ID   AMER2_XENLA             Reviewed;         624 AA.
AC   Q6INC4;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=APC membrane recruitment protein 2;
DE            Short=Amer2;
DE            Short=XAmer2;
DE   AltName: Full=Protein FAM123A;
GN   Name=amer2; Synonyms=fam123a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=22128170; DOI=10.1074/jbc.m111.308650;
RA   Pfister A.S., Tanneberger K., Schambony A., Behrens J.;
RT   "Amer2 protein is a novel negative regulator of Wnt/beta-Catenin signaling
RT   involved in neuroectodermal patterning.";
RL   J. Biol. Chem. 287:1734-1741(2012).
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. {ECO:0000269|PubMed:22128170}.
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   -!- DEVELOPMENTAL STAGE: Expressed in the ectoderm at early gastrula
CC       stages. During neurulation, expressed in the dorsal neuroectoderm, with
CC       the strongest signal detectable in the anterior neural plate. In
CC       tadpole stages, present most prominently in the brain, eye, otic
CC       vesicle, and cranial ganglia. From stage 30 onward, expression is
CC       observed in the forebrain, midbrain, and hindbrain but is excluded from
CC       the boundaries between these domains. {ECO:0000269|PubMed:22128170}.
CC   -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72359.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC072359; AAH72359.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6INC4; -.
DR   OMA; IDRICLM; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; IMP:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR019003; AMER.
DR   PANTHER; PTHR22237; PTHR22237; 1.
DR   Pfam; PF09422; WTX; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipid-binding; Membrane; Reference proteome;
KW   Wnt signaling pathway.
FT   CHAIN           1..624
FT                   /note="APC membrane recruitment protein 2"
FT                   /id="PRO_0000416262"
FT   REGION          77..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..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        195..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  67188 MW;  33DBE8719E205CDC CRC64;
     MDLHYDCAES PAAEQPSGKI NKTAFKLFGK RRSGSAMPTI FGVKNKGDGK GTGNIGMVRS
     KTLDGLADVV LESNKKEEPC TNAGAGQLNT EKSPKVVTIN PDVSSDSSVA KSHSFFSLLK
     RNGKSENVKG ELAEQKPGSR QKRGLKGLFN SMRWSKKDKS YKDDKEGASE NQPGLILPSS
     LTASLECIKE ETQKPLCEKE KSEEDIPADV PSVEHSGDVN TSAEENPLNG CVESPCPALI
     TKEPQLEDPP VIQQVDNLYQ LPDPEVETLP DNKDEDVTGD IPVNTVSIVE PECDVGQEIA
     APDPTTVDPP SEPSFDRICL MLADVTSLKS FDSLTGCGDV IADQDDDGGS SKGSKVVPGN
     GKKVTSKKNA NIVAYQGGGE EMASPEEADE TYVQELFSMI PQSEGASEKP EKVNGTTQVT
     AREVKCSDSG RDRNTVKPSK LRQVPIRRKE RGDQNSKGNE KRQCHRNSDE GYWDSTTLGQ
     EEEEPRSVGK QALPRDSCSG DALYDLYTDP DESIPKAQAE EPPVSHSHSK PLSPVTASCP
     VKTASSNKES KIPISIKHLP VHTTNQGIDS GSGSAAGHSH PVKSELPRTK IPVSKVLVRR
     VSNKAITETA AGKRAIHDPA RKHH