ID   GL24_ARATH              Reviewed;         220 AA.
AC   Q9M263; O04352;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Germin-like protein subfamily 2 member 4;
DE   Flags: Precursor;
GN   Name=GLP10; OrderedLocusNames=At3g62020; ORFNames=F21F14.190;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-220.
RC   STRAIN=cv. Columbia;
RX   PubMed=9869400; DOI=10.1023/a:1006038117130;
RA   Carter C., Graham R.A., Thornburg R.W.;
RT   "Arabidopsis thaliana contains a large family of germin-like proteins:
RT   characterization of cDNA and genomic sequences encoding 12 unique family
RT   members.";
RL   Plant Mol. Biol. 38:929-943(1998).
CC   -!- FUNCTION: May play a role in plant defense. Probably has no oxalate
CC       oxidase activity even if the active site is conserved.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9M263-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AL138642; CAB71909.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80296.1; -; Genomic_DNA.
DR   EMBL; U95036; AAB51752.1; -; mRNA.
DR   PIR; T47994; T47994.
DR   RefSeq; NP_191761.1; NM_116067.4. [Q9M263-1]
DR   AlphaFoldDB; Q9M263; -.
DR   SMR; Q9M263; -.
DR   STRING; 3702.AT3G62020.1; -.
DR   PaxDb; Q9M263; -.
DR   ProteomicsDB; 248580; -. [Q9M263-1]
DR   EnsemblPlants; AT3G62020.1; AT3G62020.1; AT3G62020. [Q9M263-1]
DR   GeneID; 825375; -.
DR   Gramene; AT3G62020.1; AT3G62020.1; AT3G62020. [Q9M263-1]
DR   KEGG; ath:AT3G62020; -.
DR   Araport; AT3G62020; -.
DR   TAIR; locus:2079582; AT3G62020.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   InParanoid; Q9M263; -.
DR   PhylomeDB; Q9M263; -.
DR   PRO; PR:Q9M263; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M263; baseline and differential.
DR   Genevisible; Q9M263; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IBA:GO_Central.
DR   GO; GO:2000280; P:regulation of root development; IBA:GO_Central.
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   Alternative splicing; Apoplast; Disulfide bond; Glycoprotein; Manganese;
KW   Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..220
FT                   /note="Germin-like protein subfamily 2 member 4"
FT                   /id="PRO_0000010824"
FT   DOMAIN          58..209
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         108
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  23550 MW;  91894D0539B6299F CRC64;
     MDSRCFGFFF TLLSLNVIVL AYDPDTLQDL CVADRTSGIK VNGFTCKPES NITASDFFFA
     GIGKPAVVNN TVGSAVTGAN VEKIAGLNTL GVSLARIDYA PGGLNPPHTH PRATEVIFVL
     EGELDVGFIT TANKLFAKTV KKGEVFVFPR GLIHYQKNND KAKPASVISA FNSQLPGTQS
     IAATLFTATP AIPDHVLTTT FQIGTKEIEK IKSKFAPKKV