ID   RHRE_PEA                Reviewed;         217 AA.
AC   Q9S8P4; Q9SC40;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Rhicadhesin receptor;
DE   AltName: Full=Germin-like protein;
DE   Flags: Precursor;
GN   Name=GER1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin Perfection; TISSUE=Root;
RA   Wisniewski J.P., Bornemann S., Brewin N.J.;
RT   "Identification of an oxalate oxidase activity in pea roots, and cloning of
RT   cDNAs encoding germin-like proteins.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 21-45.
RX   PubMed=8111015; DOI=10.1007/bf00040583;
RA   Swart S., Logman T.J., Smit G., Lugtenberg B.J., Kijne J.W.;
RT   "Purification and partial characterization of a glycoprotein from pea
RT   (Pisum sativum) with receptor activity for rhicadhesin, an attachment
RT   protein of Rhizobiaceae.";
RL   Plant Mol. Biol. 24:171-183(1994).
CC   -!- FUNCTION: Putative receptor for bacterial rhicadhesin, an attachment
CC       protein of rhizobiaceae.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast.
CC       Secreted, cell wall.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AJ250832; CAB65369.1; -; mRNA.
DR   AlphaFoldDB; Q9S8P4; -.
DR   SMR; Q9S8P4; -.
DR   PRIDE; Q9S8P4; -.
DR   BRENDA; 1.15.1.1; 4872.
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   1: Evidence at protein level;
KW   Apoplast; Cell wall; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Manganese; Metal-binding; Receptor; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8111015"
FT   CHAIN           21..217
FT                   /note="Rhicadhesin receptor"
FT                   /id="PRO_0000010842"
FT   DOMAIN          58..207
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         107
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="C -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   217 AA;  22978 MW;  FC0D0C7BA22ECCC7 CRC64;
     MKLIAVLLLV VLATATTATA ADADALQDLC VADYASVILV NGFACKPASN VTAEDFFSNL
     LVKQGATNNT FGSLVTGANV QRIPGLNTLG VSMARIDYAP GGLNPPHTHP RATEMVFVLE
     GQLDVGFITT TNQLIAKTIA KGETFVFPKG LVHFQKNNGW EPATVIAGFN SQLPGTVNIP
     LTLFNATPPV PDNVLTKAFQ IGTKEVQKIK SKFAPKK