AMOT_MOUSE
ID AMOT_MOUSE Reviewed; 1126 AA.
AC Q8VHG2; A2AMJ9; A2AMK0; Q6PFB8; Q6ZPZ1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Angiomotin;
GN Name=Amot; Synonyms=Kiaa1071;
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 183-1126 (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 199-1126 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=B6CBAF2; TISSUE=Placenta;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1126 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Pancreas;
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: Plays a central role in tight junction maintenance via the
CC complex formed with ARHGAP17, which acts by regulating the uptake of
CC polarity proteins at tight junctions. Appears to regulate endothelial
CC cell migration and tube formation. May also play a role in the assembly
CC of endothelial cell-cell junctions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with MAGI1 and angiostatin
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.
CC Note=Localized on the cell surface. May act as a transmembrane protein
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHG2-2; Sequence=VSP_027108, VSP_027109;
CC -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and placenta.
CC {ECO:0000269|PubMed:12406577}.
CC -!- DOMAIN: The angiostatin binding domain (850-1047) allows the binding to
CC angiostatin.
CC -!- DOMAIN: The coiled coil domain interacts directly with the BAR domain
CC of ARHGAP17. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by NEDD4, NEDD4L and ITCH, leading to
CC proteasomal degradation. {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Motus' means 'motility' in Latin.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL73436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM22158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM22159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL807753; CAM22158.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL807753; CAM22159.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC057638; AAH57638.1; ALT_INIT; mRNA.
DR EMBL; AF461135; AAL73436.1; ALT_INIT; mRNA.
DR EMBL; AK129277; BAC98087.1; -; mRNA.
DR CCDS; CCDS72443.1; -. [Q8VHG2-1]
DR RefSeq; NP_001277203.1; NM_001290274.1. [Q8VHG2-2]
DR RefSeq; NP_695231.3; NM_153319.3. [Q8VHG2-1]
DR RefSeq; XP_006528927.1; XM_006528864.3. [Q8VHG2-1]
DR RefSeq; XP_011246130.1; XM_011247828.2. [Q8VHG2-1]
DR AlphaFoldDB; Q8VHG2; -.
DR SMR; Q8VHG2; -.
DR BioGRID; 205274; 18.
DR IntAct; Q8VHG2; 7.
DR STRING; 10090.ENSMUSP00000108455; -.
DR iPTMnet; Q8VHG2; -.
DR PhosphoSitePlus; Q8VHG2; -.
DR MaxQB; Q8VHG2; -.
DR PaxDb; Q8VHG2; -.
DR PeptideAtlas; Q8VHG2; -.
DR PRIDE; Q8VHG2; -.
DR ProteomicsDB; 296203; -. [Q8VHG2-1]
DR ProteomicsDB; 296204; -. [Q8VHG2-2]
DR Antibodypedia; 29579; 455 antibodies from 31 providers.
DR DNASU; 27494; -.
DR Ensembl; ENSMUST00000112836; ENSMUSP00000108455; ENSMUSG00000041688. [Q8VHG2-1]
DR GeneID; 27494; -.
DR KEGG; mmu:27494; -.
DR UCSC; uc009una.2; mouse. [Q8VHG2-1]
DR UCSC; uc009unb.2; mouse. [Q8VHG2-2]
DR CTD; 154796; -.
DR MGI; MGI:108440; Amot.
DR VEuPathDB; HostDB:ENSMUSG00000041688; -.
DR eggNOG; ENOG502QVI5; Eukaryota.
DR GeneTree; ENSGT00940000159055; -.
DR InParanoid; Q8VHG2; -.
DR OMA; NLGPQSD; -.
DR OrthoDB; 369983at2759; -.
DR PhylomeDB; Q8VHG2; -.
DR TreeFam; TF333368; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 27494; 3 hits in 53 CRISPR screens.
DR ChiTaRS; Amot; mouse.
DR PRO; PR:Q8VHG2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8VHG2; protein.
DR Bgee; ENSMUSG00000041688; Expressed in placenta labyrinth and 262 other tissues.
DR ExpressionAtlas; Q8VHG2; baseline and differential.
DR Genevisible; Q8VHG2; MM.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0043532; F:angiostatin binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:MGI.
