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Database: UniProt
Entry: A9SDF7_PHYPA
LinkDB: A9SDF7_PHYPA
Original site: A9SDF7_PHYPA 
ID   A9SDF7_PHYPA            Unreviewed;       223 AA.
AC   A9SDF7; Q5KT26;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN   Name=PpGLP3b {ECO:0000313|EMBL:BAD86504.1};
GN   ORFNames=PHYPA_022422 {ECO:0000313|EMBL:PNR36571.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:BAD86504.1};
RN   [1] {ECO:0000313|EMBL:BAD86504.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15604751; DOI=10.1007/s11103-004-3475-x;
RA   Nakata M., Watanabe Y., Sakurai Y., Hashimoto Y., Matsuzaki M.,
RA   Takahashi Y., Satoh T.;
RT   "Germin-like protein gene family of a moss, Physcomitrella patens,
RT   phylogenetically falls into two characteristic new clades.";
RL   Plant Mol. Biol. 56:381-395(2004).
RN   [2] {ECO:0000313|EMBL:PNR36571.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004
RC   {ECO:0000313|EnsemblPlants:PAC:32905484.CDS.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [3] {ECO:0000313|EMBL:PNR36571.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004
RC   {ECO:0000313|EnsemblPlants:PAC:32905484.CDS.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [4] {ECO:0000313|EnsemblPlants:PAC:32905484.CDS.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
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   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000256|ARBA:ARBA00011268}.
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; AB177645; BAD86504.1; -; Genomic_DNA.
DR   EMBL; ABEU02000017; PNR36571.1; -; Genomic_DNA.
DR   RefSeq; XP_001764390.1; XM_001764338.1.
DR   RefSeq; XP_001764391.1; XM_001764339.1.
DR   RefSeq; XP_001764467.1; XM_001764415.1.
DR   AlphaFoldDB; A9SDF7; -.
DR   SMR; A9SDF7; -.
DR   STRING; 3218.A9SDF7; -.
DR   EnsemblPlants; Pp3c17_21150V3.2; PAC:32906860.CDS.1; Pp3c17_21150.
DR   EnsemblPlants; Pp3c17_21300V3.1; PAC:32905484.CDS.1; Pp3c17_21300.
DR   Gramene; Pp3c17_21150V3.2; PAC:32906860.CDS.1; Pp3c17_21150.
DR   Gramene; Pp3c17_21300V3.1; PAC:32905484.CDS.1; Pp3c17_21300.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_3_1; -.
DR   Proteomes; UP000006727; Chromosome 17.
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:SF254; GERMIN-LIKE PROTEIN SUBFAMILY 1 MEMBER 16-RELATED; 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|PIRSR:PIRSR601929-3};
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:UP000006727};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW   Signal {ECO:0000256|RuleBase:RU366015}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT   CHAIN           30..223
FT                   /note="Germin-like protein"
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT                   /id="PRO_5014297919"
FT   DOMAIN          65..214
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   BINDING         110
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
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         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         120
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   DISULFID        36..51
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ   SEQUENCE   223 AA;  23321 MW;  C450BD2A1A38B85F CRC64;
     METLAKRVVF VALLVQAALL PMLSMAADAD PIQDFCVADA SSTLTINGLV CKPAADVKVN
     DFLFRGLDKP GNTGGPTANA VTPVAAAQLP GLNTLGISLA RLDFAKGGIN VPHIHPRATE
     VLALLQGELY VGFVSTTNNT LFATTLYAGD VFVFPRGLVH FQLNVGKGAA VAIAALSSQN
     PGVQQVAPAL FAANPPINDE VLEKAFHLNQ NQVQHIKASF VKA
//
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