AGR2_XENTR
ID AGR2_XENTR Reviewed; 164 AA.
AC Q28ID5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Anterior gradient protein 2 {ECO:0000312|EMBL:CAJ82848.1};
DE Flags: Precursor;
GN Name=agr2 {ECO:0000312|EMBL:CAJ82848.1}; ORFNames=TNeu048m19.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ82848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ82848.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:O95994}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255, ECO:0000305}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:O88312}.
CC -!- SIMILARITY: Belongs to the AGR family. {ECO:0000255}.
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; CR760462; CAJ82848.1; -; mRNA.
DR RefSeq; NP_001016627.1; NM_001016627.3.
DR RefSeq; XP_012820168.1; XM_012964714.2.
DR AlphaFoldDB; Q28ID5; -.
DR SMR; Q28ID5; -.
DR STRING; 8364.ENSXETP00000049323; -.
DR PaxDb; Q28ID5; -.
DR GeneID; 549381; -.
DR KEGG; xtr:549381; -.
DR CTD; 10551; -.
DR Xenbase; XB-GENE-971548; agr2.
DR eggNOG; ENOG502RYQ8; Eukaryota.
DR HOGENOM; CLU_088048_1_0_1; -.
DR InParanoid; Q28ID5; -.
DR OrthoDB; 1382017at2759; -.
DR PhylomeDB; Q28ID5; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025625; Expressed in neurula embryo and 6 other tissues.
DR ExpressionAtlas; Q28ID5; differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0002162; F:dystroglycan binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT CHAIN 21..164
FT /note="Anterior gradient protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000392580"
FT MOTIF 34..43
FT /note="Homodimer stabilization; interchain"
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT MOTIF 49..56
FT /note="Homodimer stabilization; interchain"
FT /evidence="ECO:0000250|UniProtKB:O95994"
SQ SEQUENCE 164 AA; 18682 MW; 562A9306A41963FE CRC64;
METVLKTLFV LLVATSLTLA KDLPQATRVL QTLSRGWGDN LEWVQTYEEG LYKAKTENKP
LILINHRNDC PHSLALKKAF AEHQGIQKLA EEFVLLNVVY DPTDKNLQLD GQYVPKVVFV
DPSLVVRADL PGKYSNHQYT YEPADIDLLF ENMKKALILL KTEL