ID   PTP3_ENCCU              Reviewed;        1256 AA.
AC   Q8MTP3; Q8SU21;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Polar tube protein 3;
DE   Flags: Precursor;
GN   Name=PTP3; OrderedLocusNames=ECU11_1440;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH PTP1 AND PTP2, AND DEVELOPMENTAL STAGE.
RX   PubMed=12076771; DOI=10.1016/s0166-6851(02)00073-7;
RA   Peuvel I., Peyret P., Metenier G., Vivares C.P., Delbac F.;
RT   "The microsporidian polar tube: evidence for a third polar tube protein
RT   (PTP3) in Encephalitozoon cuniculi.";
RL   Mol. Biochem. Parasitol. 122:69-80(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Involved in the sporoblast-to-spore polar tube biogenesis.
CC       Plays a role in the control of the polar tube extrusion as part of a
CC       specific response to ionic stimuli. {ECO:0000269|PubMed:12076771}.
CC   -!- SUBUNIT: Interacts with PTP1 and PTP2. {ECO:0000269|PubMed:12076771}.
CC   -!- SUBCELLULAR LOCATION: Spore polar tube {ECO:0000269|PubMed:12076771}.
CC   -!- DEVELOPMENTAL STAGE: Found in spores. Expression is high during polar
CC       tube formation. {ECO:0000269|PubMed:12076771,
CC       ECO:0000269|PubMed:16691553}.
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DR   EMBL; AY089958; AAM09958.1; -; mRNA.
DR   EMBL; AL590450; CAD26054.2; -; Genomic_DNA.
DR   RefSeq; NP_586450.1; NM_001042283.1.
DR   AlphaFoldDB; Q8MTP3; -.
DR   SMR; Q8MTP3; -.
DR   GeneID; 860104; -.
DR   KEGG; ecu:ECU11_1440; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1440; -.
DR   HOGENOM; CLU_257808_0_0_1; -.
DR   InParanoid; Q8MTP3; -.
DR   OrthoDB; 147349at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0044099; C:polar tube; IDA:CACAO.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Signal; Sporulation.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..1256
FT                   /note="Polar tube protein 3"
FT                   /id="PRO_0000022183"
FT   REGION          18..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        606
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1094
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1256 AA;  136225 MW;  378E7E0D3A7490DA CRC64;
     MLLFLLCLYS MVARGDLGSR SSSHAVHHHH SKEGKNASGM DYGNRSTRNA RVKVRLHNHN
     DDSQDGHHHH KVHRSHGGSI KPHNQKHAKL IRNMIGTHEN DPENLTHEEK DLANMAAHGN
     LDALDMLYRN GSITPDVAES VGGSIPGGIT EPVVIQPAES SPMEVNEEAR VVDTMSPPDY
     SDPTGVYVSN GVATGRTNEE QAEINVLNRN ENPIDDGIAE EAYSSLLSVG HSLPVAKAVA
     DEIKDANVRK MLRTKRAYDI SQPPVNPVYI PQAELARATN SKDVVSDTDR QMFMKKVFEE
     YIRQGAPVER ANFEAGQAGF LIDEYNENLA SGLSPDAAYE KAMSLVDLNY QHATRAAAIA
     GGGQVAAQNA ADRSLIEETS ANEMVKTPSG LRPEVLKKKE EAINSKKLDR AQDLSSYLTK
     LHIVEPVNRA HQKLSQAAAL KDAASMEGLD NPVVQEKILT DVAASSAEDL AKAHENLENV
     KTQLKPGGRK TNALNFLSKV LTEKAIKDVN QRNEEMQKEA VKAQKEANEN SAVKSAEEHL
     AKAAEQQIIN NEGKSVFSKV LESTGDISEA AKAREEAERA MAETLRHQRE ARKAEVMKML
     GPMGMNSSVK EAVEHMATAH AGLNVVGSDL NELNKKYEEE VAHQSNIEEL LRETATSNLE
     VKEVIPPTTS RVGISEGKIK LPLKGFSNEE PKTEEETIVQ SRQRNRRNQV RNKVIGTPVE
     SGLNVVEMED GYMHISEAAK ALKINKGKVF YPESAKGIME KQKLDTSLLE HKFNTGERAG
     LDKGVGYYEA DASGFTLPLP SPLNPVPTST MTNEEKSLNI GHAFELEIED GELIQTPWIE
     FVKDMRPMVN GRMAHEAEVA AASEMKSRVE EEKKAKNLEG ITTEVYTNPD GSKFVEVSSP
     YGVPEIMTMD QAVESLKSVG SSSVGAVSEE AKKQTPEVPL DMAVTNSVKG SEESFVSSVL
     STIQKIGNGK ALAKRNAFNG KVDGEKAAIV DEYNKELINE HLSPSSTVEA RVRNSIISKA
     ESYARSMGIS TQSFLNMISQ LPDSSIKEMI SYNEAPPSAR KDVAETHFYN QIASILPDSK
     TANTGSVTEM IFNNISTVTH EPNTVGGEIL EQMTVPNLKT IEQVETKKTP TGTTQVSVSV
     PNDPGKIQVL GEVKFKGNPT TTPSSGRRPA SNQAVAPANV VPGPMVPSSG RNPLKPGARL
     PANNGPVSNA PAARIPAGQP DHTMRGFSHS FPNNPQAPGI GATPSPAVGY SGKIAR