VP8_MAIZE
ID VP8_MAIZE Reviewed; 713 AA.
AC A0A1D6L709; B1PDK9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Probable glutamate carboxypeptidase VP8 {ECO:0000305};
DE EC=3.4.17.21 {ECO:0000305};
DE AltName: Full=Protein VIVIPAROUS8 {ECO:0000303|PubMed:18203869};
DE AltName: Full=Protein WIDOW'S PEAK 1 {ECO:0000303|PubMed:18203869};
GN Name=VP8 {ECO:0000303|PubMed:18203869};
GN Synonyms=WPK1 {ECO:0000303|PubMed:18203869};
GN ORFNames=Zm00001d034383 {ECO:0000305};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=18203869; DOI=10.1104/pp.107.114108;
RA Suzuki M., Latshaw S., Sato Y., Settles A.M., Koch K.E., Hannah L.C.,
RA Kojima M., Sakakibara H., McCarty D.R.;
RT "The maize Viviparous8 locus, encoding a putative ALTERED MERISTEM
RT PROGRAM1-like peptidase, regulates abscisic acid accumulation and
RT coordinates embryo and endosperm development.";
RL Plant Physiol. 146:1193-1206(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
CC -!- FUNCTION: Involved in the regulation of meristem development and seed
CC maturation processes. Mediates regulation of embryonic regulatory genes
CC and genes controlling abscisic acid (ABA) biosynthesis and turnover in
CC developing seeds. May be required for the synthesis of small signaling
CC molecules that integrates meristem and embryo formation in seeds.
CC {ECO:0000269|PubMed:18203869}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Altered meristem development. Altered
CC developmental gene expression in meristem and non-meristem tissues of
CC the embryo. Altered pattern of aleurone differentiation in the
CC abgerminal side of the endosperm. {ECO:0000269|PubMed:18203869}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; EU401893; ACA62934.1; -; mRNA.
DR RefSeq; NP_001120724.1; NM_001127252.1.
DR AlphaFoldDB; A0A1D6L709; -.
DR SMR; A0A1D6L709; -.
DR STRING; 4577.GRMZM2G010353_P01; -.
DR MEROPS; M28.007; -.
DR EnsemblPlants; Zm00001eb060200_T002; Zm00001eb060200_P002; Zm00001eb060200.
DR GeneID; 100147738; -.
DR Gramene; Zm00001eb060200_T002; Zm00001eb060200_P002; Zm00001eb060200.
DR KEGG; zma:100147738; -.
DR eggNOG; KOG2195; Eukaryota.
DR OMA; IEFVSWD; -.
DR OrthoDB; 804230at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; A0A1D6L709; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0009908; P:flower development; IEA:EnsemblPlants.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IEA:EnsemblPlants.
DR GO; GO:0010074; P:maintenance of meristem identity; IMP:UniProtKB.
DR GO; GO:0009640; P:photomorphogenesis; IEA:EnsemblPlants.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010080; P:regulation of floral meristem growth; IEA:EnsemblPlants.
DR GO; GO:0010081; P:regulation of inflorescence meristem growth; IEA:EnsemblPlants.
DR GO; GO:0010082; P:regulation of root meristem growth; IEA:EnsemblPlants.
DR GO; GO:2000034; P:regulation of seed maturation; IMP:UniProtKB.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Glycoprotein; Growth regulation;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..713
FT /note="Probable glutamate carboxypeptidase VP8"
FT /id="PRO_0000439196"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..713
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 245..539
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 25
FT /note="L -> I (in Ref. 1; ACA62934)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="S -> G (in Ref. 1; ACA62934)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> V (in Ref. 1; ACA62934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 77451 MW; 7C44A4C43C69FEA7 CRC64;
MPHSVLARLP PGSVRLVAAF GLLLLVSLLV LHRRPGRPHV AAAAASDRLT DPSRSRLFLS
QSPGANASIA ADLRALTAGP HLAGTPASAG AAAHVLARLR AAGLQTLTRE YEPLLSYPGH
ASLALLRPDG SLLARLSLEE PADEGRRVVP PYHAYAPSGG AVAEAVFVNL GREEDYVVLE
RLGVGVRGRV AVARRGGGYR GGVVARAADK GAVAVLIAGN ADGGVERGVV LLGGPGDPLT
PGWAATSGAE RLKFDDKAVK QRFPSIPSMP VSAKTAAAII RSLGGPAIPA EWKDGLGVDT
GGLGPGPTLV NFTYQEDRKF YKIRDIFGII KGQEEPDRYV ILGNHRDAWT YGAVDPNSGT
AALLDIARRL GIMLQSGWKP RRSIILCSWD GEEFGMIGST EWVEDNLEDL HSKAVAYLNV
DCAVQGVGFF AGSTPQLDKL LVDITRQVRD PDVTGKMVHD TWNEMSGGIK IERLARTDSD
FAPFLHHAGI PSVDLYYGEE FPGYHTALDT YNWMEKHGDP FFLRHLAITE IWGLLALRLA
NDPVLPFDYQ AYTSQLQEHI KTLSALTSNG HAVNLMNGCV NDLSGAAMEV LKEMKKLQQM
DLYDEHARMR RRLLNDRLLL AERSFLQPEG LQGRGWFKHL LYSPPEDYES KLSFFPGIAD
AISRSANLSD KEQEVAMQHE VWKVCRAIQR AASVLRGEFS EQKPTNFSSL VTP
