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GL23_ARATH
ID   GL23_ARATH              Reviewed;         219 AA.
AC   P93000;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Germin-like protein subfamily 2 member 3;
DE   Flags: Precursor;
GN   Name=GLP8; OrderedLocusNames=At3g05930; ORFNames=F10A16.23, F2O10.11;
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 [MRNA].
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).
RN   [2]
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   [3]
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).
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   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; U75207; AAB51585.1; -; mRNA.
DR   EMBL; AC012393; AAF26095.1; -; Genomic_DNA.
DR   EMBL; AC013454; AAF23223.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74317.1; -; Genomic_DNA.
DR   RefSeq; NP_187244.1; NM_111467.3.
DR   AlphaFoldDB; P93000; -.
DR   SMR; P93000; -.
DR   STRING; 3702.AT3G05930.1; -.
DR   PaxDb; P93000; -.
DR   PRIDE; P93000; -.
DR   ProteomicsDB; 248500; -.
DR   EnsemblPlants; AT3G05930.1; AT3G05930.1; AT3G05930.
DR   GeneID; 819762; -.
DR   Gramene; AT3G05930.1; AT3G05930.1; AT3G05930.
DR   KEGG; ath:AT3G05930; -.
DR   Araport; AT3G05930; -.
DR   TAIR; locus:2074489; AT3G05930.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_3_1; -.
DR   InParanoid; P93000; -.
DR   OMA; HMAIADT; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; P93000; -.
DR   PRO; PR:P93000; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P93000; baseline and differential.
DR   Genevisible; P93000; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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; 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.
PE   2: Evidence at transcript level;
KW   Apoplast; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..219
FT                   /note="Germin-like protein subfamily 2 member 3"
FT                   /id="PRO_0000010823"
FT   DOMAIN          60..209
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         109
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  23033 MW;  D344858985178CFD CRC64;
     MATSMIPIFV TFMLVAAHMA LADTNMLQDF CVADLSNGLK VNGYPCKDPA KVTPEDFYFI
     GLATAAATAN SSMGSAVTGA NVEKVPGLNT LGVSISRIDY APGGLNPPHL HPRASEAIFV
     LEGRLFVGFL TTTGKLISKH VNKGDVFVFP KALLHFQQNP NKAPASVLAA FDSQLPGTQV
     VGPSLFGSNP PIPDDLLAKA FGAAAPEIQK IKGKFPPKK
 
 
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