ID Q9FWV0_ORYSJ Unreviewed; 147 AA.
AC Q9FWV0; A0A0N7KS00; Q7XD47;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE SubName: Full=Os10g0491801 protein {ECO:0000313|EMBL:BAT11434.1};
DE SubName: Full=Ubiquitin fusion protein, putative, expressed {ECO:0000313|EMBL:AAP54400.1};
GN OrderedLocusNames=LOC_Os10g34990 {ECO:0000313|EMBL:AAP54400.1},
GN Os10g0491801 {ECO:0000313|EMBL:BAT11434.1};
GN ORFNames=OSNPB_100491801 {ECO:0000313|EMBL:BAT11434.1};
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 {ECO:0000313|EMBL:BAT11434.1, ECO:0000313|Proteomes:UP000059680};
RN [1] {ECO:0000313|EMBL:AAP54400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12791992; DOI=10.1126/science.1083523;
RG Rice Chromosome 10 Sequencing Consortium;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2] {ECO:0000313|EMBL:AAP54400.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell C.R., Wing R.A., McCombie W.R., Messing J., Yuan Q., Ouyang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4] {ECO:0000313|EMBL:AAP54400.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAT11434.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23299411; DOI=10.1093/pcp/pcs183;
RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H.,
RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T.,
RA Matsumoto T., Sasaki T., Itoh T.;
RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive
RT database for rice genomics.";
RL Plant Cell Physiol. 54:E6-E6(2013).
RN [6] {ECO:0000313|EMBL:BAT11434.1, ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
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 [7] {ECO:0000313|EMBL:BAT11434.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 40S subunit of the ribosome.
CC {ECO:0000256|ARBA:ARBA00002225}.
CC -!- SUBUNIT: Part of the 40S ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00035123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; DP000086; AAP54400.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11434.1; -; Genomic_DNA.
DR RefSeq; XP_015614163.1; XM_015758677.1.
DR AlphaFoldDB; Q9FWV0; -.
DR SMR; Q9FWV0; -.
DR STRING; 39947.Q9FWV0; -.
DR PaxDb; 39947-Q9FWV0; -.
DR EnsemblPlants; Os10t0491801-00; Os10t0491801-00; Os10g0491801.
DR GeneID; 107277614; -.
DR Gramene; Os10t0491801-00; Os10t0491801-00; Os10g0491801.
DR KEGG; osa:107277614; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR OMA; IGKWEAT; -.
DR OrthoDB; 5615357at2759; -.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR10666:SF491; POLYUBIQUITIN; 1.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 82..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 16485 MW; E7D5E852B162B9AF CRC64;
MSTVMTQIFV KGLTGKTTAL RMEPSDTVES VKVKLVDKEG LPPDQQPLIF QGHQLDDGHT
LIYYGIQEES TLHLLGRICG GGGGNKKRKK KAYATPKKGK HEHRKEELAV LRHYRVDDVM
GKVERLRLMC PNPECKDVGA LMAKHHD
//
