ID A0A0D9YPX0_9ORYZ Unreviewed; 499 AA.
AC A0A0D9YPX0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G10620.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G10620.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G10620.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Seed storage protein. {ECO:0000256|ARBA:ARBA00003839,
CC ECO:0000256|RuleBase:RU003681}.
CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC chain derived from a single precursor and linked by a disulfide bond.
CC {ECO:0000256|ARBA:ARBA00011818, ECO:0000256|RuleBase:RU003681}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000256|ARBA:ARBA00007178, ECO:0000256|RuleBase:RU003681}.
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DR AlphaFoldDB; A0A0D9YPX0; -.
DR STRING; 40148.A0A0D9YPX0; -.
DR EnsemblPlants; OGLUM02G10620.1; OGLUM02G10620.1; OGLUM02G10620.
DR Gramene; OGLUM02G10620.1; OGLUM02G10620.1; OGLUM02G10620.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0048316; P:seed development; IEA:UniProt.
DR CDD; cd02243; cupin_11S_legumin_C; 1.
DR CDD; cd02242; cupin_11S_legumin_N; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR022379; 11S_seedstore_CS.
DR InterPro; IPR006044; 11S_seedstore_pln.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR31189:SF84; GLUTELIN TYPE-B 2; 1.
DR PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1.
DR Pfam; PF00190; Cupin_1; 2.
DR PRINTS; PR00439; 11SGLOBULIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU003681};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Seed storage protein {ECO:0000256|ARBA:ARBA00023129,
KW ECO:0000256|RuleBase:RU003681}; Signal {ECO:0000256|RuleBase:RU003681};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761,
KW ECO:0000256|RuleBase:RU003681}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU003681"
FT CHAIN 25..499
FT /note="Cupin type-1 domain-containing protein"
FT /evidence="ECO:0000256|RuleBase:RU003681"
FT /id="PRO_5007746262"
FT DOMAIN 50..247
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 315..464
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT REGION 467..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 56522 MW; BBA76A59EB11DE8E CRC64;
MASSVFSRFS IYFCVLLLCH GSMAQLFNPS TNPWHSPRQG SFRECRFDRL QAFEPLRKVR
SEAGVTEYFD EKNELFQCTG TFVIRRVIQP QGLLVPRYTN TPGVVYIIQG RGSMGLTFPG
CPATYQQQFQ QFSSQGQSQS QKFRDEHQKI HQFRQGDIVA LPAGVAHWFY NDGDAPVVAV
YVYDVNNNAN QLEPRQKEFL LAGNNNRAQQ QQVYGSSIEQ HSGQNIFSGF GVEMLSEALG
INAVAAKRLQ SQNDQRGEII HVKNGLQLLK PTLTQQQEQA QAQDQYQQVQ YSERQQTSSR
WNGLEENFCT IKARVNIENP SRADSYNPRA GRITSVNSQK FPILNLIQMS ATRVNLYQNA
ILSPFWNVNA HSLVYMIQGR SRVQVVSNFG KTVFDGVLRP GQLLIIPQYY AVLKKAEREG
CQYIAIKTNA NAFVSHLAGK NSVFRALPVD VVANAYRISR EQARSLKNNR GEEHGAFTPR
FQQQYYPGLS NESESETSE
//