Q5IS48 (DVL1_PANTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Segment polarity protein dishevelled homolog DVL-1
Short name=Dishevelled-1

Alternative name(s):
DSH homolog 1

Gene names

Name:

DVL1

Organism

Pan troglodytes (Chimpanzee) [Reference proteome]

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Pan

Protein attributes

Sequence length	670 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) By similarity.
Subunit structure	Interacts with BRD7 and INVS. Interacts through its PDZ domain with the C-terminal regions of VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts with CXXC4. Interacts (via PDZ domain) with NXN. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1. Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same binding site. Interacts (via DEP domain) with MUSK; the interaction is direct and mediates the formation a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Interacts (via PDZ domain) with TMEM88 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytosol By similarity. Cytoplasmic vesicle By similarity. Note: Localizes at the cell membrane upon interaction with frizzled family members By similarity.
Domain	The DIX domain promotes homooligomerization By similarity. The DEP domain mediates interaction with the cell membrane By similarity.
Post-translational modification	Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains By similarity.
Sequence similarities	Belongs to the DSH family. Contains 1 DEP domain. Contains 1 DIX domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Membrane
Molecular function	Developmental protein
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon extension Inferred from Biological aspect of Ancestor. Source: RefGenome axon guidance Inferred from Biological aspect of Ancestor. Source: RefGenome canonical Wnt signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome cochlea morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome collateral sprouting Inferred from Biological aspect of Ancestor. Source: RefGenome convergent extension Inferred from Biological aspect of Ancestor. Source: RefGenome convergent extension involved in neural plate elongation Inferred from electronic annotation. Source: Ensembl cytoplasmic microtubule organization Inferred from electronic annotation. Source: Ensembl dendrite morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome intracellular signal transduction Inferred from electronic annotation. Source: InterPro negative regulation of protein binding Inferred from electronic annotation. Source: Ensembl negative regulation of protein kinase activity Inferred from electronic annotation. Source: Ensembl neural tube development Inferred from electronic annotation. Source: Ensembl neurotransmitter secretion Inferred from electronic annotation. Source: Ensembl planar cell polarity pathway involved in neural tube closure Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of canonical Wnt signaling pathway Inferred from electronic annotation. Source: Ensembl positive regulation of neuron projection development Inferred from electronic annotation. Source: Ensembl positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Ensembl positive regulation of transcription, DNA-templated Inferred from Biological aspect of Ancestor. Source: RefGenome prepulse inhibition Inferred from electronic annotation. Source: Ensembl protein localization to microtubule Inferred from electronic annotation. Source: Ensembl protein localization to nucleus Inferred from electronic annotation. Source: Ensembl regulation of signaling Inferred from Biological aspect of Ancestor. Source: RefGenome skeletal muscle acetylcholine-gated channel clustering Inferred from Biological aspect of Ancestor. Source: RefGenome social behavior Inferred from electronic annotation. Source: Ensembl transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl
Cellular_component	axon Inferred from Biological aspect of Ancestor. Source: RefGenome cell cortex Inferred from Biological aspect of Ancestor. Source: RefGenome clathrin-coated vesicle Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from Biological aspect of Ancestor. Source: RefGenome growth cone Inferred from Biological aspect of Ancestor. Source: RefGenome lateral plasma membrane Inferred from electronic annotation. Source: Ensembl microtubule Inferred from Biological aspect of Ancestor. Source: RefGenome neuronal cell body Inferred from Biological aspect of Ancestor. Source: RefGenome synapse Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	Rac GTPase binding Inferred from Biological aspect of Ancestor. Source: RefGenome frizzled binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 670	670	Segment polarity protein dishevelled homolog DVL-1		PRO_0000145744
Regions
	Domain	1 – 85	85	DIX
	Domain	251 – 323	73	PDZ
	Domain	400 – 474	75	DEP
	Compositional bias	221 – 224	4	Poly-Arg

Sequences

	Sequence		Length	Mass (Da)
	Q5IS48 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: DA314641C8453F07	FASTA	670	72,851
	10 20 30 40 50 60 MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK 70 80 90 100 110 120 EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF 130 140 150 160 170 180 HPNVASSRDG MDNETGTESM VSHRRERARR RNREEAARTN GHPRGDRRRD VGLPPDSAST 190 200 210 220 230 240 ALSSELESSS FVDSDEDGST SRLSSSTEQS TSSRLIRKHK RRRRKQRLRQ ADRASSFSSI 250 260 270 280 290 300 TDSTMSLNIV TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM 310 320 330 340 350 360 LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTVP RADPVRPIDP 370 380 390 400 410 420 AAWLSHTAAL TGALPRYELE EAPLTVKSDM SAVVRVMQLP DSGLEIRDRM WLKITIANAV 430 440 450 460 470 480 IGADVVDWLY THVEGFKERR EARKYASSLL KHGFLRHTVN KITFSEQCYY VFGDLCSNLA 490 500 510 520 530 540 TLNLNSGSSG ASDQDTLAPL PHPAAPWPLG QGYPYQYPGP PPCFPPAYQD PGFSYGSGST 550 560 570 580 590 600 GSQQSEGSKS SGSTRSSRRA PGREKERRAA GAGGSGSESD HTAPSGVGSS WRERPAGQLS 610 620 630 640 650 660 RGSSPRSQAS ATAPGLPPPH PTTKAYTVVG GPPGGPPVRE LAAVPPELTG SRQSFQKAMG 670 NPCEFFVDIM

References

[1]	"Accelerated evolution of nervous system genes in the origin of Homo sapiens." Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T. Cell 119:1027-1040(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY665280 mRNA. Translation: AAV74318.1.
RefSeq	NP_001012432.1. NM_001012430.1.
UniGene	Ptr.6576.
3D structure databases
ProteinModelPortal	Q5IS48.
SMR	Q5IS48. Positions 251-345, 381-474.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	9598.ENSPTRP00000052962.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	457191.
KEGG	ptr:457191.
Organism-specific databases
CTD	1855.
Phylogenomic databases
eggNOG	NOG322275.
HOGENOM	HOG000017084.
HOVERGEN	HBG005542.
KO	K02353.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 2.30.42.10. 1 hit.
InterPro	IPR000591. DEP_dom. IPR008340. Dishevelled_1. IPR024580. Dishevelled_C-dom. IPR008339. Dishevelled_fam. IPR003351. Dishevelled_protein_dom. IPR001158. DIX. IPR015506. Dsh/Dvl-rel. IPR001478. PDZ. IPR029071. Ubiquitin-rel_dom. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
PANTHER	PTHR10878. PTHR10878. 1 hit. PTHR10878:SF5. PTHR10878:SF5. 1 hit.
Pfam	PF00610. DEP. 1 hit. PF02377. Dishevelled. 1 hit. PF00778. DIX. 1 hit. PF12316. Dsh_C. 1 hit. PF00595. PDZ. 1 hit. [Graphical view]
PRINTS	PR01760. DISHEVELLED.
SMART	SM00021. DAX. 1 hit. SM00049. DEP. 1 hit. SM00228. PDZ. 1 hit. [Graphical view]
SUPFAM	SSF50156. SSF50156. 1 hit. SSF54236. SSF54236. 1 hit.
PROSITE	PS50186. DEP. 1 hit. PS50841. DIX. 1 hit. PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20838055.

Entry information

Entry name

DVL1_PANTR

Accession

Primary (citable) accession number: Q5IS48

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	February 15, 2005
Last modified:	June 11, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program