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GL118_ARATH
ID   GL118_ARATH             Reviewed;         222 AA.
AC   P92999; Q9FL91;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Germin-like protein subfamily 1 member 18;
DE   AltName: Full=GLP2a copy 1;
DE   Flags: Precursor;
GN   Name=GLP2A; Synonyms=GLP5A; OrderedLocusNames=At5g39160; ORFNames=K3K3.2;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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 [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 51-222.
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=P92999-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AB010694; BAB09370.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94400.1; -; Genomic_DNA.
DR   EMBL; AY140077; AAM98218.1; -; mRNA.
DR   EMBL; BT002170; AAN72181.1; -; mRNA.
DR   EMBL; U75204; AAB51582.1; -; mRNA.
DR   RefSeq; NP_198732.2; NM_123278.4. [P92999-1]
DR   AlphaFoldDB; P92999; -.
DR   SMR; P92999; -.
DR   STRING; 3702.AT5G39160.1; -.
DR   PaxDb; P92999; -.
DR   EnsemblPlants; AT5G39160.1; AT5G39160.1; AT5G39160. [P92999-1]
DR   GeneID; 833910; -.
DR   Gramene; AT5G39160.1; AT5G39160.1; AT5G39160. [P92999-1]
DR   KEGG; ath:AT5G39160; -.
DR   Araport; AT5G39160; -.
DR   TAIR; locus:2157200; AT5G39160.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; P92999; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; P92999; -.
DR   PRO; PR:P92999; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P92999; baseline and differential.
DR   Genevisible; P92999; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..222
FT                   /note="Germin-like protein subfamily 1 member 18"
FT                   /id="PRO_0000010818"
FT   DOMAIN          62..213
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..48
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  23958 MW;  03ED6BCEC3B2746D CRC64;
     MRVSQSLVPF AIIALVLSFV NAYDPSPLQD FCVAIDDLKG VFVNGRFCKD PKRVDAKDFF
     FSGLNMPGNT NNQVGSNVTT VNVDQIPGLN TMGISLVRID YAPHGQNPPH THPRGSEILV
     LVEGTLYVGF VSSNQDNNRL FAKVLHPGDV FVFPIGMIHF QVNVGKIPAV AFAGLSSQNA
     GVITIANTVF GSNPPIYPEL LARAFQLDAS VVKELQAKFG SI
 
 
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