DDR1

DDR1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3ZOS, 4AG4, 4BKJ, 4CKR, 5BVK, 5BVN, 5BVO, 5BVW, 5FDP
Identifiers
Aliases	DDR1, CAK, CD167, DDR, EHGK2, MCK10, NEP, NTRK4, PTK3, PTK3A, RTK6, TRKE, discoidin domain receptor tyrosine kinase 1
External IDs	OMIM: 600408 MGI: 99216 HomoloGene: 68212 GeneCards: DDR1
Gene location (Human)
Chr.	Chromosome 6 (human)
End	30,900,156 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	36,015,513 bp
RNA expression pattern
	Top expressed in
	right uterine tube; ; ganglionic eminence; ; minor salivary glands; ; islet of Langerhans; ; skin of abdomen; ; substantia nigra; ; left lobe of thyroid gland; ; body of pancreas; ; temporal lobe; ; amygdala;
	Top expressed in
	ciliary body; ; iris; ; retinal pigment epithelium; ; conjunctival fornix; ; medial ganglionic eminence; ; epithelium of stomach; ; motor neuron; ; parotid gland; ; lacrimal gland; ; left lung lobe;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; collagen binding; metal ion binding; kinase activity; protein binding; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase collagen receptor activity; protein tyrosine kinase activity; ATP binding; receptor tyrosine kinase;
Cellular component	integral component of membrane; membrane; receptor complex; plasma membrane; integral component of plasma membrane; extracellular region; extracellular exosome; extracellular space;
Biological process	collagen-activated tyrosine kinase receptor signaling pathway; branching involved in mammary gland duct morphogenesis; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; female pregnancy; extracellular matrix organization; ear development; mammary gland alveolus development; regulation of extracellular matrix disassembly; smooth muscle cell migration; smooth muscle cell-matrix adhesion; regulation of cell-matrix adhesion; protein phosphorylation; cell adhesion; regulation of cell growth; peptidyl-tyrosine phosphorylation; lactation; wound healing, spreading of cells; embryo implantation; negative regulation of cell population proliferation; peptidyl-tyrosine autophosphorylation; protein autophosphorylation; axon development; neuron projection extension; cell-matrix adhesion; positive regulation of cell population proliferation; cell differentiation; regulation of extracellular matrix organization;
	Sources:Amigo / QuickGO
Orthologs
	780
	12305
ENSG00000215522; ENSG00000137332; ENSG00000229767; ENSG00000230456; ENSG00000234078;
	ENSG00000204580; ENSG00000223680
	ENSMUSG00000003534
	Q08345
	Q03146
NM_001202521; NM_001202522; NM_001202523; NM_001297652; NM_001297653;
	NM_001297654; NM_001954; NM_013993; NM_013994
	NM_001198831; NM_001198833; NM_007584; NM_172962
NP_001189450; NP_001189451; NP_001189452; NP_001284581; NP_001284582;
	NP_001284583; NP_001945; NP_054699; NP_054700; NP_001284583.1; NP_054699.2
	NP_001185760; NP_001185762; NP_031610; NP_766550
	Wikidata
View/Edit Human	View/Edit Mouse

Discoidin domain receptor family, member 1, also known as DDR1 or CD167a (cluster of differentiation 167a), is a human gene.^[5]

Function[edit]

Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation and metabolism. The protein encoded by this gene is a RTK that is widely expressed in normal and transformed epithelial cells and is activated by various types of collagen. This protein belongs to a subfamily of tyrosine kinase receptors with a homology region to the Dictyostelium discoideum protein discoidin I in their extracellular domain. Its autophosphorylation is achieved by all collagens so far tested (type I to type VI). A closely related family member is the DDR2 protein.^[6] In situ studies and Northern-blot analysis showed that expression of this encoded protein is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, this protein is significantly over-expressed in several human tumors from breast, ovarian, esophageal, and pediatric brain. This gene is located on chromosome 6p21.3 in proximity to several HLA class I genes. Alternative splicing of this gene results in multiple transcript variants.^[5]

