MP1_TALMA
ID MP1_TALMA Reviewed; 462 AA.
AC O42721;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cell wall mannoprotein 1 {ECO:0000303|PubMed:10074513, ECO:0000303|PubMed:9488383};
DE Flags: Precursor;
GN Name=MP1 {ECO:0000312|EMBL:AAC39367.1};
OS Talaromyces marneffei (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=37727;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION AS AN ANTIGEN,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=PM4 {ECO:0000303|PubMed:9488383};
RX PubMed=9488383; DOI=10.1128/iai.66.3.966-973.1998;
RA Cao L., Chan C.M., Lee C., Wong S.S., Yuen K.Y.;
RT "MP1 encodes an abundant and highly antigenic cell wall mannoprotein in the
RT pathogenic fungus Penicillium marneffei.";
RL Infect. Immun. 66:966-973(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=PM4 {ECO:0000303|PubMed:10074513};
RX PubMed=10074513; DOI=10.1128/jcm.37.4.981-986.1999;
RA Cao L., Chan K.M., Chen D., Vanittanakom N., Lee C., Chan C.M.,
RA Sirisanthana T., Tsang D.N., Yuen K.Y.;
RT "Detection of cell wall mannoprotein Mp1p in culture supernatants of
RT Penicillium marneffei and in sera of penicilliosis patients.";
RL J. Clin. Microbiol. 37:981-986(1999).
RN [3] {ECO:0007744|PDB:3L1N}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 187-346 OF MET-207 AND MET-276
RP MUTANT IN COMPLEX WITH PALMITATE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP SER-313 AND SER-332.
RC STRAIN=PM4 {ECO:0000303|PubMed:20053994};
RX PubMed=20053994; DOI=10.1074/jbc.m109.057760;
RA Liao S., Tung E.T., Zheng W., Chong K., Xu Y., Dai P., Guo Y., Bartlam M.,
RA Yuen K.Y., Rao Z.;
RT "Crystal structure of the Mp1p ligand binding domain 2 reveals its function
RT as a fatty acid-binding protein.";
RL J. Biol. Chem. 285:9211-9220(2010).
CC -!- FUNCTION: Constitutive protein of the cell wall. Binds fatty acids and
CC may thus serve as a fatty acid transporter between P.marneffei and host
CC cells during infection (PubMed:20053994). Abundant antigen target of
CC host humoral immune response (PubMed:9488383).
CC {ECO:0000269|PubMed:20053994, ECO:0000269|PubMed:9488383}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20053994}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10074513,
CC ECO:0000269|PubMed:9488383}. Note=Associated with the entire thickness
CC of the cell walls of yeast and conidia found in mold form. Localizes on
CC the outer layers of the hyphal cell walls.
CC {ECO:0000269|PubMed:9488383}.
CC -!- PTM: Mannoprotein, glycosylated. {ECO:0000269|PubMed:9488383}.
CC -!- BIOTECHNOLOGY: An enzyme-linked immunosorbent assay (ELISA) with
CC antibodies against Mp1 protein as well as Mp1 antigen-based ELISA can
CC be used to detect infections caused by P.marneffei (penicilliosis).
CC {ECO:0000269|PubMed:10074513}.
CC -!- SIMILARITY: Belongs to the cell wall mannoprotein 1 family.
CC {ECO:0000305}.
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DR EMBL; AF009957; AAC39367.1; -; mRNA.
DR PDB; 3L1N; X-ray; 1.30 A; A=187-346.
DR PDBsum; 3L1N; -.
DR AlphaFoldDB; O42721; -.
DR SMR; O42721; -.
DR VEuPathDB; FungiDB:PMAA_009820; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
DR GO; GO:0030446; C:hyphal cell wall; IDA:UniProtKB.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:UniProtKB.
DR GO; GO:0031505; P:fungal-type cell wall organization; IDA:UniProtKB.
DR InterPro; IPR021054; Cell_wall_mannoprotein_1.
DR Pfam; PF12296; HsbA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Lipid-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..462
FT /note="Cell wall mannoprotein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432781"
FT REGION 346..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:20053994,
FT ECO:0007744|PDB:3L1N"
FT MUTAGEN 313
FT /note="S->A: 2-fold increase in affinity for palmitic acid.
FT Decreased binding affinity for palmitic acid; when
FT associated with A-332."
FT /evidence="ECO:0000269|PubMed:20053994"
FT MUTAGEN 332
FT /note="S->A: Decreased binding affinity for palmitic acid;
FT when associated with A-313."
FT /evidence="ECO:0000269|PubMed:20053994"
FT HELIX 201..223
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:3L1N"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 295..319
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:3L1N"
FT HELIX 325..345
FT /evidence="ECO:0007829|PDB:3L1N"
SQ 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
