CCLOP_PEA
ID CCLOP_PEA Reviewed; 513 AA.
AC A9XMT4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Protein CYCLOPS {ECO:0000303|PubMed:19074278};
DE Short=PsCYCLOPS {ECO:0000303|PubMed:19074278};
DE AltName: Full=Protein IPD3 homolog {ECO:0000303|PubMed:21787150};
DE Short=PsIPD3 {ECO:0000303|PubMed:21787150};
DE AltName: Full=PsSYM33 {ECO:0000303|PubMed:21787150};
GN Name=IPD3 {ECO:0000303|PubMed:21787150};
GN Synonyms=SYM33 {ECO:0000303|PubMed:9790580};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19074278; DOI=10.1073/pnas.0806858105;
RA Yano K., Yoshida S., Mueller J., Singh S., Banba M., Vickers K.,
RA Markmann K., White C., Schuller B., Sato S., Asamizu E., Tabata S.,
RA Murooka Y., Perry J., Wang T.L., Kawaguchi M., Imaizumi-Anraku H.,
RA Hayashi M., Parniske M.;
RT "CYCLOPS, a mediator of symbiotic intracellular accommodation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20540-20545(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9790580; DOI=10.1007/s004380050840;
RA Tsyganov V.E., Morzhina E.V., Stefanov S.Y., Borisov A.Y., Lebsky V.K.,
RA Tikhonovich I.A.;
RT "The pea (Pisum sativum L.) genes sym33 and sym40 control infection thread
RT formation and root nodule function.";
RL Mol. Gen. Genet. 259:491-503(1998).
RN [3]
RP FUNCTION.
RX PubMed=12634913; DOI=10.1007/s00572-002-0188-3;
RA Jacobi L.M., Petrova O.S., Tsyganov V.E., Borisov A.Y., Tikhonovich I.A.;
RT "Effect of mutations in the pea genes Sym33 and Sym40. I. Arbuscular
RT mycorrhiza formation and function.";
RL Mycorrhiza 13:3-7(2003).
RN [4]
RP FUNCTION.
RX PubMed=12634914; DOI=10.1007/s00572-002-0189-2;
RA Jacobi L.M., Zubkova L.A., Barmicheva E.M., Tsyganov V.E., Borisov A.Y.,
RA Tikhonovich I.A.;
RT "Effect of mutations in the pea genes Sym33 and Sym40. II. Dynamics of
RT arbuscule development and turnover.";
RL Mycorrhiza 13:9-16(2003).
RN [5]
RP FUNCTION.
RX PubMed=21787150; DOI=10.1094/mpmi-01-11-0013;
RA Ovchinnikova E., Journet E.P., Chabaud M., Cosson V., Ratet P., Duc G.,
RA Fedorova E., Liu W., den Camp R.O., Zhukov V., Tikhonovich I., Borisov A.,
RA Bisseling T., Limpens E.;
RT "IPD3 controls the formation of nitrogen-fixing symbiosomes in pea and
RT Medicago Spp.";
RL Mol. Plant Microbe Interact. 24:1333-1344(2011).
CC -!- FUNCTION: Involved symbiotic signaling. Required for root infection by
CC symbiotic rhizobia, infection thread (IT) formation, and nodule
CC development (PubMed:9790580). Required for symbiosome formation (i.e.
CC the release of the bacteria from the ITs) and subsequent symbiosome
CC development (PubMed:21787150). Involved in arbuscular mycorrhizal (AM)
CC symbiosis (PubMed:12634913, PubMed:12634914).
CC {ECO:0000269|PubMed:12634913, ECO:0000269|PubMed:12634914,
CC ECO:0000269|PubMed:21787150, ECO:0000269|PubMed:9790580}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A7TUE1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but roots of mutant plants are impaired in the interaction
CC with rhizobia, specifically in infection thread (IT) formation in
CC symbiotic roots. {ECO:0000269|PubMed:9790580}.
CC -!- SIMILARITY: Belongs to the CYCLOPS family. {ECO:0000305}.
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DR EMBL; EF569222; ABU63669.1; -; mRNA.
DR AlphaFoldDB; A9XMT4; -.
DR SMR; A9XMT4; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR InterPro; IPR040036; CYCLOPS.
DR PANTHER; PTHR36890; PTHR36890; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Nodulation; Nucleus.
FT CHAIN 1..513
FT /note="Protein CYCLOPS"
FT /id="PRO_0000444704"
FT REGION 327..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..513
FT /evidence="ECO:0000255"
FT MOTIF 397..401
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 421..424
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 327..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57721 MW; B87D218F83057DBF CRC64;
MEGRGFSGLY KNSSEELFLK TVMESPIGMP VPTMEMLGFK TVSQSFRADS EELFKRWLTN
EEGYNSTSMG LNSRLSKRIS TELVNVSNQQ HVGVASEGRN NDKSCLQNSF LTNDVSGDFN
FPIREPVDRE LQSGNLFLAK AWFLTDQRMT RSRSSELRRR YTEMQNTQAP QGLDSMFMAP
KHDANIIKEE LAHFNGFDYL SMCEIPSQKG SFMSPSNSSS STFNTQQLVD VDKVSSCVSM
LKGTLQRKRL ECQVEKDAAE DGLNEIFGIR EPLFQSGFNE GQENWNHQKL VNVQGDFTDQ
VKDTGVIETL EGAANFVLEG FANQTSQIHG GTASGEPSQS ESSAAAPVIS SGLDACEGPS
NSSQTLCDSS WKQVGESTQN RAKGVREQIM DNLKDDRKRK RLERYGSVTS AVSDDKVDTT
KKRRVERSRK MAEAKERNLT PTIPSDMQAV MKRCENLEKE VRSLKLNLSF MNRKDSEQTK
QIEDLQKQNE ELADEKERLL EEIERLLSET GKI