PTK7_HUMAN
ID PTK7_HUMAN Reviewed; 1070 AA.
AC Q13308; A8K974; B7Z477; E9PFZ5; Q13417; Q5T650; Q6IQ54; Q8NFA5; Q8NFA6;
AC Q8NFA7; Q8NFA8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Inactive tyrosine-protein kinase 7;
DE AltName: Full=Colon carcinoma kinase 4;
DE Short=CCK-4;
DE AltName: Full=Protein-tyrosine kinase 7;
DE AltName: Full=Pseudo tyrosine kinase receptor 7;
DE AltName: Full=Tyrosine-protein kinase-like 7;
DE Flags: Precursor;
GN Name=PTK7; Synonyms=CCK4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma, and Placenta;
RX PubMed=7478540;
RA Mossie K., Jallal B., Alves F., Sures I., Plowman G.D., Ullrich A.;
RT "Colon carcinoma kinase-4 defines a new subclass of the receptor tyrosine
RT kinase family.";
RL Oncogene 11:2179-2184(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=8882711; DOI=10.1093/oxfordjournals.jbchem.a021228;
RA Park S.-K., Lee H.-S., Lee S.-T.;
RT "Characterization of the human full-length PTK7 cDNA encoding a receptor
RT protein tyrosine kinase-like molecule closely related to chick KLG.";
RL J. Biochem. 119:235-239(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS
RP 1; 2; 3; 4 AND 5).
RC TISSUE=Testis;
RX PubMed=12427550; DOI=10.1016/s0167-4781(02)00536-5;
RA Jung J.-W., Ji A.-R., Lee J., Kim U.-J., Lee S.-T.;
RT "Organization of the human PTK7 gene encoding a receptor protein tyrosine
RT kinase-like molecule and alternative splicing of its mRNA.";
RL Biochim. Biophys. Acta 1579:153-163(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6).
RC TISSUE=Testis, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP GLYCOSYLATION AT ASN-646.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-646.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP FUNCTION.
RX PubMed=18471990; DOI=10.1016/j.bbrc.2008.04.168;
RA Shin W.-S., Maeng Y.-S., Jung J.-W., Min J.-K., Kwon Y.-G., Lee S.-T.;
RT "Soluble PTK7 inhibits tube formation, migration, and invasion of
RT endothelial cells and angiogenesis.";
RL Biochem. Biophys. Res. Commun. 371:793-798(2008).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116; ASN-175; ASN-268 AND
RP ASN-283.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP FUNCTION.
RX PubMed=20558616; DOI=10.1182/blood-2010-01-262352;
RA Prebet T., Lhoumeau A.-C., Arnoulet C., Aulas A., Marchetto S.,
RA Audebert S., Puppo F., Chabannon C., Sainty D., Santoni M.-J., Sebbagh M.,
RA Summerour V., Huon Y., Shin W.-S., Lee S.-T., Esterni B., Vey N.,
RA Borg J.-P.;
RT "The cell polarity PTK7 receptor acts as a modulator of the
RT chemotherapeutic response in acute myeloid leukemia and impairs clinical
RT outcome.";
RL Blood 116:2315-2323(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, CLEAVAGE, AND MUTAGENESIS OF
RP LEU-622; MET-641 AND MET-701.
RX PubMed=20837484; DOI=10.1074/jbc.m110.165159;
RA Golubkov V.S., Chekanov A.V., Cieplak P., Aleshin A.E., Chernov A.V.,
RA Zhu W., Radichev I.A., Zhang D., Dong P.D., Strongin A.Y.;
RT "The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a highly
RT efficient proteolytic target of membrane type-1 matrix metalloproteinase:
RT implications in cancer and embryogenesis.";
RL J. Biol. Chem. 285:35740-35749(2010).
RN [14]
RP FUNCTION.
RX PubMed=21103379; DOI=10.1371/journal.pone.0014018;
RA Meng L., Sefah K., O'Donoghue M.B., Zhu G., Shangguan D., Noorali A.,
RA Chen Y., Zhou L., Tan W.;
RT "Silencing of PTK7 in colon cancer cells: caspase-10-dependent apoptosis
RT via mitochondrial pathway.";
RL PLoS ONE 5:E14018-E14018(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION, INTERACTION WITH CTNNB1, AND REGION.
