AMER1_MOUSE
ID AMER1_MOUSE Reviewed; 1132 AA.
AC Q7TS75; B1AUM2; Q8BT92; Q8C7P7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=APC membrane recruitment protein 1;
DE Short=Amer1;
DE AltName: Full=Protein FAM123B;
GN Name=Amer1; Synonyms=Fam123b;
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 1-387.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 1-389.
RC TISSUE=Embryo;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17204608; DOI=10.1126/science.1137509;
RA Rivera M.N., Kim W.J., Wells J., Driscoll D.R., Brannigan B.W., Han M.,
RA Kim J.C., Feinberg A.P., Gerald W.L., Vargas S.O., Chin L., Iafrate A.J.,
RA Bell D.W., Haber D.A.;
RT "An X chromosome gene, WTX, is commonly inactivated in Wilms tumor.";
RL Science 315:642-645(2007).
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: acts as a positive regulator by promoting LRP6
CC phosphorylation. Also acts as a negative regulator by acting as a
CC scaffold protein for the beta-catenin destruction complex and promoting
CC stabilization of Axin at the cell membrane. Promotes CTNNB1
CC ubiquitination and degradation. Involved in kidney development (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTNNB1, AXIN1, LRP6, KEAP1, APC and BTRC.
CC Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
CC ligase complexes containing BTRC and/or FBXW11. Identified in the beta-
CC catenin destruction complex containing CTNNB1, APC, AXIN1 and AXIN2.
CC Interacts with WT1 (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 -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:17204608}.
CC -!- DEVELOPMENTAL STAGE: In embryos, it is highly expressed in the neonatal
CC brain and kidney and then declines substantially in the mature organs.
CC Also expressed in lung and spleen. Expressed in the condensing
CC metanephric mesenchyme and in early epithelial structures that are
CC precursors to glomeruli. {ECO:0000269|PubMed:17204608}.
CC -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53442.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC25373.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC33914.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL671765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK049774; BAC33914.1; ALT_SEQ; mRNA.
DR EMBL; AK012651; BAC25373.1; ALT_FRAME; mRNA.
DR EMBL; BC053442; AAH53442.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41067.1; -.
DR RefSeq; NP_780388.2; NM_175179.4.
DR AlphaFoldDB; Q7TS75; -.
DR SMR; Q7TS75; -.
DR BioGRID; 215325; 5.
DR STRING; 10090.ENSMUSP00000109502; -.
DR iPTMnet; Q7TS75; -.
DR PhosphoSitePlus; Q7TS75; -.
DR jPOST; Q7TS75; -.
DR MaxQB; Q7TS75; -.
DR PaxDb; Q7TS75; -.
DR PeptideAtlas; Q7TS75; -.
DR PRIDE; Q7TS75; -.
DR ProteomicsDB; 296399; -.
DR Antibodypedia; 43710; 112 antibodies from 27 providers.
DR DNASU; 72345; -.
DR Ensembl; ENSMUST00000084535; ENSMUSP00000109502; ENSMUSG00000050332.
DR GeneID; 72345; -.
DR KEGG; mmu:72345; -.
DR UCSC; uc009ttx.2; mouse.
DR CTD; 139285; -.
DR MGI; MGI:1919595; Amer1.
DR VEuPathDB; HostDB:ENSMUSG00000050332; -.
DR eggNOG; ENOG502QT5W; Eukaryota.
DR GeneTree; ENSGT00530000063529; -.
DR HOGENOM; CLU_009351_2_0_1; -.
DR InParanoid; Q7TS75; -.
DR OMA; KPIMEYQ; -.
DR OrthoDB; 139922at2759; -.
DR PhylomeDB; Q7TS75; -.
DR TreeFam; TF333006; -.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR BioGRID-ORCS; 72345; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Amer1; mouse.
DR PRO; PR:Q7TS75; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q7TS75; protein.
DR Bgee; ENSMUSG00000050332; Expressed in dorsal pancreas and 263 other tissues.
DR Genevisible; Q7TS75; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:1904713; F:beta-catenin destruction complex binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0072161; P:mesenchymal cell differentiation involved in kidney development; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
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; 2.
DR Pfam; PF09422; WTX; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Lipid-binding; Membrane; Nucleus;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..1132
FT /note="APC membrane recruitment protein 1"
FT /id="PRO_0000281888"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..942
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTC6"
SQ SEQUENCE 1132 AA; 124164 MW; 7039226488581FCC CRC64;
MESQQDEAVQ TKGASTSSDA QDQGAEKGAK NKTTEATEGP TSEPPLSGPG RLKKTAMKLF
GGKKGICTLP SFFGGGRSKG SGKVSSKKSL NKSKTHDGLS EASQGPEDVV IEETDLSTPL
SKSSAQFPSS QSANGALEIG SKHKTSGTEA IEKAGVEKVP SVHKPKKSLK SFFSSIRRHR
KGKTSGADQS VPGAKELEGA RTRSHEHVSS ISLPSSEEIF RDTRKENAKP QDAPGPKMSP
AQVHFSPTTE KAACKNPEKL TRTCASEFMQ PKPVLEGGSL EEPHTSETEG KVVAGEVNPP
NGPVGDQLSL LFGDVTSLKS FDSLTGCGDI IAEQDMDSMT DSMASGGQRA NRDGTKRSSC
LVTYQGGGEE MALPDDDDND DEEEEEEEEE EEEEEEEEEE EEEEEEEEEL LEDEEEVKDG
EENDDLEYLW ASAQIYPRFN MNLGYHTAIS PSHQGYMLLD PVQSYPNLGL GELLTPQSDQ
QESAPNSDEG YYDSTTPGFE DDSGEALGLA HRDCLPRDSY SGDALYEFYE PDDSLEHSPP
GDDCLYDLRG RNSEMLDPFL NLEPFSSRPP GAMETEEERL VTIQKQLLYW ELRREQREAQ
EACAREAHAR EAYARDTHTR ESYGRNVRAR ETQALEAHSQ EGRVQETKVR QEKPALEYQM
RPLGPSVMGL VAGTSGGSQT SHRGTTSAFP ATSSSEPDWR DFRPLEKRFE GTCSKKDQST
CLMQLFQSDA MFEPDMQEAN FGGSPRKAYP SYSPPEEPEE EEEEKEGNAT VSFSQALVEF
TSNGNLFTSM SYSSDSDSSF TQNLPELPPM VTFDIADVER DGEGKCEENP EFNNDEDLTA
SLEAFELGYY HKHAFNSYHS RFYQGLPWGV SSLPRYLGLP GVHPRPPPAA MALNRRSRSL
DNAESLELEL SSSHLAQGYM ESDELQAHQE DSDEEGEEEE GEWGRDSPLS LYTEPPGVYD
WPPWAHCPLP VGPGLAWMSP NQLYEPFNQS SYVQATCCVP PVAMPVSVPG RTPGDSVSQL
ARPSHLPLPM GPCYNLQSQA SQSGRAKPRD VLLPVDEPSC SSISGANSQS QAKPVGITHG
IPQLPRVRPE PFQLQPNHYR ASNLDLSKER GEQGASLSTS YSSTAMNGNL AK
