GenomeNet

Database: UniProt
Entry: A0A067LL97_JATCU
LinkDB: A0A067LL97_JATCU
Original site: A0A067LL97_JATCU 
ID   A0A067LL97_JATCU        Unreviewed;       228 AA.
AC   A0A067LL97;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN   ORFNames=JCGZ_17461 {ECO:0000313|EMBL:KDP45129.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP45129.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP45129.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP45129.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK914235; KDP45129.1; -; Genomic_DNA.
DR   RefSeq; XP_012086118.1; XM_012230728.1.
DR   AlphaFoldDB; A0A067LL97; -.
DR   OrthoDB; 511349at2759; -.
DR   Proteomes; UP000027138; 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; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR31238:SF298; GERMIN-LIKE PROTEIN; 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.
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:UP000027138};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW   Signal {ECO:0000256|RuleBase:RU366015}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT   CHAIN           23..228
FT                   /note="Germin-like protein"
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT                   /id="PRO_5019619888"
FT   DOMAIN          63..214
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   BINDING         109
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         114
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         119
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        32..49
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ   SEQUENCE   228 AA;  24672 MW;  11E6944B5CC4ED0C CRC64;
     MKTANFLVAL AVVALAFSSA MAYDPSPLQD ICVATNDTKH SVFVNGKFCK DPEKVTADDF
     FITGLNVRKQ TSKQLGVRVT LLTVDQVPGL NTNALSIVRV DFAPNGSLNP PHIHPRAAEI
     LTVLEGTLYA GFITGNPDHR LFAKILKPGD AFVFPLGLIH FQLNIGKTPA VALAVLNSQN
     PGVVTIANTI FGATPSVNPD VLTRAFHLDK DLVTKLQKEE WVDPDQLY
//
DBGET integrated database retrieval system