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 22-FEB-2023, entry version 44. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF044915; AAC32812.1; -; Genomic_DNA. DR AlphaFoldDB; O76273; -. DR GlyCosmos; O76273; 8 sites, No reported glycans. 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 //