AMOL2_MOUSE
ID AMOL2_MOUSE Reviewed; 772 AA.
AC Q8K371; B8JK80; Q3TPM1; Q7TPE4; Q8BP84; Q8BS08; Q9QUS0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Angiomotin-like protein 2;
GN Name=Amotl2;
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=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).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 187-772.
RC TISSUE=Glioblastoma;
RX PubMed=12406577; DOI=10.1016/s0378-1119(02)00928-9;
RA Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA Holmgren L.;
RT "Angiomotin belongs to a novel protein family with conserved coiled-coil
RT and PDZ binding domains.";
RL Gene 298:69-77(2002).
RN [6]
RP ERRATUM OF PUBMED:12406577.
RA Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA Holmgren L.;
RL Gene 310:231-231(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752 AND SER-755, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Regulates the translocation of phosphorylated SRC to
CC peripheral cell-matrix adhesion sites. Required for proper architecture
CC of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway,
CC probably by recruiting CTNNB1 to recycling endosomes and hence
CC preventing its translocation to the nucleus. Participates in
CC angiogenesis. May play a role in the polarity, proliferation and
CC migration of endothelial cells. Selectively promotes FGF-induced MAPK
CC activation through SRC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SRC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-107 is necessary for efficient binding to
CC SRC and synergistically functioning with SRC to activate the downstream
CC MAPK pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30740.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36853.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK040912; BAC30740.1; ALT_INIT; mRNA.
DR EMBL; AK077535; BAC36853.1; ALT_FRAME; mRNA.
DR EMBL; AK141348; BAE24658.1; -; mRNA.
DR EMBL; AK164279; BAE37715.1; -; mRNA.
DR EMBL; CT573150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466560; EDL21058.1; -; Genomic_DNA.
DR EMBL; BC027824; AAH27824.1; -; mRNA.
DR EMBL; AF175967; AAD56362.2; -; mRNA.
DR EMBL; AF175968; AAD56363.1; -; mRNA.
DR CCDS; CCDS40745.1; -.
DR RefSeq; NP_062738.2; NM_019764.2.
DR RefSeq; XP_006511834.2; XM_006511771.3.
DR RefSeq; XP_006511836.1; XM_006511773.2.
DR AlphaFoldDB; Q8K371; -.
DR SMR; Q8K371; -.
DR BioGRID; 207908; 7.
DR IntAct; Q8K371; 1.
DR STRING; 10090.ENSMUSP00000035121; -.
DR iPTMnet; Q8K371; -.
DR PhosphoSitePlus; Q8K371; -.
DR jPOST; Q8K371; -.
DR MaxQB; Q8K371; -.
DR PaxDb; Q8K371; -.
DR PRIDE; Q8K371; -.
DR ProteomicsDB; 296406; -.
DR Antibodypedia; 33394; 108 antibodies from 22 providers.
DR DNASU; 56332; -.
DR Ensembl; ENSMUST00000035121; ENSMUSP00000035121; ENSMUSG00000032531.
DR GeneID; 56332; -.
DR KEGG; mmu:56332; -.
DR UCSC; uc009rfx.1; mouse.
DR CTD; 51421; -.
DR MGI; MGI:1929286; Amotl2.
DR VEuPathDB; HostDB:ENSMUSG00000032531; -.
DR eggNOG; ENOG502QR7W; Eukaryota.
DR GeneTree; ENSGT00940000156577; -.
DR InParanoid; Q8K371; -.
DR OrthoDB; 369983at2759; -.
DR PhylomeDB; Q8K371; -.
DR TreeFam; TF333368; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 56332; 7 hits in 70 CRISPR screens.
DR ChiTaRS; Amotl2; mouse.
DR PRO; PR:Q8K371; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K371; protein.
DR Bgee; ENSMUSG00000032531; Expressed in vault of skull and 249 other tissues.
DR ExpressionAtlas; Q8K371; baseline and differential.
DR Genevisible; Q8K371; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IBA:GO_Central.
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 Coiled coil; Endosome; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..772
FT /note="Angiomotin-like protein 2"
FT /id="PRO_0000190673"
FT REGION 41..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 305..578
FT /evidence="ECO:0000255"
FT MOTIF 769..772
FT /note="PDZ-binding"
FT COMPBIAS 61..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphotyrosine; by FGFR1"
FT /evidence="ECO:0000250"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 163..165
FT /note="LLQ -> ILK (in Ref. 1; BAC36853)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..197
FT /note="QLARSQQGPQP -> EPPGFLGDRST (in Ref. 5; AAD56362)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Q -> H (in Ref. 5; AAD56362)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="D -> N (in Ref. 1; BAC36853)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="H -> N (in Ref. 1; BAC36853)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="K -> R (in Ref. 5; AAD56362/AAD56363)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="L -> P (in Ref. 5; AAD56362/AAD56363)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="R -> W (in Ref. 5; AAD56362/AAD56363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 85278 MW; 9979F5F4D2A54989 CRC64;
MRTLEDSSGT VLHRLIQEQL RYGNLTETRT LLAIQQQALR GGAGAGGTGS PQASLEIGAP
EDSQVLQQAT RQEPQGQEHQ GGETHLAENR LYRLCPQPSK GEELPTYEEA KAHSQYYAAQ
QAGSRPHVGD RDPRGGVSGG GRRQDEALRE LRHGHVRSLS ERLLQLSLER NGARVPSHMS
SSHSFPQLAR SQQGPQPRGP PAEGPEPRGP PPQYPHAVMA QETAAVTDPR YRPRSSPHFQ
HAEVRILQAQ VPPVFLQQQQ YQYLPQPQEH SPPLHPAALG HGPPSSFGPP AVEGPPSAQA
TLGSAHLAQM ETVLRENARL QRDNERLQRE LESTSEKAGR IEKLENEIQR LSEAHESLMR
TSSKREALEK TMRNKMDGEM RRLQDFNRDL RERLESANRH LASKTQEAQA GSQDMVAKLL
AQSYEQQQEQ EKLEREMALL RGAIEDQRRH AELLEQALGN AQSRAARAEE ELRKKQAYVE
KVERLQQALG QLQAACEKRE QLELRLRTRL EQELKALRAQ QRQTGTLAGG GGSHGGSAEL
SALRLSEQLR EKEEQILALE ADMTKWEQKY LEERAMRQFA MDAAATAAAQ RDTTLIRHSP
QPSPSSSFNE GLLPGNHRHQ EMESRLKVLH AQILEKDAVI KVLQQRSRKD PGKATQGTLR
PAKSVPSIFA AAVGTQGWQG LVSSERQTDA RPAGDRVPAE EPPATAPLPA HTKHGSRDGS
TQTDGPADNT SACLASEPDG LLGCNSSQRT PSLDSIAATR VQDLSDMVEI LI
