Q4VCS5 (AMOT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiomotin

Gene names

Name:	AMOT
Synonyms:	KIAA1071

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1084 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. Ref.1 Ref.6
Subunit structure	Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with MAGI1. Isoform 1 interacts with angiostatin. Ref.2
Subcellular location	Cell junction › tight junction. Note: Localized on the cell surface. May act as a transmembrane protein. Ref.2
Tissue specificity	Expressed in placenta and skeletal muscle. Found in the endothelial cells of capillaries as well as larger vessels of the placenta. Ref.1
Domain	The coiled coil domain interacts directly with the BAR domain of ARHGAP17. Ref.6 The angiostatin binding domain (871-1005) allows the binding to angiostatin. Ref.6
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9
Miscellaneous	'Motus' means 'motility' in Latin.
Sequence similarities	Belongs to the angiomotin family.
Sequence caution	The sequence AAH94712.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cell junction Tight junction
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Traceable author statement Ref.2. Source: UniProtKB cell-cell junction assembly Traceable author statement Ref.2. Source: UniProtKB negative regulation of angiogenesis Inferred from direct assay Ref.1. Source: MGI negative regulation of vascular permeability Inferred from direct assay Ref.2. Source: UniProtKB positive regulation of blood vessel endothelial cell migration Inferred from direct assay Ref.2. Source: UniProtKB positive regulation of cell size Traceable author statement Ref.2. Source: UniProtKB positive regulation of stress fiber assembly Traceable author statement Ref.2. Source: UniProtKB regulation of cell migration Inferred from direct assay Ref.1. Source: MGI
Cellular component	actin filament Inferred from direct assay Ref.1. Source: UniProtKB cell surface Inferred from direct assay Ref.2. Source: UniProtKB cytoplasm Inferred from direct assay Ref.2. Source: UniProtKB endocytic vesicle Inferred from direct assay Ref.1. Source: MGI external side of plasma membrane Inferred from direct assay Ref.1. Source: MGI integral to membrane Inferred from direct assay Ref.2. Source: UniProtKB lamellipodium Inferred from direct assay Ref.1. Source: UniProtKB ruffle Inferred from direct assay Ref.1. Source: MGI stress fiber Inferred from direct assay Ref.2. Source: UniProtKB tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	angiostatin binding Inferred from direct assay Ref.1Ref.2. Source: UniProtKB protein binding Inferred from physical interaction Ref.2. Source: UniProtKB receptor activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGAP17	Q68EM7	2	EBI-2511319,EBI-1642807
NF2	P35240	6	EBI-2511319,EBI-1014472

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q4VCS5-1)

Also known as: p130;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q4VCS5-2)

Also known as: p80;

The sequence of this isoform differs from the canonical sequence as follows:
     1-409: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1084	1084	Angiomotin		PRO_0000190668
Regions
	Coiled coil	429 – 689	261	Potential
	Coiled coil	721 – 751	31	Potential
	Motif	1081 – 1084	4	PDZ-binding
Amino acid modifications
	Modified residue	305	1	Phosphoserine Ref.8
	Modified residue	312	1	Phosphoserine Ref.8
	Modified residue	712	1	Phosphoserine By similarity
	Modified residue	714	1	Phosphoserine Ref.9
	Modified residue	717	1	Phosphothreonine Ref.9
	Modified residue	719	1	Phosphotyrosine Ref.9
	Modified residue	1061	1	Phosphothreonine Ref.7
Natural variations
	Alternative sequence	1 – 409	409	Missing in isoform 2.		VSP_015709

