ID   CRN1_RHIID              Reviewed;         469 AA.
AC   A0A2H5RJD4; A0A386HVI6;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 2.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Crinkler effector protein 1 {ECO:0000303|PubMed:30233541};
DE   Flags: Precursor;
GN   Name=CRN1 {ECO:0000303|PubMed:30233541}; ORFNames=RIR_0600100;
OS   Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS   (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=747089;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, INDUCTION, SUBCELLULAR LOCATION,
RP   SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194;
RX   PubMed=30233541; DOI=10.3389/fmicb.2018.02068;
RA   Voss S., Betz R., Heidt S., Corradi N., Requena N.;
RT   "RiCRN1, a Crinkler effector from the arbuscular mycorrhizal fungus
RT   Rhizophagus irregularis, functions in arbuscule development.";
RL   Front. Microbiol. 9:2068-2068(2018).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194;
RX   PubMed=30271968; DOI=10.1038/s42003-018-0094-7;
RA   Maeda T., Kobayashi Y., Kameoka H., Okuma N., Takeda N., Yamaguchi K.,
RA   Bino T., Shigenobu S., Kawaguchi M.;
RT   "Evidence of non-tandemly repeated rDNAs and their intragenomic
RT   heterogeneity in Rhizophagus irregularis.";
RL   Commun. Biol. 1:87-87(2018).
CC   -!- FUNCTION: Effector that participates in the arbuscule development step
CC       of the symbiosis. Arbuscular mycorrhizal (AM) symbiosis is one of the
CC       most prominent and beneficial plant-microbe interactions that
CC       facilitates mineral nutrition and confers tolerance to biotic and
CC       abiotic stresses (PubMed:30233541). Is not involved in cell death
CC       processes (PubMed:30233541). {ECO:0000269|PubMed:30233541}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30233541}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30233541}. Host
CC       nucleus {ECO:0000269|PubMed:30233541}. Note=Localizes to host nuclear
CC       bodies. {ECO:0000269|PubMed:30233541}.
CC   -!- INDUCTION: Expressed during symbiosis establishment in parallel to host
CC       M.truncatula PT4, the gene coding for an arbuscule-specific phosphate
CC       transporter. {ECO:0000269|PubMed:30233541}.
CC   -!- DOMAIN: The CRN proteins have modular architectures that include a
CC       signal peptide, a conserved N-terminus, and highly diverse C-terminal
CC       domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif,
CC       which is followed by the conserved DWL domain. A highly conserved
CC       HVLVXXP motif marks the end of the CRN N-terminal domains and forms a
CC       junction where diverse C-terminal domains are fused.
CC       {ECO:0000305|PubMed:30233541}.
CC   -!- DISRUPTION PHENOTYPE: Leads to an impairment of the symbiosis in
CC       M.truncatula and to a reduction of host PT4.
CC       {ECO:0000269|PubMed:30233541}.
CC   -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GBC18181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; MH542411; AYD49683.1; -; mRNA.
DR   EMBL; BDIQ01000048; GBC18181.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5RJD4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR045379; Crinkler_N.
DR   Pfam; PF20147; Crinkler; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host nucleus; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..469
FT                   /note="Crinkler effector protein 1"
FT                   /id="PRO_5014184437"
FT   REGION          18..57
FT                   /note="LQLFLAK-like domain"
FT                   /evidence="ECO:0000305|PubMed:30233541"
FT   REGION          58..96
FT                   /note="DWL domain"
FT                   /evidence="ECO:0000305|PubMed:30233541"
FT   MOTIF           97..103
FT                   /note="HVLVXXP motif"
FT                   /evidence="ECO:0000305|PubMed:30233541"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   469 AA;  52673 MW;  D5BD0A84DA3125B2 CRC64;
     MSITLLCLIK GNTLANAFPV DIDKDQLVGH LKKVIKAEQP QTFANVDAKD LKLWRVPISD
     DHDDQLRNLS LEDSDELLAI RKISKYFPDS PPEECIHVLV EPPESTATSE VLKLREEVAS
     LQALLNKSVA FDVVVSPKRT KGFKWTVNIE QATLDGLKEH IRKMEKPPAL ENDGAVLNIV
     NESGKYSPLN DQDLREMLQL FVSNKNLKFT VFIETPSKAF SDWTFSSVCQ LYGLNGETED
     PTMTVFPNFS CGNVKPSQES LEGLMAELKS RLDNTPISLL SVEATKSLYV YSYLLAGANN
     FKGKFEIRPQ KVISGPNGHG PLDFAIDLCQ TAKTVGVTEV KKDDFVKGVA QCAVQLESSL
     SYRKRKADEM EERTFGRVFG IVTDAEKFYF MECSMDDQDR PSFKLSKPVT VVYEDNDLQT
     KVEKVLEHIV WLLEEAQKPD SALDVKEREI KRVRSGELPK VTDLEGKTN