DR GO; GO:0006935; P:chemotaxis; 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:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0035329; P:hippo signaling; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:MGI.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
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; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Tight junction; Ubl conjugation.
FT CHAIN 1..1126
FT /note="Angiomotin"
FT /id="PRO_0000190669"
FT REGION 22..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..668
FT /evidence="ECO:0000255"
FT COILED 700..730
FT /evidence="ECO:0000255"
FT MOTIF 1123..1126
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 202..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4VCS5"
FT CROSSLNK 574
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4VCS5"
FT VAR_SEQ 805..853
FT /note="VLLGGDYRVEPVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGPESTK ->
FT KEKESNRSKGTVTDLESVLTLLHTARKRDNGPGSREENLESPLSMELDL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027108"
FT VAR_SEQ 854..1126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027109"
FT CONFLICT 298
FT /note="S -> Y (in Ref. 3; AAL73436)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="S -> P (in Ref. 3; AAL73436 and 2; AAH57638)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="M -> I (in Ref. 3; AAL73436 and 2; AAH57638)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..556
FT /note="ENQREKEKLEAELATARSTNEDQRRHIEIRDQ -> FCQPYNPAERKAEVRG
FT GRFTIEAQRGHIKIRAR (in Ref. 3; AAL73436)"
FT /evidence="ECO:0000305"
FT CONFLICT 565..566
FT /note="VV -> W (in Ref. 3; AAL73436)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="I -> M (in Ref. 3; AAL73436)"
FT /evidence="ECO:0000305"
FT CONFLICT 752..754
FT /note="PSK -> RE (in Ref. 3; AAL73436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1126 AA; 120915 MW; 530D84854E943CD4 CRC64;
MRSSDDQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNSSPFST GSGNQGPQND
VLSSQDHHQQ QLVAHPARQE PQGQEIQSEN GVMEKQLSPR MQNNEELPTY EEAKVQSQYF
RGQQHASVGA AFYVTGVTNQ KMRTEGRPSV QRLTPGKMHQ DEGLRDLKQG HVRSLSERLM
QMSLATSGVK AHPPVTSAPL SPPQPNDLYK NATSSSEFYK AQGPPPSQHS LKGMEHRGPP
PEYPFKGVPS QSVVCKSQEP GHFYSEHRLN QPGRTEGQLM RYQHPPEYGA ARATQDISSL
SLSARNSQPH SPTSSLTAGA SSLPLLQSPP STRLPPGQHL VSNQGDHSAH LSRHQQHLLS
SQSHQGDHYR HAQASLTSAQ QQPGEAYSAM PRAQQSASYQ PMPADPFAMV SRAQQMVEIL
SDENRNLRQE LDGCYEKVAR LQKVETEIQR VSEAYENLVK SSSKREALEK AMRNKLEGEI
RRMHDFNRDL RDRLETANKQ LAEKEYEGSE DTRKTISQLF AKHKENQREK EKLEAELATA
RSTNEDQRRH IEIRDQALSN AQAKVVKLEE ELKKKQVYVD KVEKMQQALV QLQAACEKRE
QLEHRLRTRL ERELESLRIQ QRQGNSQPTN ASEYNAAALM ELLREKEERI LALEADMTKW
EQKYLEENVM RHFALDAAAT VAAQRDTTVI SHSPNTSYDT ALEARIQKEE EEILMANKRC
LDMEGRIKTL HAQIIEKDAM IKVLQQRSRK EPSKTEQLSS MRPAKSLMSI SNAGSGLLAH
SSTLTGAPIM EEKRDDKSWK GSLGVLLGGD YRVEPVPSTP SPVPPSTPLL SAHSKTGSRD
CSTQTERGPE STKTAAVTPI SAPMAGPVAA AAPAAAINAT AATNTATAAT NTTIMVAAAP
VAVAAVAAPA AAAATPSPAN AAALAAAAAP ATSVSAATSV SAANSISPAA PVAPAAVVPP
AAPVSPAAAV QIPAAASLTP ATVSPTAATA TAAVAAATTA AITAAAAAAT TAIQVAPATS
APVPSPASIP APATAQASAP TPTQASTPAP TEPPSPVPTP TPALVQTEGP ANPGASSGPR
RLSTPNLMCN PDKPDAPAFH SSTLERKTPI QILGQEPDAE MVEYLI
