-2017, entry version 25.
RecName: Full=Alanine and proline-rich secreted protein Apa;
AltName: Full=45 kDa glycoprotein;
AltName: Full=45/47 kDa antigen {ECO:0000303|PubMed:7558311};
AltName: Full=Antigen MPT-32;
AltName: Full=FAP-B;
AltName: Full=Fibronectin attachment protein;
AltName: Full=Immunogenic protein MPT32;
Flags: Precursor;
Name=apa; Synonyms=modD; OrderedLocusNames=Rv1860;
ORFNames=MTCY359.13;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=7558311;
Laqueyrerie A., Militzer P., Romain F., Eiglmeier K., Cole S.,
Marchel G.;
"Cloning, sequencing, and expression of the apa gene coding for the
Mycobacterium tuberculosis 45/47-kilodalton secreted antigen
complex.";
Infect. Immun. 63:4003-4010(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
Laqueyrerie A.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[4]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
PubMed=1898899;
Nagai S., Wiker H.G., Harboe M., Kinomoto M.;
"Isolation and partial characterization of major protein antigens in
the culture fluid of Mycobacterium tuberculosis.";
Infect. Immun. 59:372-382(1991).
[5]
PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION.
PubMed=7622204;
Dobos K.M., Swiderek K., Khoo K.-H., Brennan P.J., Belisle J.T.;
"Evidence for glycosylation sites on the 45-kilodalton glycoprotein of
Mycobacterium tuberculosis.";
Infect. Immun. 63:2846-2853(1995).
[6]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT THR-49; THR-57; THR-66 AND
THR-316, AND STRUCTURE OF CARBOHYDRATE.
PubMed=8626314; DOI=10.1128/jb.178.9.2498-2506.1996;
Dobos K.M., Khoo K.-H., Swiderek K.M., Brennan P.J., Belisle J.T.;
"Definition of the full extent of glycosylation of the 45-kilodalton
glycoprotein of Mycobacterium tuberculosis.";
J. Bacteriol. 178:2498-2506(1996).
[7]
PROTEIN SEQUENCE OF 40-49, CHARACTERIZATION OF GLYCOSYLATION BY MASS
SPECTROMETRY, AND BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10542234; DOI=10.1074/jbc.274.45.32023;
Horn C., Namane A., Pescher P., Riviere M., Romain F., Puzo G.,
Barzu O., Marchal G.;
"Decreased capacity of recombinant 45/47-kDa molecules (Apa) of
Mycobacterium tuberculosis to stimulate T lymphocyte responses related
to changes in their mannosylation pattern.";
J. Biol. Chem. 274:32023-32030(1999).
[8]
PROTEIN SEQUENCE OF 40-57, FUNCTION, CHARACTERIZATION OF GLYCOSYLATION
BY MASS SPECTROMETRY, AND BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10531201;
Romain F., Horn C., Pescher P., Namane A., Riviere M., Puzo G.,
Barzu O., Marchal G.;
"Deglycosylation of the 45/47-kilodalton antigen complex of
Mycobacterium tuberculosis decreases its capacity to elicit in vivo or
in vitro cellular immune responses.";
Infect. Immun. 67:5567-5572(1999).
[9]
FUNCTION, AND BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12654810; DOI=10.1128/IAI.71.4.1929-1937.2003;
Kumar P., Amara R.R., Challu V.K., Chadda V.K., Satchidanandam V.;
"The Apa protein of Mycobacterium tuberculosis stimulates gamma
interferon-secreting CD4+ and CD8+ T cells from purified protein
derivative-positive individuals and affords protection in a guinea pig
model.";
Infect. Immun. 71:1929-1937(2003).
[10]
FUNCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16092920; DOI=10.1042/BJ20050709;
Pitarque S., Herrmann J.L., Duteyrat J.L., Jackson M., Stewart G.R.,
Lecointe F., Payre B., Schwartz O., Young D.B., Marchal G.,
Lagrange P.H., Puzo G., Gicquel B., Nigou J., Neyrolles O.;
"Deciphering the molecular bases of Mycobacterium tuberculosis binding
to the lectin DC-SIGN reveals an underestimated complexity.";
Biochem. J. 392:615-624(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=H37Rv;
PubMed=25359607; DOI=10.1111/sji.12249;
Esparza M., Palomares B., Garcia T., Espinosa P., Zenteno E.,
Mancilla R.;
"PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an
adhesin, which binds the macrophage mannose receptor and promotes
phagocytosis.";
Scand. J. Immunol. 81:46-55(2015).
-!- FUNCTION: A potent antigen in animals immunized with live
bacteria, it induces a strong delayed-type hypersensitivity (DTH)
in immunized animals (PubMed:10531201). Elicits a mostly Th1 type
of T-cell response in healthy humans; induces IFN-gamma production
from CD4(+) and CD8(+) cells (PubMed:12654810). Functions as an
adhesin, binds to mouse macrophages via mannose residues
(PubMed:10531201, PubMed:25359607). Might interact via host CD209
(PubMed:16092920). {ECO:0000269|PubMed:10531201,
ECO:0000269|PubMed:12654810, ECO:0000269|PubMed:16092920,
ECO:0000269|PubMed:25359607}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10531201}. Cell
surface {ECO:0000269|PubMed:25359607}.
