AMOL1_MOUSE
ID AMOL1_MOUSE Reviewed; 968 AA.
AC Q9D4H4; B9EKN5; Q571F1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Angiomotin-like protein 1;
DE AltName: Full=junction-enriched and -associated protein;
DE Short=JEAP;
GN Name=Amotl1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-968 (ISOFORMS 1/2).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11733531; DOI=10.1074/jbc.m110154200;
RA Nishimura M., Kakizaki M., Ono Y., Morimoto K., Takeuchi M., Inoue Y.,
RA Imai T., Takai Y.;
RT "JEAP, a novel component of tight junctions in exocrine cells.";
RL J. Biol. Chem. 277:5583-5587(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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: Inhibits the Wnt/beta-catenin signaling pathway, probably by
CC recruiting CTNNB1 to recycling endosomes and hence preventing its
CC translocation to the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:11733531}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D4H4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D4H4-2; Sequence=VSP_044080;
CC -!- TISSUE SPECIFICITY: Expressed in exocrine glands, including pancreas,
CC submandibular gland, lacrimal gland, parotid gland and sublingual gland
CC (at protein level). {ECO:0000269|PubMed:11733531}.
CC -!- PTM: Polyubiquitinated by NEDD4, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
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DR EMBL; AK016526; BAB30287.1; -; mRNA.
DR EMBL; CT030247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT485607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151000; AAI51001.1; -; mRNA.
DR EMBL; BC151004; AAI51005.1; -; mRNA.
DR EMBL; BC151007; AAI51008.1; -; mRNA.
DR EMBL; AK220238; BAD90163.1; -; mRNA.
DR CCDS; CCDS40535.1; -. [Q9D4H4-1]
DR RefSeq; NP_001074864.1; NM_001081395.1. [Q9D4H4-1]
DR RefSeq; XP_006510731.1; XM_006510668.1. [Q9D4H4-2]
DR RefSeq; XP_006510732.1; XM_006510669.3. [Q9D4H4-2]
DR RefSeq; XP_006510733.1; XM_006510670.1. [Q9D4H4-2]
DR AlphaFoldDB; Q9D4H4; -.
DR SMR; Q9D4H4; -.
DR BioGRID; 217693; 10.
DR STRING; 10090.ENSMUSP00000013220; -.
DR iPTMnet; Q9D4H4; -.
DR PhosphoSitePlus; Q9D4H4; -.
DR MaxQB; Q9D4H4; -.
DR PaxDb; Q9D4H4; -.
DR PeptideAtlas; Q9D4H4; -.
DR PRIDE; Q9D4H4; -.
DR ProteomicsDB; 296404; -. [Q9D4H4-1]
DR ProteomicsDB; 296405; -. [Q9D4H4-2]
DR Antibodypedia; 654; 132 antibodies from 25 providers.
DR DNASU; 75723; -.
DR Ensembl; ENSMUST00000013220; ENSMUSP00000013220; ENSMUSG00000013076. [Q9D4H4-1]
DR GeneID; 75723; -.
DR KEGG; mmu:75723; -.
DR UCSC; uc009oep.1; mouse. [Q9D4H4-1]
DR CTD; 154810; -.
DR MGI; MGI:1922973; Amotl1.
DR VEuPathDB; HostDB:ENSMUSG00000013076; -.
DR eggNOG; ENOG502QVI5; Eukaryota.
DR GeneTree; ENSGT00940000160158; -.
DR HOGENOM; CLU_009937_1_0_1; -.
DR InParanoid; Q9D4H4; -.
DR PhylomeDB; Q9D4H4; -.
DR TreeFam; TF333368; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 75723; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Amotl1; mouse.
DR PRO; PR:Q9D4H4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D4H4; protein.
DR Bgee; ENSMUSG00000013076; Expressed in manus and 214 other tissues.
DR ExpressionAtlas; Q9D4H4; baseline and differential.
DR Genevisible; Q9D4H4; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IMP:MGI.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:MGI.
DR GO; GO:0035329; P:hippo signaling; IGI:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR009114; Angiomotin.
DR InterPro; IPR024646; Angiomotin_C.
DR Pfam; PF12240; Angiomotin_C; 1.
DR PRINTS; PR01807; ANGIOMOTIN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Phosphoprotein;
KW Reference proteome; Tight junction; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..968
FT /note="Angiomotin-like protein 1"
FT /id="PRO_0000190671"
FT REGION 152..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..291
FT /evidence="ECO:0000255"
FT COILED 449..645
FT /evidence="ECO:0000255"
FT COILED 676..705
FT /evidence="ECO:0000255"
FT COILED 748..773
FT /evidence="ECO:0000255"
FT MOTIF 965..968
FT /note="PDZ-binding"
FT COMPBIAS 152..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044080"
FT CONFLICT 221
FT /note="Missing (in Ref. 2; BAD90163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 107950 MW; 400DCC70DD21E789 CRC64;
MRRAKSRRGP CEPVLRAPPP ICYSPSSPVQ ILEDPAYFYP DLQLYSGRHE ASTLTVEASG
GLRGKSVEDP LSSFHSPNFL RTPEVEMRGS EDVASGRVLQ RLIQEQLRYG TPTENMNLLA
IQHQATGSAG PAHATTNFSS TETLTQEDPQ MVYQSARQEP QGQEHQGDNT VMEKQVRSTQ
PQQNNEELPT YEEAKAQSQF FRGQQQQQQQ QQQQQQQQQQ QGQGPLSHTY YMAGGTSQKS
RTEGRPTVNR ANSGQAHKDE ALKELKQGHV RSLSERIMQL SLERNGAKQH LPSSGNGKSF
KAGGEPSPAQ PVCKALDPRG PPPEYPFKTK PMKSPVSKNQ DHGLYYNDQH PGVLHEMVKP
YPAPQPARTE VAVLRYQPPP EYGVTSRPCQ LPFPSTVQQH SPMSSQTSSI GGTLHSVSLP
LPLPISLAAS QPLPASPNQQ LGPDAFAIVE RAQQMVEILT EENRVLHQEL QGCYDNADKL
HKFEKELQSI SEAYESLVKS TTKRESLDKA MRTKLEGEIR RLHDFNRDLR DRLETANRQL
SSREYDGHED KAAESHYVSQ NKEFLKEKEK LEMELAAVRT ASEDHRRHIE ILDQALSNAQ
ARVIKLEEEL REKQAYVEKV EKLQQALTQL QSACEKRGQM ERRLRTWLER ELDALRTQQK
HGTGPPVSLP ECNAPALMEL VREKEERILA LEADMTKWEQ KYLEESTIRH FAMSAAAAAT
AERDTTISNH SRNGSYGESS LEAHIWPEEE EVVQANRRCQ DMEYTIKNLH AKIIEKDAMI
KVLQQRSRKD AGKTDSASLR PARSVPSIAA ATGTHSRQTS LTSSQLTEEK KEEKTTWKGS
IGFLLGKEHQ GQASAPLLPT TPASALSLPA STTSASSTHA KTGSKDSSTQ TDKSTELFWP
SMASLPSRGR LSTAPSNSPI LKHPAAKGAV EKQENSPGHG KASEHRGRVS NLLHKPEFPD
GEMMEVLI
