ID D7LSS0_ARALL Unreviewed; 220 AA.
AC D7LSS0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN ORFNames=ARALYDRAFT_486710 {ECO:0000313|EMBL:EFH54686.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: May play a role in plant defense. Probably has no oxalate
CC oxidase activity even if the active site is conserved.
CC {ECO:0000256|ARBA:ARBA00003629}.
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}.
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DR EMBL; GL348717; EFH54686.1; -; Genomic_DNA.
DR RefSeq; XP_002878427.1; XM_002878381.1.
DR AlphaFoldDB; D7LSS0; -.
DR STRING; 81972.D7LSS0; -.
DR EnsemblPlants; fgenesh2_kg.5__2702__AT3G62020.1; fgenesh2_kg.5__2702__AT3G62020.1; fgenesh2_kg.5__2702__AT3G62020.1.
DR GeneID; 9312720; -.
DR Gramene; fgenesh2_kg.5__2702__AT3G62020.1; fgenesh2_kg.5__2702__AT3G62020.1; fgenesh2_kg.5__2702__AT3G62020.1.
DR KEGG; aly:9312720; -.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR HOGENOM; CLU_015790_0_3_1; -.
DR OrthoDB; 367741at2759; -.
DR Proteomes; UP000008694; 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; IPR019780; Germin_Mn-BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR31238:SF327; GERMIN-LIKE PROTEIN SUBFAMILY 2 MEMBER 4; 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.
DR PROSITE; PS00725; GERMIN; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU366015};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601929-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000008694};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366015}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT CHAIN 22..220
FT /note="Germin-like protein"
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT /id="PRO_5019617436"
FT DOMAIN 58..209
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT BINDING 105
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 110
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 115
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT DISULFID 31..46
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ SEQUENCE 220 AA; 23466 MW; 5C1763C67355AB83 CRC64;
MDSRCYGFFF ALFSLTVVAL AYDPDTLQDL CVADHTSGIK VNGFTCKPES NITASDFFFA
GIGKPAVVNN TVGSAVTGAN VEKIAGLNTL GVSLARIDYA PGGLNPPHTH PRATEVIFVL
EGELDVGFIT TANKLFAKTV KKGEVFVFPR GLIHYQKNND KAKPASVISA FNSQLPGTQS
IAATLFTATP AIPDHVLTTA FQIGTKEIEK IKSKFAPKKV
//