RX PubMed=21132015; DOI=10.1038/embor.2010.185;
RA Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F.,
RA Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M., Shin W.-S.,
RA Lee S.-T., Kodjabachian L., Borg J.-P.;
RT "Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin
RT canonical signalling.";
RL EMBO Rep. 12:43-49(2011).
RN [17]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-276; SER-410; ASP-745; GLN-766;
RP VAL-777; ARG-783; VAL-933; THR-1029 AND GLN-1038.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Inactive tyrosine kinase involved in Wnt signaling pathway.
CC Component of both the non-canonical (also known as the Wnt/planar cell
CC polarity signaling) and the canonical Wnt signaling pathway. Functions
CC in cell adhesion, cell migration, cell polarity, proliferation, actin
CC cytoskeleton reorganization and apoptosis. Has a role in embryogenesis,
CC epithelial tissue organization and angiogenesis.
CC {ECO:0000269|PubMed:18471990, ECO:0000269|PubMed:20558616,
CC ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:21103379,
CC ECO:0000269|PubMed:21132015}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:21132015}.
CC -!- INTERACTION:
CC Q13308; P35222: CTNNB1; NbExp=5; IntAct=EBI-2803245, EBI-491549;
CC Q13308; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2803245, EBI-11749135;
CC Q13308; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2803245, EBI-10171774;
CC Q13308; Q99750: MDFI; NbExp=3; IntAct=EBI-2803245, EBI-724076;
CC Q13308; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2803245, EBI-11522433;
CC Q13308; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2803245, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20837484}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:20837484}. Cell
CC junction {ECO:0000269|PubMed:20837484}. Note=Colocalizes with MMP14 at
CC cell junctions. Also localizes at the leading edge of migrating cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PTK7-1;
CC IsoId=Q13308-1; Sequence=Displayed;
CC Name=2; Synonyms=PTK7-2;
CC IsoId=Q13308-2; Sequence=VSP_037182;
CC Name=3; Synonyms=PTK7-3;
CC IsoId=Q13308-3; Sequence=VSP_037181;
CC Name=4; Synonyms=PTK7-4;
CC IsoId=Q13308-4; Sequence=VSP_037183;
CC Name=5; Synonyms=PTK7-5;
CC IsoId=Q13308-5; Sequence=VSP_037184, VSP_037185;
CC Name=6;
CC IsoId=Q13308-6; Sequence=VSP_044775;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, liver, pancreas, kidney,
CC placenta and melanocytes. Weakly expressed in thyroid gland, ovary,
CC brain, heart and skeletal muscle. Also expressed in erythroleukemia
CC cells. But not expressed in colon.
CC -!- INDUCTION: Higher expression in cell lines established from normal non-
CC tumorigenic tissues compared to cell lines established from highly
CC metastatic invasive carcinomas (at protein level).
CC {ECO:0000269|PubMed:20837484}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: MMP14 cleaves PTK7 between Pro-621 and Leu-622 generating an N-
CC terminal soluble (70 kDa) fragment and a membrane C-terminal (50 kDa)
CC fragment. Proteolysis by MMP14 regulates PTK7 function in non-canonical
CC Wnt signaling pathway. {ECO:0000269|PubMed:20837484}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTK7ID41901ch6p21.html";
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DR EMBL; U33635; AAA87565.1; -; mRNA.
DR EMBL; U40271; AAC50484.2; -; mRNA.
DR EMBL; AF447176; AAL39062.1; -; Genomic_DNA.
DR EMBL; AF447157; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447158; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447162; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447164; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447167; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447170; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447171; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447173; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447174; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF447175; AAL39062.1; JOINED; Genomic_DNA.
DR EMBL; AF531868; AAN04862.1; -; mRNA.
DR EMBL; AF531869; AAN04863.1; -; mRNA.
DR EMBL; AF531870; AAN04864.1; -; mRNA.
