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Cell wall mannoprotein 1

 MP1_TALMA               Reviewed;         462 AA.
O42721;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
02-NOV-2016, entry version 35.
RecName: Full=Cell wall mannoprotein 1 {ECO:0000303|PubMed:10074513, ECO:0000303|PubMed:9488383};
Flags: Precursor;
Name=MP1 {ECO:0000312|EMBL:AAC39367.1};
Talaromyces marneffei (Penicillium marneffei).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
NCBI_TaxID=37727;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION AS AN ANTIGEN,
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=PM4 {ECO:0000303|PubMed:9488383};
PubMed=9488383;
Cao L., Chan C.M., Lee C., Wong S.S., Yuen K.Y.;
"MP1 encodes an abundant and highly antigenic cell wall mannoprotein
in the pathogenic fungus Penicillium marneffei.";
Infect. Immun. 66:966-973(1998).
[2]
SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
STRAIN=PM4 {ECO:0000303|PubMed:10074513};
PubMed=10074513;
Cao L., Chan K.M., Chen D., Vanittanakom N., Lee C., Chan C.M.,
Sirisanthana T., Tsang D.N., Yuen K.Y.;
"Detection of cell wall mannoprotein Mp1p in culture supernatants of
Penicillium marneffei and in sera of penicilliosis patients.";
J. Clin. Microbiol. 37:981-986(1999).
[3] {ECO:0000244|PDB:3L1N}
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 187-346 OF MET-207 AND
MET-276 MUTANT IN COMPLEX WITH FATTY ACIDS, FUNCTION, SUBUNIT, AND
MUTAGENESIS OF SER-313 AND SER-332.
STRAIN=PM4 {ECO:0000303|PubMed:20053994};
PubMed=20053994; DOI=10.1074/jbc.M109.057760;
Liao S., Tung E.T., Zheng W., Chong K., Xu Y., Dai P., Guo Y.,
Bartlam M., Yuen K.Y., Rao Z.;
"Crystal structure of the Mp1p ligand binding domain 2 reveals its
function as a fatty acid-binding protein.";
J. Biol. Chem. 285:9211-9220(2010).
-!- FUNCTION: Constitutive protein of the cell wall. Binds fatty acids
and may thus serve as a fatty acid transporter between P.marneffei
and host cells during infection (PubMed:20053994). Abundant
antigen target of host humoral immune response (PubMed:9488383).
{ECO:0000269|PubMed:20053994, ECO:0000269|PubMed:9488383}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20053994}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:10074513, ECO:0000269|PubMed:9488383}.
Note=Associated with the entire thickness of the cell walls of
yeast and conidia found in mold form. Localizes on the outer
layers of the hyphal cell walls. {ECO:0000269|PubMed:9488383}.
-!- PTM: Mannoprotein, glycosylated. {ECO:0000269|PubMed:9488383}.
-!- BIOTECHNOLOGY: An enzyme-linked immunosorbent assay (ELISA) with
antibodies against Mp1 protein as well as Mp1 antigen-based ELISA
can be used to detect infections caused by P.marneffei
(penicilliosis). {ECO:0000269|PubMed:10074513}.
-!- SIMILARITY: Belongs to the cell wall mannoprotein 1 family.
{ECO:0000305}.
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EMBL; AF009957; AAC39367.1; -; mRNA.
PDB; 3L1N; X-ray; 1.30 A; A=187-346.
PDBsum; 3L1N; -.
SMR; O42721; -.
eggNOG; ENOG410J1RI; Eukaryota.
eggNOG; ENOG410YRM0; LUCA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
GO; GO:0030446; C:hyphal cell wall; IDA:UniProtKB.
GO; GO:0030445; C:yeast-form cell wall; IDA:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0005199; F:structural constituent of cell wall; IDA:UniProtKB.
GO; GO:0031505; P:fungal-type cell wall organization; IDA:UniProtKB.
InterPro; IPR021054; Cell_wall_mannoprotein_1.
Pfam; PF12296; HsbA; 2.
1: Evidence at protein level;
3D-structure; Cell wall; Lipid-binding; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 462 Cell wall mannoprotein 1. {ECO:0000255}.
/FTId=PRO_0000432781.
REGION 275 282 Fatty acid-binding.
{ECO:0000269|PubMed:20053994}.
REGION 298 316 Fatty acid-binding.
{ECO:0000269|PubMed:20053994}.
REGION 332 339 Fatty acid-binding.
{ECO:0000269|PubMed:20053994}.
MUTAGEN 313 313 S->A: 2-fold increase in affinity for
palmitic acid. Decreased binding affinity
for palmitic acid; when associated with
A-332. {ECO:0000269|PubMed:20053994}.
MUTAGEN 332 332 S->A: Decreased binding affinity for
palmitic acid; when associated with A-
313. {ECO:0000269|PubMed:20053994}.
HELIX 201 223 {ECO:0000244|PDB:3L1N}.
HELIX 230 249 {ECO:0000244|PDB:3L1N}.
TURN 250 252 {ECO:0000244|PDB:3L1N}.
HELIX 258 265 {ECO:0000244|PDB:3L1N}.
HELIX 267 284 {ECO:0000244|PDB:3L1N}.
HELIX 286 291 {ECO:0000244|PDB:3L1N}.
HELIX 295 319 {ECO:0000244|PDB:3L1N}.
HELIX 322 324 {ECO:0000244|PDB:3L1N}.
HELIX 325 345 {ECO:0000244|PDB:3L1N}.
SEQUENCE 462 AA; 47895 MW; 3EAE5FBA4FC6A298 CRC64;
MKFLSSLVVL GLSAQALASP YVDHQATKDQ RDVNVFKQVL QDINLDVQKF DQDITQYQGG
DPTVLLADSD AIIKTTEEGI QRIGPQPPLS VTEALALVGP VQGVNKLIMK AVDHLIEKKG
PLVGGGYGPQ VKDSLERQAH AASKLSELVS SKVPSPLAPI SKQLSDQVAQ ALQKGIQAFS
ISARQATKVK REATKVQRDI SAFKKVIQNI SLAVNKFNVD IERYVGGDAS HLLADGNVLI
KATLDGVQSL QNEPPLSSME ALALVGPVQD LSNQILLAIQ NLIDKKEPLV QAGFGGKVEN
NLRQQEEAAQ KLSELVSTKV PHELADISRQ LSDGIAAGIK KGIDAFAGTG PAPTTSSTPE
ASTAPAPSTP PQTPEDTLVP ATSTPAPGPA PTAPDSSMVW PTSTTASPDV QPTITSSGTS
VPAAPTGGNS SPAVPAFTGA ASANQVSGAV GLAAGLLAVL AF


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