-!- PTM: Glycosylated, with mannose residues (PubMed:8626314,
PubMed:10542234, PubMed:10531201, PubMed:25359607). The secreted
protein has from 0 to 9 mannose residues, the majority have 6, 7,
or 8 mannose residues (22, 24 and 17% respectively)
(PubMed:10531201). Deglycosylated molecules had a significantly
lower capacity to elicit a DTH reaction in guinea pigs in vivo or
to activate specific T lymphocytes in vitro (PubMed:10531201).
Pretreating mouse macrophages with mannan decreases binding of
M.tuberculosis (PubMed:25359607). The non-glycosylated form
stimulates IFN-gamma production however, so glycosylation is not
essential (PubMed:12654810). {ECO:0000269|PubMed:10531201,
ECO:0000269|PubMed:10542234, ECO:0000269|PubMed:25359607,
ECO:0000269|PubMed:8626314, ECO:0000305|PubMed:12654810}.
-!- PTM: Runs as 45 and 47 kDa protein, the nature of the difference
between the 2 forms is not known but is still seen after alpha-
mannosidase treatment (PubMed:10531201).
{ECO:0000269|PubMed:10531201}.
-!- MASS SPECTROMETRY: Mass=28782; Mass_error=1.6;
Method=Electrospray; Range=40-325; Note=Chemically or
enzymatically deglycosylated protein.;
Evidence={ECO:0000269|PubMed:10531201};
-!- BIOTECHNOLOGY: Major immunodominant antigen that has potential as
a vaccine against tuberculosis (PubMed:10542234, PubMed:10531201,
PubMed:12654810). Can be used as a DNA vaccine in guinea pigs
(PubMed:12654810). Apa-ELISA could be used in diagnosis.
{ECO:0000269|PubMed:10531201, ECO:0000269|PubMed:10542234,
ECO:0000269|PubMed:12654810}.
-!- SIMILARITY: Belongs to the Apa family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be involved in molybdenum
transport. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X80268; CAA56555.1; -; Genomic_DNA.
EMBL; X99258; CAA67645.1; -; Genomic_DNA.
EMBL; AL123456; CCP44626.1; -; Genomic_DNA.
PIR; D70666; D70666.
RefSeq; WP_003911690.1; NZ_KK339370.1.
RefSeq; YP_177849.1; NC_000962.3.
ProteinModelPortal; P9WIR7; -.
STRING; 83332.Rv1860; -.
iPTMnet; P9WIR7; -.
PaxDb; P9WIR7; -.
EnsemblBacteria; CCP44626; CCP44626; Rv1860.
GeneID; 885896; -.
KEGG; mtu:Rv1860; -.
TubercuList; Rv1860; -.
OMA; GEFFMPY; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0050840; F:extracellular matrix binding; IEA:InterPro.
GO; GO:0009267; P:cellular response to starvation; IEP:MTBBASE.
GO; GO:0052559; P:induction by symbiont of host immune response; IDA:MTBBASE.
InterPro; IPR010801; FAP.
Pfam; PF07174; FAP; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 39 {ECO:0000269|PubMed:10531201,
ECO:0000269|PubMed:10542234}.
CHAIN 40 325 Alanine and proline-rich secreted protein
Apa.
/FTId=PRO_0000020745.
REPEAT 85 88 1.
REPEAT 94 97 2.
REPEAT 104 107 3.
REGION 85 107 3 X 4 AA approximate repeats of [DA]-P-N-
A.
CARBOHYD 49 49 O-linked (Man...) threonine.
{ECO:0000269|PubMed:8626314}.
CARBOHYD 57 57 O-linked (Man...) threonine.
{ECO:0000269|PubMed:8626314}.
CARBOHYD 66 66 O-linked (Man) threonine.
{ECO:0000269|PubMed:8626314}.
CARBOHYD 316 316 O-linked (Man...) threonine.
{ECO:0000269|PubMed:8626314}.
SEQUENCE 325 AA; 32721 MW; 59E5D0455A997BED CRC64;
MHQVDPNLTR RKGRLAALAI AAMASASLVT VAVPATANAD PEPAPPVPTT AASPPSTAAA
PPAPATPVAP PPPAAANTPN AQPGDPNAAP PPADPNAPPP PVIAPNAPQP VRIDNPVGGF
SFALPAGWVE SDAAHFDYGS ALLSKTTGDP PFPGQPPPVA NDTRIVLGRL DQKLYASAEA
TDSKAAARLG SDMGEFYMPY PGTRINQETV SLDANGVSGS ASYYEVKFSD PSKPNGQIWT
GVIGSPAANA PDAGPPQRWF VVWLGTANNP VDKGAAKALA ESIRPLVAPP PAPAPAPAEP
APAPAPAGEV APTPTTPTPQ RTLPA


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