DR EMBL; AF531871; AAN04865.1; -; mRNA.
DR EMBL; AF531872; AAN04866.1; -; mRNA.
DR EMBL; AK291016; BAF83705.1; -; mRNA.
DR EMBL; AK292589; BAF85278.1; -; mRNA.
DR EMBL; AK296953; BAH12463.1; -; mRNA.
DR EMBL; AL355385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04154.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04155.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04156.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04158.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04160.1; -; Genomic_DNA.
DR EMBL; BC071557; AAH71557.1; -; mRNA.
DR CCDS; CCDS4884.1; -. [Q13308-1]
DR CCDS; CCDS4885.1; -. [Q13308-2]
DR CCDS; CCDS4886.1; -. [Q13308-3]
DR CCDS; CCDS4887.1; -. [Q13308-4]
DR CCDS; CCDS59021.1; -. [Q13308-6]
DR PIR; JC4593; JC4593.
DR RefSeq; NP_001257327.1; NM_001270398.1. [Q13308-6]
DR RefSeq; NP_002812.2; NM_002821.4. [Q13308-1]
DR RefSeq; NP_690619.1; NM_152880.3. [Q13308-2]
DR RefSeq; NP_690620.1; NM_152881.3. [Q13308-3]
DR RefSeq; NP_690621.1; NM_152882.3. [Q13308-4]
DR PDB; 6VG3; X-ray; 1.95 A; A/B/C=774-1069.
DR PDBsum; 6VG3; -.
DR AlphaFoldDB; Q13308; -.
DR SMR; Q13308; -.
DR BioGRID; 111721; 111.
DR IntAct; Q13308; 57.
DR MINT; Q13308; -.
DR STRING; 9606.ENSP00000418754; -.
DR GlyConnect; 655; 40 N-Linked glycans (6 sites).
DR GlyGen; Q13308; 11 sites, 46 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q13308; -.
DR MetOSite; Q13308; -.
DR PhosphoSitePlus; Q13308; -.
DR SwissPalm; Q13308; -.
DR BioMuta; PTK7; -.
DR DMDM; 116242736; -.
DR EPD; Q13308; -.
DR jPOST; Q13308; -.
DR MassIVE; Q13308; -.
DR MaxQB; Q13308; -.
DR PaxDb; Q13308; -.
DR PeptideAtlas; Q13308; -.
DR PRIDE; Q13308; -.
DR ProteomicsDB; 20212; -.
DR ProteomicsDB; 59293; -. [Q13308-1]
DR ProteomicsDB; 59294; -. [Q13308-2]
DR ProteomicsDB; 59295; -. [Q13308-3]
DR ProteomicsDB; 59296; -. [Q13308-4]
DR ProteomicsDB; 59297; -. [Q13308-5]
DR TopDownProteomics; Q13308-3; -. [Q13308-3]
DR ABCD; Q13308; 1 sequenced antibody.
DR Antibodypedia; 1008; 593 antibodies from 38 providers.
DR DNASU; 5754; -.
DR Ensembl; ENST00000230418.8; ENSP00000230418.4; ENSG00000112655.16. [Q13308-5]
DR Ensembl; ENST00000230419.9; ENSP00000230419.4; ENSG00000112655.16. [Q13308-1]
DR Ensembl; ENST00000345201.6; ENSP00000325992.4; ENSG00000112655.16. [Q13308-2]
DR Ensembl; ENST00000349241.6; ENSP00000325462.4; ENSG00000112655.16. [Q13308-3]
DR Ensembl; ENST00000352931.6; ENSP00000326029.3; ENSG00000112655.16. [Q13308-4]
DR Ensembl; ENST00000481273.5; ENSP00000418754.1; ENSG00000112655.16. [Q13308-6]
DR GeneID; 5754; -.
DR KEGG; hsa:5754; -.
DR MANE-Select; ENST00000230419.9; ENSP00000230419.4; NM_002821.5; NP_002812.2.
DR UCSC; uc003oub.3; human. [Q13308-1]
DR CTD; 5754; -.
