AMER2_MOUSE
ID AMER2_MOUSE Reviewed; 672 AA.
AC Q8CCJ4; Q7TNC5; Q8K0U9; Q9D0Q2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=APC membrane recruitment protein 2;
DE Short=Amer2;
DE AltName: Full=Protein FAM123A;
GN Name=Amer2; Synonyms=Fam123a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-672 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-672 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-672 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 599-608, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-223; SER-227 AND
RP SER-284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBUNIT: Interacts with APC. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CCJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCJ4-2; Sequence=VSP_024090;
CC -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30356.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH56350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB27452.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC103355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK032651; BAC27972.1; ALT_INIT; mRNA.
DR EMBL; AK011185; BAB27452.1; ALT_INIT; mRNA.
DR EMBL; AK139177; BAE23912.1; ALT_INIT; mRNA.
DR EMBL; BC030356; AAH30356.1; ALT_INIT; mRNA.
DR EMBL; BC056350; AAH56350.1; ALT_INIT; mRNA.
DR CCDS; CCDS27177.2; -. [Q8CCJ4-1]
DR CCDS; CCDS88682.1; -. [Q8CCJ4-2]
DR RefSeq; NP_001158177.1; NM_001164705.1. [Q8CCJ4-2]
DR RefSeq; NP_082389.1; NM_028113.3. [Q8CCJ4-1]
DR RefSeq; XP_006519653.1; XM_006519590.3. [Q8CCJ4-1]
DR AlphaFoldDB; Q8CCJ4; -.
DR BioGRID; 215168; 1.
DR IntAct; Q8CCJ4; 1.
DR MINT; Q8CCJ4; -.
DR STRING; 10090.ENSMUSP00000022561; -.
DR iPTMnet; Q8CCJ4; -.
DR PhosphoSitePlus; Q8CCJ4; -.
DR jPOST; Q8CCJ4; -.
DR MaxQB; Q8CCJ4; -.
DR PaxDb; Q8CCJ4; -.
DR PeptideAtlas; Q8CCJ4; -.
DR PRIDE; Q8CCJ4; -.
DR ProteomicsDB; 281969; -. [Q8CCJ4-1]
DR ProteomicsDB; 281970; -. [Q8CCJ4-2]
DR Antibodypedia; 49984; 29 antibodies from 10 providers.
DR DNASU; 72125; -.
DR Ensembl; ENSMUST00000022561; ENSMUSP00000022561; ENSMUSG00000021986. [Q8CCJ4-1]
DR Ensembl; ENSMUST00000225247; ENSMUSP00000153031; ENSMUSG00000021986. [Q8CCJ4-2]
DR GeneID; 72125; -.
DR KEGG; mmu:72125; -.
DR UCSC; uc007ufb.2; mouse. [Q8CCJ4-2]
DR UCSC; uc011zmz.1; mouse. [Q8CCJ4-1]
DR CTD; 219287; -.
DR MGI; MGI:1919375; Amer2.
DR VEuPathDB; HostDB:ENSMUSG00000021986; -.
DR eggNOG; ENOG502QU08; Eukaryota.
DR GeneTree; ENSGT00530000063529; -.
DR InParanoid; Q8CCJ4; -.
DR OMA; IDRICLM; -.
DR OrthoDB; 379029at2759; -.
DR PhylomeDB; Q8CCJ4; -.
DR TreeFam; TF333006; -.
DR BioGRID-ORCS; 72125; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Amer2; mouse.
DR PRO; PR:Q8CCJ4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CCJ4; protein.
DR Bgee; ENSMUSG00000021986; Expressed in superior cervical ganglion and 159 other tissues.
DR ExpressionAtlas; Q8CCJ4; baseline and differential.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..672
FT /note="APC membrane recruitment protein 2"
FT /id="PRO_0000281886"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT VAR_SEQ 255..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024090"
SQ SEQUENCE 672 AA; 69933 MW; 5CE3FFDF4FFE1348 CRC64;
METGRSRGGG AAVSERGGGA RAGVCGRQEQ AGALAADMDS HCECAAETPA AEPPSGKINK
AAFKLFKKRK SGGTMPSIFG VKNKGDGKSS GPTGMVRSRT HDGLAEVLVL EGSKKEEPPG
GSDHSGARPI PGPPKPSGPG LGSLASSSVA KSHSFFSLLK KNGRSETGKG DHAEASKAGG
KQKRGLKGIF SSMRWHRRDK RGKEEEEKAV RAAGPGNLVL PGSLTASLEC VKEEPPRAAR
RPDSPGQDAS RHAAGEPAGG EQAPASAESA PERICLEAGS PTGSGDQSSR GEDAEGHRRE
EKPGAALESG AGEVQAAEDA SKTGDVPIKT VPLVDSEGGS GRASAVPDPS SVDPPSDPSA
DRICLMFSDV TSLKSFDSLT GCGDIIADPE EEAGPSCDKH VPGPGKPVLS KKNASVVAYQ
GGGEEMASPD QVDDTYLPEF WDMLSQTEDQ GQGTQEGAAK AATASDIKLA PETSSDTRCG
EAAKDMSSVK RRRLHRIPIE SQQKEEPKHP EKEHQEGVPN SDEGYWDSTT PGPEEESISN
SSSSKKVVIP RDSDSGDALC DLYVEPEASP ATLPATEDPP CLSRLKPVSP GTITCPLRTP
GSLLKDSKIP ISIKHLSNLP SSHPVVHQQP ARSEVPRTKI PVSKVLVRRV SNRGLAGTTI
RAAACHDSAK KL