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p130) [UniParc]. Last modified July 5, 2005. Version 1. Checksum: D7E7021E9535A628	FASTA	1,084	118,085
	10 20 30 40 50 60 MRNSEEQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNGPPFPS GSGNPGPQSD 70 80 90 100 110 120 VLSPQDHHQQ LVAHAARQEP QGQEIQSENL IMEKQLSPRM QNNEELPTYE EAKVQSQYFR 130 140 150 160 170 180 GQQHASVGAA FYVTGVTNQK MRTEGRPSVQ RLNPGKMHQD EGLRDLKQGH VRSLSERLMQ 190 200 210 220 230 240 MSLATSGVKA HPPVTSAPLS PPQPNDLYKN PTSSSEFYKA QGPLPNQHSL KGMEHRGPPP 250 260 270 280 290 300 EYPFKGMPPQ SVVCKPQEPG HFYSEHRLNQ PGRTEGQLMR YQHPPEYGAA RPAQDISLPL 310 320 330 340 350 360 SARNSQPHSP TSSLTSGGSL PLLQSPPSTR LSPARHPLVP NQGDHSAHLP RPQQHFLPNQ 370 380 390 400 410 420 AHQGDHYRLS QPGLSQQQQQ QQQQHHHHHH HQQQQQQQPQ QQPGEAYSAM PRAQPSSASY 430 440 450 460 470 480 QPVPADPFAI VSRAQQMVEI LSDENRNLRQ ELEGCYEKVA RLQKVETEIQ RVSEAYENLV 490 500 510 520 530 540 KSSSKREALE KAMRNKLEGE IRRMHDFNRD LRERLETANK QLAEKEYEGS EDTRKTISQL 550 560 570 580 590 600 FAKNKESQRE KEKLEAELAT ARSTNEDQRR HIEIRDQALS NAQAKVVKLE EELKKKQVYV 610 620 630 640 650 660 DKVEKMQQAL VQLQAACEKR EQLEHRLRTR LERELESLRI QQRQGNCQPT NVSEYNAAAL 670 680 690 700 710 720 MELLREKEER ILALEADMTK WEQKYLEENV MRHFALDAAA TVAAQRDTTV ISHSPNTSYD 730 740 750 760 770 780 TALEARIQKE EEEILMANKR CLDMEGRIKT LHAQIIEKDA MIKVLQQRSR KEPSKTEQLS 790 800 810 820 830 840 CMRPAKSLMS ISNAGSGLLS HSSTLTGSPI MEEKRDDKSW KGSLGILLGG DYRAEYVPST 850 860 870 880 890 900 PSPVPPSTPL LSAHSKTGSR DCSTQTERGT ESNKTAAVAP ISVPAPVAAA ATAAAITATA 910 920 930 940 950 960 ATITTTMVAA APVAVAAAAA PAAAAAPSPA TAAATAAAVS PAAAGQIPAA ASVASAAAVA 970 980 990 1000 1010 1020 PSAAAAAAVQ VAPAAPAPVP APALVPVPAP AAAQASAPAQ TQAPTSAPAV APTPAPTPTP 1030 1040 1050 1060 1070 1080 AVAQAEVPAS PATGPGPHRL SIPSLTCNPD KTDGPVFHSN TLERKTPIQI LGQEPDAEMV EYLI
	Isoform 2 (p80) [UniParc]. Checksum: EBC28B74427AD481	FASTA	675	72,540
	10 20 30 40 50 60 MPRAQPSSAS YQPVPADPFA IVSRAQQMVE ILSDENRNLR QELEGCYEKV ARLQKVETEI 70 80 90 100 110 120 QRVSEAYENL VKSSSKREAL EKAMRNKLEG EIRRMHDFNR DLRERLETAN KQLAEKEYEG 130 140 150 160 170 180 SEDTRKTISQ LFAKNKESQR EKEKLEAELA TARSTNEDQR RHIEIRDQAL SNAQAKVVKL 190 200 210 220 230 240 EEELKKKQVY VDKVEKMQQA LVQLQAACEK REQLEHRLRT RLERELESLR IQQRQGNCQP 250 260 270 280 290 300 TNVSEYNAAA LMELLREKEE RILALEADMT KWEQKYLEEN VMRHFALDAA ATVAAQRDTT 310 320 330 340 350 360 VISHSPNTSY DTALEARIQK EEEEILMANK RCLDMEGRIK TLHAQIIEKD AMIKVLQQRS 370 380 390 400 410 420 RKEPSKTEQL SCMRPAKSLM SISNAGSGLL SHSSTLTGSP IMEEKRDDKS WKGSLGILLG 430 440 450 460 470 480 GDYRAEYVPS TPSPVPPSTP LLSAHSKTGS RDCSTQTERG TESNKTAAVA PISVPAPVAA 490 500 510 520 530 540 AATAAAITAT AATITTTMVA AAPVAVAAAA APAAAAAPSP ATAAATAAAV SPAAAGQIPA 550 560 570 580 590 600 AASVASAAAV APSAAAAAAV QVAPAAPAPV PAPALVPVPA PAAAQASAPA QTQAPTSAPA 610 620 630 640 650 660 VAPTPAPTPT PAVAQAEVPA SPATGPGPHR LSIPSLTCNP DKTDGPVFHS NTLERKTPIQ 670 ILGQEPDAEM VEYLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Angiomotin. An angiostatin binding protein that regulates endothelial cell migration and tube formation." Troyanovsky B., Levchenko T., Maensson G., Matvijenko O., Holmgren L. J. Cell Biol. 152:1247-1254(2001) [PubMed: 11257124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION. Tissue: Placenta.
[2]	"Angiomotin regulates endothelial cell-cell junctions and cell motility." Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., Holmgren L. J. Biol. Chem. 280:34859-34869(2005) [PubMed: 16043488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TOPOLOGY, INTERACTION WITH ANGIOSTATIN AND MAGI1, SUBCELLULAR LOCATION.
[3]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 (ISOFORM 1). Tissue: Spinal cord.
[6]	"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells." Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T. Cell 125:535-548(2006) [PubMed: 16678097] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, FUNCTION, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; MPP5; INADL AND PARD3.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1061, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-312, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; THR-717 AND TYR-719, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF286598 mRNA. Translation: AAG01851.1. AY987378 mRNA. Translation: AAY24451.1. AB028994 mRNA. Translation: BAA83023.3. BC094712 mRNA. Translation: AAH94712.1. Sequence problems.
IPI	IPI00163085. IPI00644547.
RefSeq	NP_001106962.1. NM_001113490.1. NP_573572.1. NM_133265.2.
UniGene	Hs.528051.
3D structure databases
ProteinModelPortal	Q4VCS5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q4VCS5. 36 interactions.
STRING	Q4VCS5.
PTM databases
PhosphoSite	Q4VCS5.
Polymorphism databases
DMDM	74753814.
Proteomic databases
PRIDE	Q4VCS5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371959; ENSP00000361027; ENSG00000126016.
GeneID	154796.
KEGG	hsa:154796.
UCSC	uc004epr.1. human. uc004eps.1. human.
Organism-specific databases
CTD	154796.
GeneCards	GC0XM112017.
HGNC	HGNC:17810. AMOT.
MIM	300410. gene.
neXtProt	NX_Q4VCS5.
PharmGKB	PA24773.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063846.
HOGENOM	HBG445905.
HOVERGEN	HBG066485.
InParanoid	Q4VCS5.
OMA	WKGSLGI.
PhylomeDB	Q4VCS5.
Gene expression databases
ArrayExpress	Q4VCS5.
Bgee	Q4VCS5.
CleanEx	HS_AMOT.
Genevestigator	Q4VCS5.
GermOnline	ENSG00000126016. Homo sapiens.
Family and domain databases
InterPro	IPR009114. Angiomotin. IPR024646. Angiomotin_C. [Graphical view]
PANTHER	PTHR14826. Angiomotin. 1 hit.
Pfam	PF12240. Angiomotin_C. 1 hit. [Graphical view]
PRINTS	PR01807. ANGIOMOTIN.
ProtoNet	Search...
Other
NextBio	87314.
SOURCE	Search...

Entry information

Entry name

AMOT_HUMAN

Accession

Primary (citable) accession number: Q4VCS5
Secondary accession number(s): Q504X5, Q9HD27, Q9UPT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	July 5, 2005
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.