AMER2_XENTR
ID AMER2_XENTR Reviewed; 566 AA.
AC A4IGN8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=APC membrane recruitment protein 2;
DE Short=Amer2;
DE AltName: Full=Protein FAM123A;
GN Name=amer2; Synonyms=fam123a;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of the canonical Wnt signaling pathway
CC involved in neuroectodermal patterning. Acts by specifically binding
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to
CC the cell membrane and interacting with key regulators of the canonical
CC Wnt signaling pathway, such as components of the beta-catenin
CC destruction complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Translocates to the cell membrane following
CC binding to PtdIns(4,5)P2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
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DR EMBL; AAMC01105341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC135184; AAI35185.1; -; mRNA.
DR RefSeq; NP_001263429.1; NM_001276500.1.
DR AlphaFoldDB; A4IGN8; -.
DR STRING; 8364.ENSXETP00000062669; -.
DR PaxDb; A4IGN8; -.
DR Ensembl; ENSXETT00000060487; ENSXETP00000062669; ENSXETG00000033579.
DR GeneID; 100038269; -.
DR KEGG; xtr:100038269; -.
DR CTD; 219287; -.
DR Xenbase; XB-GENE-994663; amer2.
DR eggNOG; ENOG502QU08; Eukaryota.
DR HOGENOM; CLU_032195_0_0_1; -.
DR InParanoid; A4IGN8; -.
DR OrthoDB; 379029at2759; -.
DR PhylomeDB; A4IGN8; -.
DR TreeFam; TF333006; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000033579; Expressed in brain and 2 other tissues.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0007398; P:ectoderm development; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR019003; AMER.
DR PANTHER; PTHR22237; PTHR22237; 2.
DR Pfam; PF09422; WTX; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Lipid-binding; Membrane; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..566
FT /note="APC membrane recruitment protein 2"
FT /id="PRO_0000416263"
FT REGION 120..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 60980 MW; 34B3103781173300 CRC64;
MDLHYDCAES PAAEQPSGKI NKTAFKLFGK RKSGSGMPTI FGVKNKGDSK GTGKIGMVRS
KTLDGLADVV LESNKKEEPC TEAGAGQLNP EKSPKVLTIN ADVSSNSSVA KSHSFFSLLK
KNGKSENVRG EQAEQKAGSR QKRGLKGLFN SMRWSKKDKS YKDDKEGASE SQPGLILPSS
LTASLECIKE ETQKPLCEKG KSTEDIPADV PLAEHSGDVN TSAEENSLKA SEESPCSALI
TEQPQLEDAP LAQLQENLCQ LPQPEVETLQ NNKDEHVTGC GDVIADQDDD GGSSMGSKLV
PGNGKKVMSK KNTNIVAYQG GGEEMASPEQ VDETYVQELF SMIPPSEGAS EKTEKVNGTT
QASREVKCSD SAQDRNAIKP SKLKQVPVYR KERGDQNSKA NEKRQCLRNS DEGYWDSPTP
GQEEEEPRSV GKQALARDSC SGDALYDLYT DPDESIAKAQ VEEPPLSHSH SKPLSPVTTS
CPVKTASSNK ESKIPISIKH LPVHTTNQGT DSSSGSATGH PHPVKSELPR TKIPVSKVLV
RRVSNKAITE TAAGKRAIHD PARKHH
