GLP1_IPONI
ID GLP1_IPONI Reviewed; 214 AA.
AC P45853;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Germin-like protein;
DE Flags: Precursor;
GN Name=GLP;
OS Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=35883;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Choisy; TISSUE=Cotyledon;
RX PubMed=8888623; DOI=10.1093/oxfordjournals.pcp.a029022;
RA Ono M., Sage-Ono K., Inoue M., Kamada H., Harada H.;
RT "Transient increase in the level of mRNA for a germin-like protein in
RT leaves of the short-day plant Pharbitis nil during the photoperiodic
RT induction of flowering.";
RL Plant Cell Physiol. 37:855-861(1996).
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: Cotyledons and leaves.
CC -!- DEVELOPMENTAL STAGE: Increased transiently during flower induction.
CC -!- INDUCTION: Expressed with a circadian rhythm, with peak expression 10
CC hours from the beginning of the night.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; D45425; BAA08266.1; -; mRNA.
DR AlphaFoldDB; P45853; -.
DR SMR; P45853; -.
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..214
FT /note="Germin-like protein"
FT /id="PRO_0000010838"
FT DOMAIN 58..204
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 108
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 DISULFID 28..44
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 22608 MW; 2BF187AA8CCAC4AC CRC64;
MVMMRIFFFL FLLAFPVFTA NASVNDFCVA NGPGARDTPS GFVCKNTAKV TAADFVYSGL
AKPGNTTNII NAAVTPAFVG QFPGVIGLGV TLARLDLAPG GVIPMHTHPG ASEILNVVEG
TILAAFISSG NKVYEKALYP GDVMVFPQGL LDFQEITGKI APGLCELRQR NPGLQILEFQ
HCFPTIFPPK TIAGTTCLDE ATIKKLKSGL GGTN