AMER1_DANRE
ID AMER1_DANRE Reviewed; 930 AA.
AC F1RDM5; A9JTD0;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=APC membrane recruitment protein 1;
DE Short=Amer1;
DE AltName: Full=Protein FAM123B;
GN Name=amer1; Synonyms=fam123b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by
CC specifically binding phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2), translocating to the cell membrane and interacting
CC with key regulators of the canonical Wnt signaling pathway, such as
CC components of the beta-catenin destruction complex. Acts both as a
CC positive and negative regulator of the Wnt signaling pathway, depending
CC on the context (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between
CC nucleus and cytoplasm. Detected in nuclear paraspeckles that are found
CC close to splicing speckles. Translocates to the cell membrane following
CC binding to PtdIns(4,5)P2 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI55292.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR812469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC155291; AAI55292.1; ALT_INIT; mRNA.
DR AlphaFoldDB; F1RDM5; -.
DR STRING; 7955.ENSDARP00000099285; -.
DR PaxDb; F1RDM5; -.
DR ZFIN; ZDB-GENE-070719-2; amer1.
DR eggNOG; ENOG502QT5W; Eukaryota.
DR HOGENOM; CLU_009351_1_0_1; -.
DR InParanoid; F1RDM5; -.
DR OMA; KPIMEYQ; -.
DR TreeFam; TF333006; -.
DR Reactome; R-DRE-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DRE-196299; Beta-catenin phosphorylation cascade.
DR PRO; PR:F1RDM5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0060828; P: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; Cytoplasm; Lipid-binding; Membrane; Nucleus;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..930
FT /note="APC membrane recruitment protein 1"
FT /id="PRO_0000416259"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 231
FT /note="E -> K (in Ref. 2; AAI55292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 102526 MW; E6C949F15F0DA2DE CRC64;
MEIATRCEVG AMRGPSSDSV SHDIPQPQSP PSVKIRKTAF KFFGGRKSIC VLPSFFGGRG
RSQRKGSSKT GVTKSQTYDG VSRACWDDLG RSSSEVASGD FEFCSEPQKS QEDHGKSQSL
PRQRRGLRGL FSSIRRHRKN KNVEVEKREA LEMSSSFHAK TVPGALPSVS DRGDYHGDSQ
GEELVPDVPN QTTGSECELP LAATECTIDV TLVPEKRRSR VEMDKRRRAE EEGIGEDEKT
GRQEGLMTYH QPLSAESELD RLAEQNVDVP DGEPPVASCS SENLVFGDVS SLKSFDSLTG
CGDIIADQDD VSVAESSVSA DRGSRNAGKR SSCFVTYQGG GEEMATPDEI DADYLQSLWE
SETSNEVCYI PSDRGSDSPS LTPDQQLSSI RATSSSSPMG ITETALTPAD LLSPQSDRQE
SVPNSDEGYY DSTTPGMEEE SRERPHQERL PRDSYSGDAL YELFEPDDRL LSPSLPPKDA
HSFVGAPLQA DKSPTNPLYS LASTAIETGA METEEERLSK IQHALLCCEL QNLRSPSKNQ
LLFHSDCFYD DSNLPVDDSK QDLQEVINQR YPQSPPRSQA VKEGVPRIRG QVQESSLFAP
CADSVLNPQV IETTRPQPQS DDQGSLRPSR GCSQSQEELM VCFSQALVDF TKNTRLYRNS
TESLDGSESS SPFGPSLRAL PAIVTFDVVD MENEGECEQQ TDLAEEEEEL ASPYEPFEDD
GCYLQQDAFA ECDQRTFDAY EQSLLLSNAW GIASLPRHLS LGRPCPPVPA PLALNRRSRS
LDTDSLEFQT SEIYTSVTKY DSKGTAFSQS RTVDCNDMDF PRQPCRITVD SWRRGYRQNF
DSSNASQQEL KLPHLSQSTV RPSHLPLKNN CRSRNLPAAT RVDGEGEILF GGGDALYPCS
YPPMGTQWKN RPVGVTQGVP HLRSEQSADH
