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Database: UniProt
Entry: P15590
LinkDB: P15590
Original site: P15590 
ID   GLB1_MAIZE              Reviewed;         573 AA.
AC   P15590;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Globulin-1 S allele;
DE            Short=GLB1-S;
DE   AltName: Full=7S-like;
DE   Flags: Precursor;
GN   Name=GLB1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Va26;
RX   PubMed=16667080; DOI=10.1104/pp.91.2.636;
RA   Belanger F.C., Kriz A.L.;
RT   "Molecular characterization of the major maize embryo globulin encoded by
RT   the Glb1 gene.";
RL   Plant Physiol. 91:636-643(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 87-100.
RX   PubMed=2775172; DOI=10.1007/bf02401804;
RA   Kriz A.L.;
RT   "Characterization of embryo globulins encoded by the maize Glb genes.";
RL   Biochem. Genet. 27:239-251(1989).
CC   -!- PTM: Three protein-processing steps occur in the formation of the
CC       mature protein from the primary translation product.
CC   -!- POLYMORPHISM: The three most commonly occurring GLB1 alleles have the
CC       designation L, I, and S for large, intermediate, and small proteins,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000305}.
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DR   EMBL; M24845; AAA33467.1; -; mRNA.
DR   AlphaFoldDB; P15590; -.
DR   SMR; P15590; -.
DR   STRING; 4577.P15590; -.
DR   GlyCosmos; P15590; 1 site, No reported glycans.
DR   PaxDb; 4577-GRMZM2G067919_P02; -.
DR   MaizeGDB; 30181; -.
DR   eggNOG; ENOG502QQEP; Eukaryota.
DR   InParanoid; P15590; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P15590; baseline and differential.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd02245; cupin_7S_vicilin-like_C; 1.
DR   CDD; cd02244; cupin_7S_vicilin-like_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR31189:SF82; 63 KDA GLOBULIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC-like cupins; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Reference proteome;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..18
FT                   /note="Or 21"
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..86
FT                   /evidence="ECO:0000269|PubMed:2775172"
FT                   /id="PRO_0000032178"
FT   CHAIN           87..573
FT                   /note="Globulin-1 S allele"
FT                   /id="PRO_0000032179"
FT   DOMAIN          104..262
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          311..493
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          65..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   573 AA;  65029 MW;  525ED1D00A062976 CRC64;
     MVSARIVVLL AVLLCAAAAV ASSWEDDNHH HHGGHKSGRC VRRCEDRPWH QRPRCLEQCR
     EEEREKRQER SRHEADDRSG EGSSEDERER EQEKEEKQKD RRPYVFDRRS FRRVVRSEQG
     SLRVLRPFDE VSRLLRGIRD YRVAVLEANP RSFVVPSHTD AHCIGYVAEG EGVVTTIENG
     ERRSYTIKQG HVFVAPAGAV TYLANTDGRK KLVITKILHT ISVPGEFQFF FGPGGRNPES
     FLSSFSKSIQ RAAYKTSSDR LERLFGRHGQ DKGIIVRATE EQTRELRRHA SEGGHGPHWP
     LPPFGESRGP YSLLDQRPSI ANQHGQLYEA DARSFHDLAE HDVSVSFANI TAGSMSAPLY
     NTRSFKIAYV PNGKGYAEIV CPHRQSQGGE SERERGKGRR SEEEEESSEE QEEVGQGYHT
     IRARLSPGTA FVVPAGHPFV AVASRDSNLQ IVCFEVHADR NEKVFLAGAD NVLQKLDRVA
     KALSFASKAE EVDEVLGSRR EKGFLPGPKE SGGHEEREQE EEEREERHGG RGERERHGRE
     EREKEEEERE GRHGRGRREE VAETLLRMVT ARM
//
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