ID   GLP1_SINAL              Reviewed;         211 AA.
AC   P45854;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Germin-like protein 1;
DE   Flags: Precursor;
GN   Name=GLP1;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=7824658; DOI=10.1104/pp.106.3.905;
RA   Heintzen C., Fischer R., Melzer S., Kappeler S., Apel K., Staiger D.;
RT   "Circadian oscillations of a transcript encoding a germin-like protein that
RT   is associated with cell walls in young leaves of the long-day plant Sinapis
RT   alba L.";
RL   Plant Physiol. 106:905-915(1994).
CC   -!- FUNCTION: May be involved in the maturation of walls of growing cells.
CC   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast.
CC       Secreted, cell wall.
CC   -!- TISSUE SPECIFICITY: Epidermis and spongy parenchyma of young leaves and
CC       epidermis and cortex of stems and petioles.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X84786; CAA59257.1; -; mRNA.
DR   PIR; T10454; T10454.
DR   AlphaFoldDB; P45854; -.
DR   SMR; P45854; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Disulfide bond; Glycoprotein; Manganese;
KW   Metal-binding; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..211
FT                   /note="Germin-like protein 1"
FT                   /id="PRO_0000010839"
FT   DOMAIN          55..201
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..41
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  21998 MW;  9AFB828167D07EC7 CRC64;
     MKMRIQIFFI LSLFSSISFA SVQDFCVADP KGPQNPSGYS CKNPDQVTEN DFAFSGLGKA
     GNTSNVIKAA VTPAFAPAFA GLNGLDVSLA RLDLAGGGVI PLHTHPGASE VLVVIQGTIC
     AGFISSANKV YLKTLSRGDS MVFPQGLLHF QLNSGKGPAL AFVAFGSSSP GLQILPFALF
     ANDLPSELVE ATTFLSDEEV KKLKGVLGGT N