ENP1_ENCCU
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 03-AUG-2022, entry version 63.
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 PRIDE; Q8SWL3; -.
DR GeneID; 860258; -.
DR KEGG; ecu:ECU01_0820; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0820; -.
DR HOGENOM; CLU_715897_0_0_1; -.
DR InParanoid; Q8SWL3; -.
DR OrthoDB; 1164865at2759; -.
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
