ID A0A176WG56_MARPO Unreviewed; 197 AA.
AC A0A176WG56;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN ORFNames=AXG93_4202s1090 {ECO:0000313|EMBL:OAE32107.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE32107.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE32107.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE32107.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271, ECO:0000256|RuleBase:RU366015}.
CC -!- SIMILARITY: Belongs to the germin family.
CC {ECO:0000256|ARBA:ARBA00007456, ECO:0000256|RuleBase:RU366015}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE32107.1}.
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DR EMBL; LVLJ01000890; OAE32107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WG56; -.
DR SMR; A0A176WG56; -.
DR OrthoDB; 367741at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd02241; cupin_OxOx; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR001929; Germin.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR31238:SF291; GERMIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR31238; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 3; 1.
DR Pfam; PF00190; Cupin_1; 1.
DR PRINTS; PR00325; GERMIN.
DR SMART; SM00835; Cupin_1; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU366015};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601929-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601929-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015}.
FT DOMAIN 43..190
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT BINDING 86
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 91
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 96
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
SQ SEQUENCE 197 AA; 20897 MW; 2E121EF6193FFA99 CRC64;
MLMQSVQASD PELTKDFQVP AGINAADIDG TFFTSEALRN VTPNVASPFA TVTTANLVAP
AKAPFLAVDG LGVSMALLQF PPGTVNPPHT HPRGTELLFI IEGTLDVGLV DTTNKLFTNT
LYKGDIFAFP KGLVHFQINN DKYKTVTALG GFSSSNAGLV RLPNTLFNTS TPISDKVLQI
SFGISGDVVK ALRAQFA
//