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Database: UniProt
Entry: A0A199UES2_ANACO
LinkDB: A0A199UES2_ANACO
Original site: A0A199UES2_ANACO 
ID   A0A199UES2_ANACO        Unreviewed;       215 AA.
AC   A0A199UES2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN   Name=LOC109725047 {ECO:0000313|RefSeq:XP_020109685.1};
GN   ORFNames=ACMD2_16505 {ECO:0000313|EMBL:OAY63070.1};
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY63070.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY63070.1, ECO:0000313|Proteomes:UP000092600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY63070.1};
RX   PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA   Redwan R.M., Saidin A., Kumar S.V.;
RT   "The draft genome of MD-2 pineapple using hybrid error correction of long
RT   reads.";
RL   DNA Res. 0:0-0(2016).
RN   [2] {ECO:0000313|RefSeq:XP_020109685.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_020109685.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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; LSRQ01008394; OAY63070.1; -; Genomic_DNA.
DR   RefSeq; XP_020109685.1; XM_020254096.1.
DR   STRING; 4615.A0A199UES2; -.
DR   EnsemblPlants; Aco008231.1.mrna1; Aco008231.1.mrna1; Aco008231.1.path1.
DR   GeneID; 109725047; -.
DR   Gramene; Aco008231.1.mrna1; Aco008231.1.mrna1; Aco008231.1.path1.
DR   OrthoDB; 367741at2759; -.
DR   Proteomes; UP000092600; Unassembled WGS sequence.
DR   Proteomes; UP000515123; Linkage group 19.
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:SF300; GERMIN-LIKE PROTEIN SUBFAMILY 1 MEMBER 13-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:UP000092600};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW   Signal {ECO:0000256|RuleBase:RU366015}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT   CHAIN           21..215
FT                   /note="Germin-like protein"
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT                   /id="PRO_5041471667"
FT   DOMAIN          59..209
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   BINDING         104
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         107
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         109
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         109
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
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         155
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ   SEQUENCE   215 AA;  23327 MW;  8A1A81D0F77AA76D CRC64;
     MASHVLLLAL LALVLSQAIA SDPSPLQDFC VADKNSPVFV NGFVCKNPNF TTPEDFFFKG
     LDQPGNTMNK LGFNATLVNA MMLPGLNTLG ISLARLDFAP YGLNPPHTHP RATEVFTVLE
     GTFYVGFVTS NPDNKLFSKI LNKGDVFVFP EGLIHFQFNV GKTSAFGISG LSSQNPDVIT
     IANAVFGSNP PISDDILAKA FQLDKKIVDW LQTQF
//
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