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CIP73_LOTJA
ID   CIP73_LOTJA             Reviewed;         691 AA.
AC   D5LXJ0;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Ubiquitin-like domain-containing protein CIP73 {ECO:0000305};
DE   AltName: Full=CCaMK-interacting protein of approximately 73 kDa {ECO:0000303|PubMed:21209278};
GN   Name=CIP73 {ECO:0000303|PubMed:21209278};
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305 {ECO:0000312|EMBL:ADE96995.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCAMK, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX   PubMed=21209278; DOI=10.1104/pp.110.167965;
RA   Kang H., Zhu H., Chu X., Yang Z., Yuan S., Yu D., Wang C., Hong Z.,
RA   Zhang Z.;
RT   "A novel interaction between CCaMK and a protein containing the Scythe_N
RT   ubiquitin-like domain in Lotus japonicus.";
RL   Plant Physiol. 155:1312-1324(2011).
CC   -!- FUNCTION: Involved in root nodulation. Required for root nodule
CC       organogenesis after infection by symbiotic rhizobia. Probably not
CC       involved in arbuscular mycorrhizal (AM) symbiosis. Acts downstream of
CC       CCAMK. {ECO:0000269|PubMed:21209278}.
CC   -!- SUBUNIT: Interacts with CCAMK. {ECO:0000269|PubMed:21209278}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21209278}.
CC   -!- TISSUE SPECIFICITY: Highly epressed in roots. Expressed at very low
CC       levels in leaves and stems. {ECO:0000269|PubMed:21209278}.
CC   -!- PTM: Phosphorylated at the N-terminus by CCAMK.
CC       {ECO:0000269|PubMed:21209278}.
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DR   EMBL; GU980966; ADE96995.1; -; mRNA.
DR   AlphaFoldDB; D5LXJ0; -.
DR   SMR; D5LXJ0; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Nodulation; Nucleus.
FT   CHAIN           1..691
FT                   /note="Ubiquitin-like domain-containing protein CIP73"
FT                   /id="PRO_0000444705"
FT   DOMAIN          22..97
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          92..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  73080 MW;  EAF4660DF3DBDF91 CRC64;
     MGSNGTEEIT SDISTGNAAT TIEIKIKMLD SQTFTLRVDK QMPVPALKAQ IESLTGVMSE
     RQRLICQGKV LKDDQLLSAY HVEDGHTLHL VARHPDLTPP GSLPNHSATE PNSSTGHGYS
     NQVAPGVFIE TFNVPVQGDG VPSEINRIVS AVLGSMGLPN FASGGEGIFV REHDSTGLGR
     TSDFTGNPSR PQPEQAGFRI SSDSSRNSFG FPAAVSLGSL GSLQPPVIPD SLTTLLQYLS
     HINHEFDTIA REGGNNVQAA EAHRNEERGF VSSRLSSTPE GLSSPASLAE VLLSTRRVII
     EQAGECLLQL ARQLENHADI ADPLSRSSTQ SRALRTGVMF YNLGAYLLEL GRTTMTLRLG
     QTPSEAVVNG GPAVFISPSG PNHIMVQPLP FQPGASFGAI PVGAAQSNSS LGGGLGSSFF
     PRRIDIQIRR GASTTPGTNQ EEHGDTQSAS VQRNTGESSV NQTTSRRPDA SIAGEPGVRV
     VPIRTMVAAV PVLGRFQSSV NTNNEQGSQP ASQQHTAPHS TAEFTLHRQS MEDSARNGTL
     PTPNTQQEPS SSRVVNINIL SAGGPENNES ERQVPSSVLQ FLRALFPGGE IHVEDPSSQG
     TTAGVTSAAT SSGAAQAPEA EPNVSEEGIF LSNLLRGIMP VISQHIGRGG DSSEDQVTRD
     PSTQVEIGAG TSRRQSDSES SPPNSKRQKM E
 
 
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