PHS1_PHALU
ID PHS1_PHALU Reviewed; 428 AA.
AC P80463; Q40913;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Phaseolin;
DE Flags: Precursor;
GN Name=PHA;
GN and
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. G25804; 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).
RN [2]
RP PROTEIN SEQUENCE OF 25-44 AND 237-252.
RC TISSUE=Cotyledon;
RX PubMed=8547338; DOI=10.1016/0167-4838(95)00176-x;
RA Sparvoli F., Daminati M.G., Lioi L., Bollini R.;
RT "In vivo endoproteolytically cleaved phaseolin is stable and accumulates in
RT developing Phaseolus lunatus L. seeds.";
RL Biochim. Biophys. Acta 1292:15-22(1996).
CC -!- FUNCTION: Major seed storage protein.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain. Vacuole.
CC Note=Cotyledonary membrane-bound vacuolar protein bodies.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; U01121; AAA99532.1; -; mRNA.
DR AlphaFoldDB; P80463; -.
DR SMR; P80463; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Seed storage protein; Signal;
KW Storage protein; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8547338"
FT CHAIN 25..428
FT /note="Phaseolin"
FT /id="PRO_0000032192"
FT DOMAIN 38..196
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 231..386
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 399..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 239
FT /note="D -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47956 MW; 9F72BA8556B0AB81 CRC64;
MMRARVPLLL LGILFLASLS ASFAISLREH NESQDNPFYF SSDNSWQTLF KNQYGHIRVL
QSFDQHSERL QNLEDYRLVE FMSKPETLLL PQQADAEFLL VVRSGSALLA LVKPGGTIIY
SLKQQDTLKI PAGTIFFLIN PQNNEDLRII KLAMTVNNPQ IQDFFLSSTE AQQSYLYGFR
KDILDASFNS PIEEINRLLF AEEGRQEGVI VNIGSDLIQE LSRHAKSSSR KSLDHNSLDI
SNEWGNLTDI VYNSLDVLLT YVEIKEGGLF VPHYNSKAIV ILVVEEGVAK VELVGPKREK
ESLELETYRA DVSEGDVFVI PAAYPVAIKA ISNVNFTSFG INANNNYRIL LTGKGGPTGK
EDNIISAGIN PDVLGLMFPG SGEDVQKLFN NQNLSHFVNG SYHKNAQPQP HEQEQQKQQK
GRKGAFVY