DR DisGeNET; 5754; -.
DR GeneCards; PTK7; -.
DR HGNC; HGNC:9618; PTK7.
DR HPA; ENSG00000112655; Low tissue specificity.
DR MIM; 601890; gene.
DR neXtProt; NX_Q13308; -.
DR OpenTargets; ENSG00000112655; -.
DR PharmGKB; PA33961; -.
DR VEuPathDB; HostDB:ENSG00000112655; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000157908; -.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; Q13308; -.
DR OMA; MWWEHAG; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; Q13308; -.
DR TreeFam; TF326835; -.
DR PathwayCommons; Q13308; -.
DR SignaLink; Q13308; -.
DR SIGNOR; Q13308; -.
DR BioGRID-ORCS; 5754; 19 hits in 1117 CRISPR screens.
DR ChiTaRS; PTK7; human.
DR GeneWiki; PTK7; -.
DR GenomeRNAi; 5754; -.
DR Pharos; Q13308; Tbio.
DR PRO; PR:Q13308; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13308; protein.
DR Bgee; ENSG00000112655; Expressed in stromal cell of endometrium and 125 other tissues.
DR ExpressionAtlas; Q13308; baseline and differential.
DR Genevisible; Q13308; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:1904929; F:coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0003401; P:axis elongation; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0060026; P:convergent extension; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 7.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 7.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1070
FT /note="Inactive tyrosine-protein kinase 7"
FT /id="PRO_0000016748"
FT TOPO_DOM 31..704
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..218
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..317
FT /note="Ig-like C2-type 3"
FT DOMAIN 309..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 412..497
FT /note="Ig-like C2-type 5"
FT DOMAIN 503..586
FT /note="Ig-like C2-type 6"
FT DOMAIN 578..680
FT /note="Ig-like C2-type 7"
FT DOMAIN 796..1066
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 736..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..1070
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:21132015"
FT SITE 621..622
FT /note="Cleavage; by MMP14"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKG3"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 53..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 433..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 524..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 613..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..26
FT /note="MGAARGSPARPRRLPLLSVLLLPLLG -> MGSFLSGEKRPSAPTVGSAMEK
FT KEFPTPPGRVGP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044775"
FT VAR_SEQ 410..540
FT /note="TVPSWLKKPQDSQLEEGKPGYLDCLTQATPKPTVVWYRNQMLISEDSRFEVF
FT KNGTLRINSVEVYDGTWYRCMSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEA
FT TVPCSATGREKPTIKWERAD -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12427550"
FT /id="VSP_037181"
FT VAR_SEQ 500..539
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12427550,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_037182"
FT VAR_SEQ 627..682
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12427550"
FT /id="VSP_037183"
FT VAR_SEQ 804..816
FT /note="KSEFGEVFLAKAQ -> RPQAVPEDFQEQG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12427550"
FT /id="VSP_037184"
FT VAR_SEQ 817..1070
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12427550"
FT /id="VSP_037185"
FT VARIANT 276
FT /note="R -> H (in dbSNP:rs56188167)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041502"
FT VARIANT 410
FT /note="T -> S (in dbSNP:rs34021075)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041503"
FT VARIANT 745
FT /note="E -> D (in dbSNP:rs9472017)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041504"
FT VARIANT 766
FT /note="E -> Q (in dbSNP:rs56216742)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041505"
FT VARIANT 777
FT /note="A -> V (in dbSNP:rs34764696)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041506"
FT VARIANT 783
FT /note="H -> R (in dbSNP:rs55820547)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041507"
FT VARIANT 933
FT /note="A -> V (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041508"
FT VARIANT 1029
FT /note="P -> T (in dbSNP:rs55755163)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041509"
FT VARIANT 1038
FT /note="R -> Q (in dbSNP:rs34865794)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041510"
FT MUTAGEN 622
FT /note="L->D: Prevents proteolysis by MMP14."
FT /evidence="ECO:0000269|PubMed:20837484"
FT MUTAGEN 641
FT /note="M->R: No impact on proteolysis by MMP14."
