ID   ENP1_ENCCU              Reviewed;         357 AA.
AC   Q8SWL3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Spore wall and anchoring disk complex protein EnP1;
DE   AltName: Full=Host cell adhesion protein EnP1;
DE   Flags: Precursor;
GN   Name=EnP1; OrderedLocusNames=ECU01_0820;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
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   SUBCELLULAR LOCATION.
RX   PubMed=16368098; DOI=10.1016/j.ijpara.2005.10.005;
RA   Peuvel-Fanget I., Polonais V., Brosson D., Texier C., Kuhn L., Peyret P.,
RA   Vivares C.P., Delbac F.;
RT   "EnP1 and EnP2, two proteins associated with the Encephalitozoon cuniculi
RT   endospore, the chitin-rich inner layer of the microsporidian spore wall.";
RL   Int. J. Parasitol. 36:309-318(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16469199; DOI=10.1017/s0031182005009777;
RA   Taupin V., Metenier G., Delbac F., Vivares C.P., Prensier G.;
RT   "Expression of two cell wall proteins during the intracellular development
RT   of Encephalitozoon cuniculi: an immunocytochemical and in situ
RT   hybridization study with ultrathin frozen sections.";
RL   Parasitology 132:815-825(2006).
RN   [5]
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   PubMed=17557882; DOI=10.1128/ec.00113-07;
RA   Southern T.R., Jolly C.E., Lester M.E., Hayman J.R.;
RT   "EnP1, a microsporidian spore wall protein that enables spores to adhere to
RT   and infect host cells in vitro.";
RL   Eukaryot. Cell 6:1354-1362(2007).
CC   -!- FUNCTION: Spore wall protein involved in the adhesion to host cells
CC       surface glycoaminoglycans (GAGs). Microsporidian spore adherence is an
CC       integral part of activation and host cell invasion which requires the
CC       extrusion at the spore apex of a very long and coiled structure, the
CC       polar tube, through which the sporoplasm is pushed to enter into the
CC       potential host cell. {ECO:0000269|PubMed:17557882}.
CC   -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:16368098,
CC       ECO:0000269|PubMed:16469199, ECO:0000269|PubMed:17557882}. Spore,
CC       perispore {ECO:0000269|PubMed:16469199}. Note=Localizes also at the
CC       anchoring disk complex which consists of the polar sac and the
CC       anchoring disk, playing a crucial role in the rupture of the spore wall
CC       and the subsequent release of the polar tube following activation.
CC       {ECO:0000269|PubMed:17557882}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during merogony and a large part of
CC       sporogony. {ECO:0000269|PubMed:16469199, ECO:0000269|PubMed:16691553}.
CC   -!- DOMAIN: Heparin-binding motifs (HBMs) are characterized by an XBBXBX or
CC       XBBBXXBX sequence, where X is any neutral amino acid and B is a
CC       positively charged basic amino acid, and are defined as the consensus
CC       sequence necessary for protein-heparin interactions. HBM1 motif is
CC       necessary for spore adherence to host cells.
CC       {ECO:0000269|PubMed:17557882}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=In like a shot - Issue 110
CC       of October 2009;
CC       URL="https://web.expasy.org/spotlight/back_issues/110";
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DR   EMBL; AL391737; CAD24952.1; -; Genomic_DNA.
DR   RefSeq; XP_965917.1; XM_960824.1.
DR   AlphaFoldDB; Q8SWL3; -.
DR   STRING; 284813.Q8SWL3; -.
DR   GlyCosmos; Q8SWL3; 1 site, No reported glycans.
DR   VEuPathDB; MicrosporidiaDB:ECU01_0820; -.
DR   HOGENOM; CLU_715897_0_0_1; -.
DR   InParanoid; Q8SWL3; -.
DR   OMA; PRICKEK; -.
DR   OrthoDB; 1344317at2759; -.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0031160; C:spore wall; IDA:CACAO.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell adhesion; Glycoprotein; Reference proteome; Signal; Sporulation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..357
FT                   /note="Spore wall and anchoring disk complex protein EnP1"
FT                   /id="PRO_0000377523"
FT   MOTIF           150..158
FT                   /note="HBM1"
FT   MOTIF           329..334
FT                   /note="HBM2"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   357 AA;  40584 MW;  ABF93E135E9735B1 CRC64;
     MKLLGFLIVG LSAISALKTK ALHLTCEQEL RPYSAVVDAN CMAFALNGSN IHEAIKYLQA
     MNIKKAYVLY WNDHDLRGTP MVLYDNGALA PFDPYTNTAK YVLCVEACPC PGSKAASVGG
     FQAATSSEKI YVEGSARPAQ CSEVCIEPVE RRPHYKKIVV NPSPSNCIPC EPECYDSSSS
     SECNKKRCKT FPRICKEKCG SRRRGCPRKV EVLKSQKTYT FDIEKYRRRG EVVVRVCSKD
     SKEKFERFIL SRNGEIRGNN NKNCILEPLP KCLRCPGQLH KLKKHIERKV CQEVCMYINA
     KCDIFVLVGD CDFYRVVVND RRRYRNLHLK KVRGHKLREL IKHGLFGVEF GPLDLDR
//