ID   ESR2A_MAIZE             Reviewed;         132 AA.
AC   O24565;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=CLAVATA3/ESR (CLE)-related protein ESR2 {ECO:0000303|PubMed:18034320};
DE            Short=ZmESR2 {ECO:0000303|PubMed:18034320};
DE   AltName: Full=Embryo surrounding region protein 2 {ECO:0000303|PubMed:9263463};
DE   Contains:
DE     RecName: Full=ESR2p {ECO:0000303|PubMed:9263463};
DE   Flags: Precursor;
GN   Name=ESR2 {ECO:0000303|PubMed:18034320};
GN   Synonyms=ESR2g1 {ECO:0000303|PubMed:9263463};
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Leaf;
RX   PubMed=9263463; DOI=10.1046/j.1365-313x.1997.12010235.x;
RA   Opsahl-Ferstad H.G., Le Deunff E., Dumas C., Rogowsky P.M.;
RT   "ZmEsr, a novel endosperm-specific gene expressed in a restricted region
RT   around the maize embryo.";
RL   Plant J. 12:235-246(1997).
RN   [2]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=12096094; DOI=10.1093/jxb/erf010;
RA   Bonello J.-F., Sevilla-Lecoq S., Berne A., Risueno M.-C., Dumas C.,
RA   Rogowsky P.M.;
RT   "Esr proteins are secreted by the cells of the embryo surrounding region.";
RL   J. Exp. Bot. 53:1559-1568(2002).
RN   [3]
RP   REVIEW.
RX   PubMed=18034320; DOI=10.1007/s00018-007-7411-5;
RA   Jun J.H., Fiume E., Fletcher J.C.;
RT   "The CLE family of plant polypeptide signaling molecules.";
RL   Cell. Mol. Life Sci. 65:743-755(2008).
RN   [4]
RP   REVIEW.
RX   PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA   Wang G., Fiers M.;
RT   "CLE peptide signaling during plant development.";
RL   Protoplasma 240:33-43(2010).
CC   -!- FUNCTION: [ESR2p]: Extracellular signal peptide that regulates cell
CC       fate. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [ESR2p]: Secreted, extracellular space
CC       {ECO:0000269|PubMed:12096094}.
CC   -!- TISSUE SPECIFICITY: [ESR2p]: Seed endosperm.
CC       {ECO:0000269|PubMed:12096094, ECO:0000269|PubMed:9263463}.
CC   -!- DEVELOPMENTAL STAGE: [ESR2p]: Expressed specifically in the embryo
CC       surrounding region at the micropylar end of the seed endosperm at early
CC       stages (4 to 7 days after pollination, DAP) and ever-decreasing parts
CC       of the suspensor at subsequent stages (at protein level).
CC       {ECO:0000269|PubMed:12096094, ECO:0000269|PubMed:9263463}.
CC   -!- PTM: [ESR2p]: The O-glycosylation (arabinosylation) of the
CC       hydroxyproline Pro-85 enhances binding affinity of the ESR2p peptide
CC       for its receptor. {ECO:0000250|UniProtKB:O49519}.
CC   -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC       {ECO:0000305}.
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DR   EMBL; X98499; CAA67125.1; -; Genomic_DNA.
DR   PIR; T03280; T03280.
DR   AlphaFoldDB; O24565; -.
DR   PRIDE; O24565; -.
DR   MaizeGDB; 230285; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; O24565; baseline.
DR   GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; ISS:UniProtKB.
DR   GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Glycoprotein; Hydroxylation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..132
FT                   /note="CLAVATA3/ESR (CLE)-related protein ESR2"
FT                   /id="PRO_0000401223"
FT   PEPTIDE         79..90
FT                   /note="ESR2p"
FT                   /evidence="ECO:0000250|UniProtKB:O49519"
FT                   /id="PRO_0000401224"
FT   REGION          68..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         82
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:O49519"
FT   MOD_RES         85
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:O49519"
FT   CARBOHYD        85
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:O49519"
SQ   SEQUENCE   132 AA;  14360 MW;  738E056FBA14656C CRC64;
     MASRMGMVAI VSLFVCALVA STSVNANVWQ TDEDAFYSTN KLGVNGNMEM AQQQSGFIGH
     RPRLASFNRA SKQLDSEKRP VPSGPDPIHH SIPSHAPQHP PSYGKAPYED DRSRASPGLS
     NPIGPPPFLD RY