FT /evidence="ECO:0000269|PubMed:20837484"
FT MUTAGEN 701
FT /note="M->D: No impact on proteolysis by MMP14."
FT /evidence="ECO:0000269|PubMed:20837484"
FT CONFLICT 87
FT /note="F -> L (in Ref. 4; BAF85278)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="R -> P (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="L -> P (in Ref. 7; AAH71557)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="T -> K (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="G -> S (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..496
FT /note="RV -> VL (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> G (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="Q -> R (in Ref. 4; BAH12463)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="I -> F (in Ref. 4; BAF85278)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="G -> E (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="P -> A (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="F -> S (in Ref. 1; AAA87565)"
FT /evidence="ECO:0000305"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 796..804
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 806..816
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 823..832
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 837..852
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 861..865
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 867..876
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 879..882
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 883..890
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 904..923
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 936..938
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 944..946
FT /evidence="ECO:0007829|PDB:6VG3"
FT TURN 952..956
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 957..959
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:6VG3"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 970..972
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 975..980
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 985..1000
FT /evidence="ECO:0007829|PDB:6VG3"
FT TURN 1006..1009
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 1012..1020
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 1034..1043
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 1048..1050
FT /evidence="ECO:0007829|PDB:6VG3"
FT HELIX 1054..1062
FT /evidence="ECO:0007829|PDB:6VG3"
SQ SEQUENCE 1070 AA; 118392 MW; 304926A1774EB5F4 CRC64;
MGAARGSPAR PRRLPLLSVL LLPLLGGTQT AIVFIKQPSS QDALQGRRAL LRCEVEAPGP
VHVYWLLDGA PVQDTERRFA QGSSLSFAAV DRLQDSGTFQ CVARDDVTGE EARSANASFN
IKWIEAGPVV LKHPASEAEI QPQTQVTLRC HIDGHPRPTY QWFRDGTPLS DGQSNHTVSS
KERNLTLRPA GPEHSGLYSC CAHSAFGQAC SSQNFTLSIA DESFARVVLA PQDVVVARYE
EAMFHCQFSA QPPPSLQWLF EDETPITNRS RPPHLRRATV FANGSLLLTQ VRPRNAGIYR
CIGQGQRGPP IILEATLHLA EIEDMPLFEP RVFTAGSEER VTCLPPKGLP EPSVWWEHAG
VRLPTHGRVY QKGHELVLAN IAESDAGVYT CHAANLAGQR RQDVNITVAT VPSWLKKPQD
SQLEEGKPGY LDCLTQATPK PTVVWYRNQM LISEDSRFEV FKNGTLRINS VEVYDGTWYR
CMSSTPAGSI EAQARVQVLE KLKFTPPPQP QQCMEFDKEA TVPCSATGRE KPTIKWERAD
GSSLPEWVTD NAGTLHFARV TRDDAGNYTC IASNGPQGQI RAHVQLTVAV FITFKVEPER
TTVYQGHTAL LQCEAQGDPK PLIQWKGKDR ILDPTKLGPR MHIFQNGSLV IHDVAPEDSG
RYTCIAGNSC NIKHTEAPLY VVDKPVPEES EGPGSPPPYK MIQTIGLSVG AAVAYIIAVL
GLMFYCKKRC KAKRLQKQPE GEEPEMECLN GGPLQNGQPS AEIQEEVALT SLGSGPAATN
KRHSTSDKMH FPRSSLQPIT TLGKSEFGEV FLAKAQGLEE GVAETLVLVK SLQSKDEQQQ
LDFRRELEMF GKLNHANVVR LLGLCREAEP HYMVLEYVDL GDLKQFLRIS KSKDEKLKSQ
PLSTKQKVAL CTQVALGMEH LSNNRFVHKD LAARNCLVSA QRQVKVSALG LSKDVYNSEY
YHFRQAWVPL RWMSPEAILE GDFSTKSDVW AFGVLMWEVF THGEMPHGGQ ADDEVLADLQ
AGKARLPQPE GCPSKLYRLM QRCWALSPKD RPSFSEIASA LGDSTVDSKP
