ID   SKP5_ORYSJ              Reviewed;         165 AA.
AC   Q6H4D6;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=SKP1-like protein 5 {ECO:0000303|PubMed:24616269};
DE   AltName: Full=SKP1-like 5 {ECO:0000305};
GN   Name=SKP5 {ECO:0000305}; Synonyms=OSK5 {ECO:0000303|PubMed:24616269};
GN   OrderedLocusNames=Os09g0274700 {ECO:0000312|EMBL:BAT07190.1},
GN   LOC_Os09g10260 {ECO:0000305};
GN   ORFNames=OJ1031_C12.36 {ECO:0000312|EMBL:BAD25948.1},
GN   OsJ_28634 {ECO:0000312|EMBL:EAZ44010.1},
GN   OSJNBb0012I09.3 {ECO:0000312|EMBL:BAD26413.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [4]
RP   INTERACTION WITH D3.
RX   PubMed=24616269; DOI=10.1093/pcp/pcu045;
RA   Zhao J., Wang T., Wang M., Liu Y., Yuan S., Gao Y., Yin L., Sun W.,
RA   Peng L., Zhang W., Wan J., Li X.;
RT   "DWARF3 participates in an SCF complex and associates with DWARF14 to
RT   suppress rice shoot branching.";
RL   Plant Cell Physiol. 55:1096-1109(2014).
RN   [5]
RP   INTERACTION WITH VIRUS P7-2 PROTEIN.
RX   PubMed=28494021; DOI=10.1371/journal.pone.0177518;
RA   Tao T., Zhou C.J., Wang Q., Chen X.R., Sun Q., Zhao T.Y., Ye J.C., Wang Y.,
RA   Zhang Z.Y., Zhang Y.L., Guo Z.J., Wang X.B., Li D.W., Yu J.L., Han C.G.;
RT   "Rice black streaked dwarf virus P7-2 forms a SCF complex through binding
RT   to Oryza sativa SKP1-like proteins, and interacts with GID2 involved in the
RT   gibberellin pathway.";
RL   PLoS ONE 12:E0177518-E0177518(2017).
CC   -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC       degradation of target proteins. Together with CUL1, a RING-box and a F-
CC       box protein, it forms a SCF E3 ubiquitin ligase complex. The functional
CC       specificity of this complex depends on the type of F-box protein. In
CC       the SCF complex, it serves as an adapter that links the F-box protein
CC       to CUL1. {ECO:0000250|UniProtKB:Q9FHW7}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9FHW7}.
CC   -!- SUBUNIT: Part of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
CC       ligase complex (By similarity). Interacts with rice black streaked
CC       dwarf virus RBSDV protein P7-2 (PubMed:28494021). Is able to form the
CC       SCF complex together with CUL1 and the viral P7-2 protein (By
CC       similarity). Interacts with D3 (PubMed:24616269).
CC       {ECO:0000250|UniProtKB:Q6PL11, ECO:0000269|PubMed:24616269,
CC       ECO:0000269|PubMed:28494021}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9FHW7}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; AP005547; BAD25948.1; -; Genomic_DNA.
DR   EMBL; AP005878; BAD26413.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT07190.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ44010.1; -; Genomic_DNA.
DR   RefSeq; XP_015611431.1; XM_015755945.1.
DR   AlphaFoldDB; Q6H4D6; -.
DR   SMR; Q6H4D6; -.
DR   STRING; 4530.OS09T0273800-01; -.
DR   PaxDb; Q6H4D6; -.
DR   PRIDE; Q6H4D6; -.
DR   GeneID; 107275506; -.
DR   KEGG; osa:107275506; -.
DR   InParanoid; Q6H4D6; -.
DR   OrthoDB; 1412723at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR016897; SKP1.
DR   InterPro; IPR001232; SKP1-like.
DR   InterPro; IPR036296; SKP1-like_dim_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR016072; Skp1_comp_dimer.
DR   InterPro; IPR016073; Skp1_comp_POZ.
DR   PANTHER; PTHR11165; PTHR11165; 1.
DR   Pfam; PF01466; Skp1; 1.
DR   Pfam; PF03931; Skp1_POZ; 1.
DR   PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR   SMART; SM00512; Skp1; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF81382; SSF81382; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..165
FT                   /note="SKP1-like protein 5"
FT                   /id="PRO_0000446884"
FT   REGION          106..164
FT                   /note="Interaction with the F-box domain of F-box proteins"
FT                   /evidence="ECO:0000250|UniProtKB:Q39255"
SQ   SEQUENCE   165 AA;  18009 MW;  46AC3DBDA8BA1A18 CRC64;
     MAAVKEGADA GDSKILLISS DGQHFQVTEA EASMSKLVSN MIEDGCTENG VPLPNVASNV
     LAKVLEYCKK HAAAAAAEDV AVKDQELKSF DASFIDVDNT MLFNLILAAN YLNVPSLLDL
     ACQHTADLIK GKTVQEIRDM FGIVNDFTPE EEEEIRKENE WAFEN