AMER2_DANRE
ID AMER2_DANRE Reviewed; 654 AA.
AC F1QGH6; A6H8T6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=APC membrane recruitment protein 2;
DE Short=Amer2;
DE AltName: Full=Protein FAM123A;
GN Name=amer2; Synonyms=fam123a; ORFNames=zgc:165647;
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=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-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; CR383672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146746; AAI46747.1; -; mRNA.
DR RefSeq; NP_001093622.1; NM_001100152.1.
DR AlphaFoldDB; F1QGH6; -.
DR STRING; 7955.ENSDARP00000102405; -.
DR PaxDb; F1QGH6; -.
DR Ensembl; ENSDART00000115165; ENSDARP00000102405; ENSDARG00000075222.
DR GeneID; 100101649; -.
DR KEGG; dre:100101649; -.
DR CTD; 219287; -.
DR ZFIN; ZDB-GENE-070719-5; amer2.
DR eggNOG; ENOG502QU08; Eukaryota.
DR GeneTree; ENSGT00530000063529; -.
DR HOGENOM; CLU_032195_0_0_1; -.
DR InParanoid; F1QGH6; -.
DR OMA; IDRICLM; -.
DR OrthoDB; 379029at2759; -.
DR TreeFam; TF333006; -.
DR PRO; PR:F1QGH6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000075222; Expressed in retina and 9 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; 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..654
FT /note="APC membrane recruitment protein 2"
FT /id="PRO_0000416261"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 85
FT /note="E -> G (in Ref. 2; AAI46747)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> E (in Ref. 2; AAI46747)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="L -> F (in Ref. 2; AAI46747)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="S -> N (in Ref. 2; AAI46747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 69090 MW; 7848BCBE198E5E91 CRC64;
MEVQTECSEP PPCDPQPPGK LNKAAFKLFG KRKSGSSMPS IFSVRNKGES TGKAAGKTLE
LVRSKTHDGL ITDTPSELDS HRKEESASSD QLHAGTPDGV STAPLRSSIT KSFSFFSLLR
RSSSRAGDGT TTVGRRGRGL KGLFSSMRWR RKPQIQEDTL EVAKEVKEGD LILSSSSGSV
KTEKDMTLTL EPLPQVFEES PLPGDSDKWK VASMQGIQGT NEVECGNCGP SVSQQHTVTE
ESPAPSPLRV QTGGLQNHKH SSSTHLSSIP TCALTPPMEH STADPQSEQS VDRLCSMFTD
VTSLKSFDSL TGCGDIIADP EEDSGNGGSA TSSGTGSSSG GCMGRRLSGA GTNSERCSPA
KPPLPPQVSS LASIHASCYM PAHQRPRAAP KKPQGSGVVA YMGGGEEMAS PEGVDDADMQ
GLWHMLPQKD EDSPAPRRAE PVLHHAPARL EKRPPQVKAL GLSKIPVSGS SKTGKQQPSR
PSPPPVDKEL QDAPPSDEGY WDSPTPGPED EDSTFLRRDG LLRDSCSGDA LYDLYDPDSP
SAAGSDDDAS SPTKSAGDLK MNLPSPKCSS SATSSFRSMK GSTSLPRDSK IPISVRQTPP
SHSSSQGALS SNLSPTSTTP PKKTDAPPRT KIPVSKVPVR RSGGKSTSTS QSRK
