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Q8BKG3 (PTK7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive tyrosine-protein kinase 7
Alternative name(s):
Protein chuzhoi
Protein-tyrosine kinase 7
Pseudo tyrosine kinase receptor 7
Tyrosine-protein kinase-like 7
Gene names
Name:Ptk7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1062 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. Ref.5 Ref.8 Ref.9

Subunit structure

Interacts with CTNNB1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein. Cell junction By similarity. Note: Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.

Tissue specificity

Expressed at high levels in lung and un-pregnant uterus among adult tissues, and in the tail, limbs, somites, gut and craniofacial regions among embryonic tissues. Ref.1

Domain

The protein kinase domain is predicted to be catalytically inactive.

Post-translational modification

MMP14 cleaves PTK7 between Pro-613 and Leu-614 generating an N-terminal soluble (70 kDa) fragment and a membrane C-terminal (50 kDa) fragment By similarity. Proteolysis by MMP14 regulates PTK7 function in non-canonical Wnt signaling pathway By similarity.

Disruption phenotype

Mice die perinatally and display craniorachischisis, a severe form of neural tube defect in which the neural tube fails to close from the midbrain hindbrain boundary to the base of the spine. Chuzhoi mutants also display disruption of planar cell polarity in the inner ear, and defective heart and lung development. Ref.5 Ref.8 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAH27800.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell adhesion
Wnt signaling pathway
   Cellular componentCell junction
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from electronic annotation. Source: Ensembl

axis elongation

Inferred from mutant phenotype Ref.9. Source: MGI

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cochlea morphogenesis

Inferred from mutant phenotype Ref.9. Source: MGI

convergent extension

Inferred from mutant phenotype Ref.9. Source: MGI

establishment of epithelial cell apical/basal polarity

Inferred from mutant phenotype Ref.5. Source: MGI

establishment of planar polarity

Inferred from mutant phenotype Ref.9. Source: MGI

lung-associated mesenchyme development

Inferred from mutant phenotype Ref.9. Source: MGI

neural tube closure

Inferred from mutant phenotype Ref.5Ref.9. Source: MGI

planar cell polarity pathway involved in neural tube closure

Inferred from genetic interaction Ref.9. Source: MGI

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from genetic interaction PubMed 20643356. Source: MGI

   Cellular_componentcell-cell junction

Inferred from direct assay PubMed 20215345. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay Ref.9. Source: MGI

plasma membrane

Inferred from direct assay PubMed 20215345. Source: MGI

   Molecular_functiontransferase activity, transferring phosphorus-containing groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10621040Inactive tyrosine-protein kinase 7
PRO_0000260435

Regions

Topological domain23 – 696674Extracellular Potential
Transmembrane697 – 71721Helical; Potential
Topological domain718 – 1062345Cytoplasmic Potential
Domain23 – 11290Ig-like C2-type 1
Domain120 – 21091Ig-like C2-type 2
Domain217 – 30993Ig-like C2-type 3
Domain301 – 39999Ig-like C2-type 4
Domain404 – 48986Ig-like C2-type 5
Domain495 – 57884Ig-like C2-type 6
Domain570 – 672103Ig-like C2-type 7
Domain788 – 1058271Protein kinase; inactive
Region786 – 1062277Interaction with CTNNB1 By similarity

Sites

Site613 – 6142Cleavage; by MMP14 By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Ref.7
Glycosylation1081N-linked (GlcNAc...) Ref.6
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Ref.7
Glycosylation3971N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5591N-linked (GlcNAc...) Ref.7
Glycosylation6381N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 93 By similarity
Disulfide bond142 ↔ 192 By similarity
Disulfide bond238 ↔ 293 By similarity
Disulfide bond335 ↔ 383 By similarity
Disulfide bond425 ↔ 473 By similarity
Disulfide bond516 ↔ 562 By similarity
Disulfide bond605 ↔ 656 By similarity

Experimental info

Sequence conflict8181L → R in BAC53806. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8BKG3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 138E25198A21E6A1

FASTA1,062117,532
        10         20         30         40         50         60 
MGARPLTLLR ALLLPLLAGA QAAIVFIKEP SSQDALQGRR ALLRCEVEAP DPVHVYWLLN 

        70         80         90        100        110        120 
GVPVQDTERR FAQGSSLSFA AVDRLQDSGA FQCVARDNVT GEEVRSTNAS FNIKWIEAGP 

       130        140        150        160        170        180 
VVLKHPASEA EIQPQTQVTL RCHIDGHPRP TYQWFRDGTP LSDDQSTHTV SSRERNLTLR 

       190        200        210        220        230        240 
PASPEHSGLY SCCAHNAFGQ ACSSQNFTLS VADESFARVV LAPQDVVVAR NEEAMFHCQF 

       250        260        270        280        290        300 
SAQPPPSLQW VFEDETPITN RSRPPHLRRA VVFANGSLLL TQVRPRNAGV YRCIGQGQRG 

       310        320        330        340        350        360 
PPIVLEATLH LAEIEDMLPF EPRVFIAGDE ERVTCPAPQG LPTPSVWWEH AGVPLPAHGR 

       370        380        390        400        410        420 
VHQKGLELVF VTIAESDTGV YTCHASNLAG QRRQDVNITV ATVPTWLRKP QDSQLEEGKP 

       430        440        450        460        470        480 
GYLHCLTQAT PKPTVIWYRN QMLISEDSRF EVSKNGTLRI NSVEVYDGTL YRCVSSTPAG 

