ID   PHSA_PHAVU              Reviewed;         436 AA.
AC   P07219;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Phaseolin, alpha-type;
DE   Flags: Precursor;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tendergreen; TISSUE=Cotyledon;
RX   PubMed=2997710; DOI=10.1093/nar/13.18.6483;
RA   Slightom J.L., Drong R.F., Klassy R.C., Hoffman L.M.;
RT   "Nucleotide sequences from phaseolin cDNA clones: the major storage
RT   proteins from Phaseolus vulgaris are encoded by two unique gene families.";
RL   Nucleic Acids Res. 13:6483-6498(1985).
RN   [2]
RP   GLYCOSYLATION AT ASN-258 AND ASN-347, AND STRUCTURE OF CARBOHYDRATES.
RX   PubMed=3654619; DOI=10.1016/s0021-9258(19)76439-4;
RA   Sturm A., Van Kuik J.A., Vliegenthart J.F.G., Chrispeels M.J.;
RT   "Structure, position, and biosynthesis of the high mannose and the complex
RT   oligosaccharide side chains of the bean storage protein phaseolin.";
RL   J. Biol. Chem. 262:13392-13403(1987).
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   -!- PTM: N-glycosylated; glycans consist in Man9(GlcNAc)2 and Man7(GlcNAc)2
CC       when dually glycosylated at Asn-258 and Asn-347, whereas it consists in
CC       Xyl-Man3(GlcNAc)2 when solely glycosylated at Asn-258.
CC       {ECO:0000269|PubMed:3654619}.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000305}.
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DR   EMBL; X02980; CAA26718.1; -; mRNA.
DR   PIR; A23498; A23498.
DR   AlphaFoldDB; P07219; -.
DR   SMR; P07219; -.
DR   STRING; 3885.XP_007143287.1; -.
DR   Allergome; 8837; Pha v Phaseolin.
DR   GlyConnect; 493; 2 N-Linked glycans (2 sites).
DR   iPTMnet; P07219; -.
DR   EnsemblPlants; ESW15282; ESW15282; PHAVU_007G0597000g.
DR   Gramene; ESW15282; ESW15282; PHAVU_007G0597000g.
DR   eggNOG; ENOG502QQEP; Eukaryota.
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; 1.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 2.
PE   1: Evidence at protein level;
KW   Glycoprotein; Seed storage protein; Signal; Storage protein; Vacuole.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..436
FT                   /note="Phaseolin, alpha-type"
FT                   /id="PRO_0000032194"
FT   DOMAIN          245..396
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   REGION          233..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) (complex) asparagine;
FT                   alternate"
FT                   /evidence="ECO:0000269|PubMed:3654619"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT                   alternate"
FT                   /evidence="ECO:0000269|PubMed:3654619"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3654619"
FT                   /id="CAR_000077"
SQ   SEQUENCE   436 AA;  49271 MW;  1053C16FE37F9574 CRC64;
     MMRARVPLLL LGILFLASLS ASFATSLREE EESQDNPFYF NSDNSWNTLF KNQYGHIRVL
     QRFDQQSKRL QNLEDYRLVE FRSKPETLLL PQQADAELLL VVRSGSAILV LVKPDDRREY
     FFLTQGDNPI FSDNQKIPAG TIFYLVNPDP KEDLRIIQLA MPVNNPQIHE FFLSSTEAQQ
     SYLQEFSKHI LEASFNSKFE EINRVLFEEE GQQEEGQQEG VIVNIDSEQI EELSKHAKSS
     SRKSHSKQDN TIGNEFGNLT ERTDNSLNVL ISSIEMKEGA LFVPHYYSKA IVILVVNEGE
     AHVELVGPKG NKETLEFESY RAELSKDDVF VIPAAYPVAI KATSNVNFTG FGINANNNNR
     NLLAGKTDNV ISSIGRALDG KDVLGLTFSG SGEEVMKLIN KQSGSYFVDG HHHQQEQQKG
     SHQQEQQKGR KGAFVY