References[edit]

^ ^a ^b ^c ENSG00000137332, ENSG00000229767, ENSG00000230456, ENSG00000234078, ENSG00000204580, ENSG00000223680 GRCh38: Ensembl release 89: ENSG00000215522, ENSG00000137332, ENSG00000229767, ENSG00000230456, ENSG00000234078, ENSG00000204580, ENSG00000223680 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003534 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: DDR1 discoidin domain receptor family, member 1".
^ Fu HL, Valiathan RR, Arkwright R, Sohail A, Mihai C, Kumarasiri M, Mahasenan KV, Mobashery S, Huang P, Agarwal G, Fridman R (Mar 2013). "Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling". The Journal of Biological Chemistry. 288 (11): 7430–7. doi:10.1074/jbc.R112.444158. PMC 3597784. PMID 23335507.

Further reading[edit]

Edelhoff S, Sweetser DA, Disteche CM (Jan 1995). "Mapping of the NEP receptor tyrosine kinase gene to human chromosome 6p21.3 and mouse chromosome 17C". Genomics. 25 (1): 309–11. doi:10.1016/0888-7543(95)80144-B. PMID 7774938.
Shelling AN, Butler R, Jones T, Laval S, Boyle JM, Ganesan TS (Jan 1995). "Localization of an epithelial-specific receptor kinase (EDDR1) to chromosome 6q16". Genomics. 25 (2): 584–7. doi:10.1016/0888-7543(95)80065-T. PMID 7789998.
Weiner TM, Liu ET, Craven RJ, Cance WG (Jan 1994). "Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors". Annals of Surgical Oncology. 1 (1): 18–27. doi:10.1007/BF02303537. PMID 7834423. S2CID 2737602.
Laval S, Butler R, Shelling AN, Hanby AM, Poulsom R, Ganesan TS (Nov 1994). "Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line". Cell Growth & Differentiation. 5 (11): 1173–83. PMID 7848919.
Kato JY, Matsuoka M, Strom DK, Sherr CJ (Apr 1994). "Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase". Molecular and Cellular Biology. 14 (4): 2713–21. doi:10.1128/MCB.14.4.2713. PMC 358637. PMID 8139570.
Di Marco E, Cutuli N, Guerra L, Cancedda R, De Luca M (Nov 1993). "Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues". The Journal of Biological Chemistry. 268 (32): 24290–5. doi:10.1016/S0021-9258(20)80524-9. hdl:11380/607761. PMID 8226977.
Perez JL, Shen X, Finkernagel S, Sciorra L, Jenkins NA, Gilbert DJ, Copeland NG, Wong TW (Jan 1994). "Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain". Oncogene. 9 (1): 211–9. PMID 8302582.
Johnson JD, Edman JC, Rutter WJ (Jun 1993). "A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain". Proceedings of the National Academy of Sciences of the United States of America. 90 (12): 5677–81. Bibcode:1993PNAS...90.5677J. doi:10.1073/pnas.90.12.5677. PMC 46784. PMID 8390675.
Perez JL, Jing SQ, Wong TW (Apr 1996). "Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines". Oncogene. 12 (7): 1469–77. PMID 8622863.
Valent A, Meddeb M, Danglot G, Duverger A, Nguyen VC, Bernheim A (Jul 1996). "Assignment of the NTRK4 (trkE) gene to chromosome 6p21". Human Genetics. 98 (1): 12–5. doi:10.1007/s004390050152. PMID 8682498. S2CID 9450185.
Playford MP, Butler RJ, Wang XC, Katso RM, Cooke IE, Ganesan TS (Jul 1996). "The genomic structure of discoidin receptor tyrosine kinase". Genome Research. 6 (7): 620–7. doi:10.1101/gr.6.7.620. PMID 8796349.
Sakuma S, Saya H, Tada M, Nakao M, Fujiwara T, Roth JA, Sawamura Y, Shinohe Y, Abe H (Dec 1996). "Receptor protein tyrosine kinase DDR is up-regulated by p53 protein". FEBS Letters. 398 (2–3): 165–9. doi:10.1016/S0014-5793(96)01234-3. PMID 8977099. S2CID 7573214.
Nemoto T, Ohashi K, Akashi T, Johnson JD, Hirokawa K (1998). "Overexpression of protein tyrosine kinases in human esophageal cancer". Pathobiology. 65 (4): 195–203. doi:10.1159/000164123. PMID 9396043.
Tanaka K, Nagayama Y, Nakano T, Takamura N, Namba H, Fukada S, Kuma K, Yamashita S, Niwa M (Mar 1998). "Expression profile of receptor-type protein tyrosine kinase genes in the human thyroid". Endocrinology. 139 (3): 852–8. doi:10.1210/endo.139.3.5791. PMID 9492013.
Vogel W, Gish GD, Alves F, Pawson T (Dec 1997). "The discoidin domain receptor tyrosine kinases are activated by collagen". Molecular Cell. 1 (1): 13–23. doi:10.1016/S1097-2765(00)80003-9. PMID 9659899.
Shrivastava A, Radziejewski C, Campbell E, Kovac L, McGlynn M, Ryan TE, Davis S, Goldfarb MP, Glass DJ, Lemke G, Yancopoulos GD (Dec 1997). "An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors". Molecular Cell. 1 (1): 25–34. doi:10.1016/S1097-2765(00)80004-0. PMID 9659900.
Vogel W, Brakebusch C, Fässler R, Alves F, Ruggiero F, Pawson T (Feb 2000). "Discoidin domain receptor 1 is activated independently of beta(1) integrin". The Journal of Biological Chemistry. 275 (8): 5779–84. doi:10.1074/jbc.275.8.5779. PMID 10681566.
Foehr ED, Tatavos A, Tanabe E, Raffioni S, Goetz S, Dimarco E, De Luca M, Bradshaw RA (May 2000). "Discoidin domain receptor 1 (DDR1) signaling in PC12 cells: activation of juxtamembrane domains in PDGFR/DDR/TrkA chimeric receptors". FASEB Journal. 14 (7): 973–81. doi:10.1096/fasebj.14.7.973. PMID 10783152. S2CID 43317719.
Weiner HL, Huang H, Zagzag D, Boyce H, Lichtenbaum R, Ziff EB (Dec 2000). "Consistent and selective expression of the discoidin domain receptor-1 tyrosine kinase in human brain tumors". Neurosurgery. 47 (6): 1400–9. doi:10.1097/00006123-200012000-00028. PMID 11126911. S2CID 2299503.
Mohan RR, Mohan RR, Wilson SE (Jan 2001). "Discoidin domain receptor (DDR) 1 and 2: collagen-activated tyrosine kinase receptors in the cornea". Experimental Eye Research. 72 (1): 87–92. doi:10.1006/exer.2000.0932. PMID 11133186.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This membrane protein–related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] ENSG00000137332, ENSG00000229767, ENSG00000230456, ENSG00000234078, ENSG00000204580, ENSG00000223680 GRCh38: Ensembl release 89: ENSG00000215522, ENSG00000137332, ENSG00000229767, ENSG00000230456, ENSG00000234078, ENSG00000204580, ENSG00000223680 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003534 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: DDR1 discoidin domain receptor family, member 1".

[pmid23335507-6] Fu HL, Valiathan RR, Arkwright R, Sohail A, Mihai C, Kumarasiri M, Mahasenan KV, Mobashery S, Huang P, Agarwal G, Fridman R (Mar 2013). "Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling". The Journal of Biological Chemistry. 288 (11): 7430–7. doi:10.1074/jbc.R112.444158. PMC 3597784. PMID 23335507.

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[6]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

DDR1

Function[edit]

References[edit]

Further reading[edit]

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