       490        500        510        520        530        540 
SIEAQARVQV LEKLKFTPPP QPQQCMEFDK EATVPCSATG REKPTVKWVR ADGSSLPEWV 

       550        560        570        580        590        600 
TDNAGTLHFA RVTRDDAGNY TCIASNEPQG QIRAHVQLTV AVFITFKVEP ERTTVYQGHT 

       610        620        630        640        650        660 
ALLRCEAQGD PKPLIQWKGK DRILDPTKLG PRMHIFQNGS LVIHDVAPED SGSYTCIAGN 

       670        680        690        700        710        720 
SCNIRHTEAP LLVVDKPVME DSEGPGSPPP YKMIQTIGLS VGAAVAYIIA VLGLMFYCKK 

       730        740        750        760        770        780 
RCKAKRLQKQ PEGEEPEMEC LNGGPLQNGQ PSAEIQEEVA LTSLGSGPPA TNKRHSAGDR 

       790        800        810        820        830        840 
MHFPRASLQP ITTLGKSEFG EVFLAKAQGV EEGATETLVL VKSLQSRDEQ QQLDFRREVE 

       850        860        870        880        890        900 
MFGKLNHANV VRLLGLCREA EPHYMVLEYV DLGDLKQFLR ISKNKDEKLK SQPLSTKQKV 

       910        920        930        940        950        960 
ALCSQVALGM EHLSNNRFVH KDLAARNCLI SAQRQVKVSA LGLSKDVYNS EYYHFRQAWV 

       970        980        990       1000       1010       1020 
PLRWMSPEAV LEGDFSTKSD VWAFGVLMWE VFTHGEMPHG GQADDEVLAD LQAGKARLPQ 

      1030       1040       1050       1060 
PEGCPSKLYR LMQRCWAPNP KDRPSFSEIA STLGDSPADS KQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the full-length mouse Ptk7 cDNA encoding a defective receptor protein tyrosine kinase."
Jung J.-W., Shin W.S., Song J., Lee S.-T.
Gene 328:75-84(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Strain: BALB/c and C57BL/6.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Lung.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary tumor.
[4]"Isolation and characterization of novel human and mouse genes, which are expressed in the digestive tract."
Daigo Y., Takayama I., Fujino M.A.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 774-1062.
Strain: W/Wv.
[5]"PTK7/CCK-4 is a novel regulator of planar cell polarity in vertebrates."
Lu X., Borchers A.G.M., Jolicoeur C., Rayburn H., Baker J.C., Tessier-Lavigne M.
Nature 430:93-98(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108 AND ASN-397.
Tissue: Myoblast.
[7]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98; ASN-275; ASN-397 AND ASN-559.
[8]"PTK7 is essential for polarized cell motility and convergent extension during mouse gastrulation."
Yen W.W., Williams M., Periasamy A., Conaway M., Burdsal C., Keller R., Lu X., Sutherland A.
Development 136:2039-2048(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"The novel mouse mutant, chuzhoi, has disruption of Ptk7 protein and exhibits defects in neural tube, heart and lung development and abnormal planar cell polarity in the ear."
Paudyal A., Damrau C., Patterson V.L., Ermakov A., Formstone C., Lalanne Z., Wells S., Lu X., Norris D.P., Dean C.H., Henderson D.J., Murdoch J.N.
BMC Dev. Biol. 10:87-87(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF531873 mRNA. Translation: AAQ10071.1.
AY303976 Genomic DNA. Translation: AAQ73496.1.
AK018379 mRNA. Translation: BAE43251.1.
AK053044 mRNA. Translation: BAC35248.1.
AK163135 mRNA. Translation: BAE37208.1.
BC027800 mRNA. Translation: AAH27800.1. Different initiation.
BC076578 mRNA. Translation: AAH76578.1.
AB055408 mRNA. Translation: BAC53806.1.
CCDSCCDS37637.1.
RefSeqNP_780377.1. NM_175168.4.
UniGeneMm.181833.

3D structure databases

ProteinModelPortalQ8BKG3.
SMRQ8BKG3. Positions 26-674, 794-1046.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BKG3. 1 interaction.
MINTMINT-4111157.
STRING10090.ENSMUSP00000043703.

PTM databases

PhosphoSiteQ8BKG3.

Proteomic databases

MaxQBQ8BKG3.
PaxDbQ8BKG3.
PRIDEQ8BKG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044442; ENSMUSP00000043703; ENSMUSG00000023972.
GeneID71461.
KEGGmmu:71461.
UCSCuc008cth.2. mouse.

Organism-specific databases

CTD5754.
MGIMGI:1918711. Ptk7.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117404.
HOGENOMHOG000115767.
HOVERGENHBG008320.
InParanoidQ8BKG3.
KOK05127.
OMADGTWYRC.
OrthoDBEOG790G1M.
PhylomeDBQ8BKG3.
TreeFamTF326835.

Gene expression databases

ArrayExpressQ8BKG3.
BgeeQ8BKG3.
CleanExMM_PTK7.
GenevestigatorQ8BKG3.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07679. I-set. 5 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 6 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 7 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio333833.
PROQ8BKG3.
SOURCESearch...

Entry information

Entry namePTK7_MOUSE
AccessionPrimary (citable) accession number: Q8BKG3
Secondary accession number(s): Q3V422 expand/collapse secondary AC list , Q6W8S9, Q8CHK5, Q8K178
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot