AMER3_MOUSE
ID AMER3_MOUSE Reviewed; 780 AA.
AC Q6NS69; Q8BS82;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=APC membrane recruitment protein 3;
DE Short=Amer3;
DE AltName: Full=Protein FAM123C;
GN Name=Amer3; Synonyms=Fam123c;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-780.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
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 (By similarity).
CC {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; BC070435; AAH70435.1; -; mRNA.
DR EMBL; AK034979; BAC28901.1; -; mRNA.
DR CCDS; CCDS14871.1; -.
DR RefSeq; NP_998892.1; NM_213727.2.
DR RefSeq; XP_006495883.1; XM_006495820.2.
DR RefSeq; XP_006495884.1; XM_006495821.3.
DR AlphaFoldDB; Q6NS69; -.
DR BioGRID; 229228; 2.
DR STRING; 10090.ENSMUSP00000054748; -.
DR iPTMnet; Q6NS69; -.
DR PhosphoSitePlus; Q6NS69; -.
DR PaxDb; Q6NS69; -.
DR PRIDE; Q6NS69; -.
DR ProteomicsDB; 296349; -.
DR Antibodypedia; 50181; 18 antibodies from 7 providers.
DR Ensembl; ENSMUST00000052670; ENSMUSP00000054748; ENSMUSG00000045174.
DR GeneID; 211383; -.
DR KEGG; mmu:211383; -.
DR UCSC; uc011wjc.1; mouse.
DR CTD; 205147; -.
DR MGI; MGI:3026939; Amer3.
DR VEuPathDB; HostDB:ENSMUSG00000045174; -.
DR eggNOG; ENOG502QVAK; Eukaryota.
DR GeneTree; ENSGT00530000063529; -.
DR HOGENOM; CLU_011805_0_0_1; -.
DR InParanoid; Q6NS69; -.
DR OMA; LSMCSFH; -.
DR OrthoDB; 152946at2759; -.
DR PhylomeDB; Q6NS69; -.
DR TreeFam; TF333006; -.
DR BioGRID-ORCS; 211383; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Amer3; mouse.
DR PRO; PR:Q6NS69; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6NS69; protein.
DR Bgee; ENSMUSG00000045174; Expressed in neural tube marginal layer and 107 other tissues.
DR Genevisible; Q6NS69; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
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..780
FT /note="APC membrane recruitment protein 3"
FT /id="PRO_0000320595"
FT REGION 20..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 83159 MW; 5A625E87A32EAD1D CRC64;
MELRRGKTFI KSSVQISHEK LIDSPAKEDP DKWPLSLGEQ QRAYGEKSSQ TSPCSQGYGR
CPNKEVLSDP EGGPVPLCGT TFKLVRKSKT HDSVPGAVKA AAPTGQMVGS TSFSETPGGQ
RMIDYRHFVP QMPFVPAVAK SIPRKRISLK RSKKCFRNLF HMRRSKTENL ASLSAKGKNL
SPSGVPAQQG TAFLSMGEGL GLDSLCQDLS DSEFLHDSPF DLCSALCEDV ASLKSFDSLT
GCGEIFADGS SVPSVELKDG PESPAHSPQA LDCKTPCGPA QGGMEQLMSP AQNEASDFNK
FWDSVNRSVQ QQQRALMGPW LTSPEGTETD QTRLDTSGLA ELPLFPCRGP PSGSKASSID
TGTPKSEQPE SVSTSDEGYY DSFSPGLEEE KKEAASPGTP AATFPRDSYS GDALYELFYD
PSEAPVGPIL DDDCVSESLS GPALGTPLSM CSFRVGAEEN LAPAPGPDLL SQGFLQSTWK
GKECLLKLCD TELAITMGIV NWLRRTPPAT SPTPASTPAP TPALVLREPA APPDPHRVLR
GASVGVKGRE DQATTCFPPS RQEPWAHSGT KNLLVRECEV LGEPARGSKT PSKDDSLEEG
TQDFSEGQSS SEATMTSISG NNKAVTSATC LSSQKELGTP GNLRYSQGPL RPGHRGSALD
PGPMLVGCVT HVAALQIYPD SNSPRQDKGN GLFWKPQAWG PNILQKNPIS SKPNEAAGCG
LSSSASPQDQ KCRDLFLDLN QLKLEPSRLG PQACSSVDSQ PQQLCPRAPE QVPHRGSVGS
