VCLB_PEA
ID VCLB_PEA Reviewed; 410 AA.
AC P02854;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Provicilin;
DE AltName: Full=Type B;
DE Flags: Precursor; Fragment;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE (CLONES PDUB7 AND PDUB4), AND GLYCOSYLATION AT ASN-359.
RC STRAIN=cv. Feltham First;
RX PubMed=6687941; DOI=10.1093/nar/11.8.2367;
RA Lycett G.W., Delauney A.J., Gatehouse J.A., Gilroy J., Croy R.R.D.,
RA Boulter D.;
RT "The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding
RT sequence for preprovicilin.";
RL Nucleic Acids Res. 11:2367-2380(1983).
CC -!- FUNCTION: Seed storage protein.
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 PIR; A03344; FWPMVB.
DR AlphaFoldDB; P02854; -.
DR SMR; P02854; -.
DR Allergome; 947; Pis s 1.
DR iPTMnet; P02854; -.
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 Glycoprotein; Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..15
FT CHAIN 16..>410
FT /note="Provicilin"
FT /id="PRO_0000032182"
FT DOMAIN 23..181
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 241..409
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 223..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 221..222
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6687941"
FT NON_TER 410
SQ SEQUENCE 410 AA; 46385 MW; 8AF68CE85A316FA2 CRC64;
MLLAIAFLAS VCVSSRSDQE NPFIFKSNRF QTLYENENGH IRLLQKFDKR SKIFENLQNY
RLLEYKSKPH TLFLPQYTDA DFILVVLSGK ATLTVLKSND RNSFNLERGD AIKLPAGSIA
YFANRDDNEE PRVLDLAIPV NKPGQLQSFL LSGTQNQKSS LSGFSKNILE AAFNTNYEEI
EKVLLEQQEQ EPQHRRSLKD RRQEINEENV IVKVSRDQIE ELSKNAKSSS KKSVSSESGP
FNLRSRNPIY SNKFGKFFEI TPEKNQQLQD LDIFVNSVDI KVGSLLLPNY NSRAIVIVTV
TEGKGDFELV GQRNENQGKE NDKEEEQEEE TSKQVQLYRA KLSPGDVFVI PAGHPVAINA
SSDLNLIGLG INAENNERNF LAGEEDNVIS QVERPVKELA FPGSSHEVDR