ID   GLP1_MESCR              Reviewed;         233 AA.
AC   P45852;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Germin-like protein;
DE   Flags: Precursor;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=16652997; DOI=10.1104/pp.100.1.537;
RA   Michalowski C.B., Bohnert H.J.;
RT   "Nucleotide sequence of a root-specific transcript encoding a germin-like
RT   protein from the halophyte Mesembryanthemum crystallinum.";
RL   Plant Physiol. 100:537-538(1992).
CC   -!- FUNCTION: May be involved in seed germination.
CC   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in unstressed roots.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; M93041; AAA33030.1; -; mRNA.
DR   PIR; T12426; T12426.
DR   AlphaFoldDB; P45852; -.
DR   SMR; P45852; -.
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; Disulfide bond; Manganese; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..233
FT                   /note="Germin-like protein"
FT                   /id="PRO_0000010837"
FT   DOMAIN          63..215
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..49
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  25112 MW;  183DD4F4402F09A8 CRC64;
     MEAYKMFAFV VLLATTLYQA YATDPTQLQD FCVGVNKPND GLFVNGLFCK DPMEVNPDDF
     LFRGLNMPAN TDNALGFAAT LVTAANLPGL NTLGISVARL DFAPHGLNPP HTHPRATEVF
     VVLEGTFYVG FVTSNLADGG NKLFAKVLNK GDVFVFPQGL IHFQLNIGNY PGVGISGLSS
     QNPGVITIAN AVFGPEHLSQ LMFLLRPSIS MRIWSSFFRI GSQVVAATTS MCS