PP16A_CUCMA
ID PP16A_CUCMA Reviewed; 150 AA.
AC Q9ZT47;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=16 kDa phloem protein 1;
GN Name=PP16-1;
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Big max; TISSUE=Stem;
RX PubMed=9872750; DOI=10.1126/science.283.5398.94;
RA Xoconostle-Cazares B., Xiang Y., Ruiz-Medrano R., Wang H.-L., Monzer J.,
RA Yoo B.-C., McFarland K.C., Franceschi V.R., Lucas W.J.;
RT "Plant paralog to viral movement protein that potentiates transport of mRNA
RT into the phloem.";
RL Science 283:94-98(1999).
CC -!- FUNCTION: Binds to both sense and antisense RNA. Interacts with
CC mesophyll plasmodesmata to mediate its own cell-to-cell transport and
CC potentiate RNA trafficking. {ECO:0000269|PubMed:9872750}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- TISSUE SPECIFICITY: Sieve elements of leaves, stems, roots and flowers.
CC {ECO:0000269|PubMed:9872750}.
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DR EMBL; AF079170; AAD05496.1; -; mRNA.
DR PIR; T50648; T50648.
DR AlphaFoldDB; Q9ZT47; -.
DR SMR; Q9ZT47; -.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Metal-binding; Reference proteome;
KW RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9872750"
FT CHAIN 2..150
FT /note="16 kDa phloem protein 1"
FT /id="PRO_0000058529"
FT DOMAIN 1..108
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 150 AA; 16588 MW; 51A3F02B9385F027 CRC64;
MGMGMMEVHL ISGKGLQAHD PLNKPIDPYA EINFKGQERM SKVAKNAGPN PLWDEKFKFL
AEYPGSGGDF HILFKVMDHD AIDGDDYIGD VKIDVKNLLA EGVRKGKSEM PPRMYHVLAH
KIHFKGEIEV GVSFKLQGGG GCGGCYPWEN
