ID   PTP1_ENCHE              Reviewed;         453 AA.
AC   O76273;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Polar tube protein 1;
DE   AltName: Full=Major polar tube protein;
DE            Short=Major PTP;
DE   AltName: Full=PTP Eh55;
DE   Flags: Precursor;
GN   Name=PTP1; Synonyms=PTP55;
OS   Encephalitozoon hellem (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=27973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=9747973; DOI=10.1016/s0166-6851(98)00071-1;
RA   Keohane E.M., Orr G.A., Zhang H.S., Takvorian P.M., Cali A., Tanowitz H.B.,
RA   Wittner M., Weiss L.M.;
RT   "The molecular characterization of the major polar tube protein gene from
RT   Encephalitozoon hellem, a microsporidian parasite of humans.";
RL   Mol. Biochem. Parasitol. 94:227-236(1998).
RN   [2]
RP   O-MANNOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15501763; DOI=10.1128/iai.72.11.6341-6350.2004;
RA   Xu Y., Takvorian P.M., Cali A., Orr G.A., Weiss L.M.;
RT   "Glycosylation of the major polar tube protein of Encephalitozoon hellem, a
RT   microsporidian parasite that infects humans.";
RL   Infect. Immun. 72:6341-6350(2004).
CC   -!- FUNCTION: Involved in formation of a polar tube through which the
CC       infectious agent is passed on to the host cell.
CC   -!- SUBCELLULAR LOCATION: Spore polar tube {ECO:0000269|PubMed:9747973}.
CC   -!- DEVELOPMENTAL STAGE: Found in spores. Expression is high during polar
CC       tube formation. {ECO:0000269|PubMed:9747973}.
CC   -!- PTM: O-mannosylated. O-mannosylation has functional significance for
CC       the ability of microsporidia to invade their host cells.
CC       {ECO:0000269|PubMed:15501763}.
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DR   EMBL; AF044915; AAC32812.1; -; Genomic_DNA.
DR   AlphaFoldDB; O76273; -.
DR   VEuPathDB; MicrosporidiaDB:EHEL_060170; -.
DR   VEuPathDB; MicrosporidiaDB:KMI_03g04600; -.
DR   GO; GO:0044099; C:polar tube; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycoprotein; Repeat; Signal; Sporulation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..453
FT                   /note="Polar tube protein 1"
FT                   /id="PRO_0000022182"
FT   REPEAT          214..233
FT                   /note="1"
FT   REPEAT          234..253
FT                   /note="2"
FT   REPEAT          254..273
FT                   /note="3"
FT   REPEAT          274..293
FT                   /note="4"
FT   REPEAT          294..313
FT                   /note="5"
FT   REPEAT          314..333
FT                   /note="6"
FT   REGION          61..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..333
FT                   /note="6 X 20 AA approximate tandem repeats"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  45461 MW;  DE519DFC6FF7F963 CRC64;
     MKGISKILSA SIMVMKLGNV YSAVPLCSNT YDPSQQQPSY VLIPSTPEAI TNCAYSPKNA
     YVPSSPTTSS STPGTNNDNE TSPTTEDVGT CKISVVKHCD TPGASSTPCE PEQTIPAQPV
     TMATVTPAII ASVQTPSVVS VIPVTQKVIQ PATMIVPPSS IIPGYYPNGT PAAPGQQGQI
     LSGSVLAPGA SSCQLVPGNT PGQMLPGMTP GVSPCLPTQG GDGSNQTIPG IVYPCQPGQG
     GSGSNQTIPG VISPCQPGQG GSGSNQTIPG IVYPCQPGQG GSGSNQTIPG VISPCQPGQG
     GSGSNQTIPG IVYPCQPGQN GDGSNQTIPG VISPCQPGQG GNGNGTTGQP GQCVSVPQTP
     NPIAMPPISG ISGNGYPTST TYTQSLGQLG PCIDVQKPTS SCESQTNEKS TMQYAMEACA
     APTPTVVIGN SEYLVGPGMY SSLTSPCNSC CQC