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