ID   ENP1_ENCIN              Reviewed;         348 AA.
AC   A7TZU4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   22-FEB-2023, entry version 20.
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;
OS   Encephalitozoon intestinalis (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=58839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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 infection.
CC       {ECO:0000269|PubMed:17557882}.
CC   -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:17557882}. Spore,
CC       perispore {ECO:0000269|PubMed:17557882}. 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   -!- DOMAIN: Heparin-binding motifs (HBM) 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. HBM motifs may be
CC       involved in spore adherence to host cells.
CC       {ECO:0000269|PubMed:17557882}.
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DR   EMBL; EF539266; ABU24317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7TZU4; -.
DR   GlyCosmos; A7TZU4; 3 sites, No reported glycans.
DR   VEuPathDB; MicrosporidiaDB:Eint_010720; -.
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   3: Inferred from homology;
KW   Cell adhesion; Glycoprotein; Signal; Sporulation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..348
FT                   /note="Spore wall and anchoring disk complex protein EnP1"
FT                   /id="PRO_0000377524"
FT   MOTIF           193..198
FT                   /note="HBM1"
FT   MOTIF           248..256
FT                   /note="HBM2"
FT   MOTIF           322..327
FT                   /note="HBM3"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   348 AA;  39101 MW;  13694D713A5FA4A2 CRC64;
     MKLLGLLISA FGAINALKIK ALYLSCDYEL RPYNAVIDSQ CMAFALNGSN IHEAIRYLNA
     MNIDKAYVLY WNDHDLHQNP MVLHKNGALA PFDRYTNTAK HVLCVEACSC PGPQSRPVVC
     PENNGASVSS PCPPCGQGNN TTVCDKVVVN PQPVKPLPAP CTPCAPCESS SSEKSESKEC
     MTFPRICKKK CGPRHGRSPK KVEIVKSQKT YTFDIERYKR RGDVVVRVCS QDCKDKFEKF
     VLTKTGEIRK GKDKKCIPEP LPECLQCPKN LYKLKSGIEA KVCSEVCMYI NSKCEIFVLI
     GDCDFYKVVM NERRRKQSSF HLKKIRGQKL RELIRQGLFG VEFSPLKC
//