PHS2_PHALU
ID PHS2_PHALU Reviewed; 423 AA.
AC Q43617;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Phaseolin;
DE Flags: Precursor; Fragment;
GN Name=PHS;
OS Phaseolus lunatus (Lima bean) (Phaseolus limensis).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3884;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Henderson; TISSUE=Cotyledon;
RX PubMed=8001810; DOI=10.1139/g94-107;
RA Kami J.A., Gepts P.;
RT "Phaseolin nucleotide sequence diversity in Phaseolus. I. Intraspecific
RT diversity in Phaseolus vulgaris.";
RL Genome 37:751-757(1994).
CC -!- FUNCTION: Major seed storage protein.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000250}. Vacuole
CC {ECO:0000250}. Note=Cotyledonary membrane-bound vacuolar protein
CC bodies. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; U01122; AAA99533.1; -; mRNA.
DR AlphaFoldDB; Q43617; -.
DR SMR; Q43617; -.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 2: Evidence at transcript level;
KW Glycoprotein; Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL <1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..423
FT /note="Phaseolin"
FT /id="PRO_0000032193"
FT DOMAIN 35..193
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 228..383
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 423 AA; 47514 MW; E0383563B4141FEE CRC64;
RRVPLLLLGI LFLASLSASF AISLREHNES QDNPFYFSSD NSWQTLFKNQ YGHIRVLQRF
DQRSERLQNL EDYRLVEFMS KPETLLLPQQ ADAEFLLVVR SGSALLALVK PGGTIIYSLK
QQDTLKIPAG TIFFLINPEN NEDLRIIKLA MTVNNPQIQD FFLSSTEAQQ SYLYGFSKHI
LDASFNSPIE KINRLLFAEE GRQEGVIVNI GSDLIQELSR HAKSSSRKSL DHNSLDISNE
WGNLTDIVYN SLDVLLTYVE IKEGGLFVPH YNSKAIVILV VEEGVAKVEL VGPKREKESL
ELETYRADVS EGDVFVIPAA FPFAIKAISN VNFTSFGINA NNNYRIFLTG KGGPTGKEDN
IISAGINPDV LGLMFPGSGE DVQKLFNNQN LSHFVNGSYH KNAHPHEQEQ QKQQKGRKGA
FVY
