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Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b)

 DDR2_MOUSE              Reviewed;         854 AA.
Q62371; B2RSD7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=Discoidin domain-containing receptor 2;
Short=Discoidin domain receptor 2;
EC=2.7.10.1;
AltName: Full=CD167 antigen-like family member B;
AltName: Full=Neurotrophic tyrosine kinase, receptor-related 3;
AltName: Full=Receptor protein-tyrosine kinase TKT;
AltName: Full=Tyrosine-protein kinase TYRO10;
AltName: CD_antigen=CD167b;
Flags: Precursor;
Name=Ddr2; Synonyms=Ntrkr3, Tkt, Tyro10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8247548;
Karn T., Holtrich U., Braeuninger A., Boehme B., Wolf G.,
Ruebsamen-Waigmann H., Strebhardt K.;
"Structure, expression and chromosomal mapping of TKT from man and
mouse: a new subclass of receptor tyrosine kinases with a factor VIII-
like domain.";
Oncogene 8:3433-3440(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8108131;
Lai C., Lemke G.E.;
"Structure and expression of the Tyro 10 receptor tyrosine kinase.";
Oncogene 9:877-883(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11375938; DOI=10.1093/embo-reports/kve094;
Labrador J.P., Azcoitia V., Tuckermann J., Lin C., Olaso E., Manes S.,
Bruckner K., Goergen J.L., Lemke G., Yancopoulos G., Angel P.,
Martinez C., Klein R.;
"The collagen receptor DDR2 regulates proliferation and its
elimination leads to dwarfism.";
EMBO Rep. 2:446-452(2001).
[5]
FUNCTION.
PubMed=11723120; DOI=10.1074/jbc.M107571200;
Olaso E., Labrador J.-P., Wang L., Ikeda K., Eng F.J., Klein R.,
Lovett D.H., Lin H.C., Friedman S.L.;
"Discoidin domain receptor 2 regulates fibroblast proliferation and
migration through the extracellular matrix in association with
transcriptional activation of matrix metalloproteinase-2.";
J. Biol. Chem. 277:3606-3613(2002).
[6]
FUNCTION, INTERACTION WITH SRC AND SHC1, MUTAGENESIS OF TYR-471 AND
LYS-608, AND PHOSPHORYLATION AT TYR-471.
PubMed=11884411; DOI=10.1074/jbc.M201078200;
Ikeda K., Wang L.H., Torres R., Zhao H., Olaso E., Eng F.J.,
Labrador P., Klein R., Lovett D., Yancopoulos G.D., Friedman S.L.,
Lin H.C.;
"Discoidin domain receptor 2 interacts with Src and Shc following its
activation by type I collagen.";
J. Biol. Chem. 277:19206-19212(2002).
[7]
FUNCTION IN UP-REGULATION OF MMP13.
PubMed=15509586; DOI=10.1074/jbc.M411954200;
Xu L., Peng H., Wu D., Hu K., Goldring M.B., Olsen B.R., Li Y.;
"Activation of the discoidin domain receptor 2 induces expression of
matrix metalloproteinase 13 associated with osteoarthritis in mice.";
J. Biol. Chem. 280:548-555(2005).
[8]
INVOLVEMENT IN SLI, AND TISSUE SPECIFICITY.
PubMed=18483174; DOI=10.1210/me.2007-0310;
Kano K., Marin de Evsikova C., Young J., Wnek C., Maddatu T.P.,
Nishina P.M., Naggert J.K.;
"A novel dwarfism with gonadal dysfunction due to loss-of-function
allele of the collagen receptor gene, Ddr2, in the mouse.";
Mol. Endocrinol. 22:1866-1880(2008).
[9]
INVOLVEMENT IN SLI, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19681157; DOI=10.1002/mrd.21093;
Kano K., Kitamura A., Matsuwaki T., Morimatsu M., Naito K.;
"Discoidin domain receptor 2 (DDR2) is required for maintenance of
spermatogenesis in male mice.";
Mol. Reprod. Dev. 77:29-37(2010).
-!- FUNCTION: Tyrosine kinase that functions as cell surface receptor
for fibrillar collagen and regulates cell differentiation,
remodeling of the extracellular matrix, cell migration and cell
proliferation. Required for normal bone development. Regulates
osteoblast differentiation and chondrocyte maturation via a
signaling pathway that involves MAP kinases and leads to the
activation of the transcription factor RUNX2. Regulates remodeling
of the extracellular matrix by up-regulation of the collagenases
MMP1, MMP2 and MMP13, and thereby facilitates cell migration and
tumor cell invasion. Promotes fibroblast migration and
proliferation, and thereby contributes to cutaneous wound healing.
{ECO:0000269|PubMed:11375938, ECO:0000269|PubMed:11723120,
ECO:0000269|PubMed:11884411, ECO:0000269|PubMed:15509586,
ECO:0000269|PubMed:19681157}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Present in an inactive state in the absence of
collagen binding and phosphorylation by SRC. Tyrosine
phosphorylation enhances the affinity for ATP and the catalytic
activity.
-!- SUBUNIT: Binds hydroxyproline-rich sequence motifs in fibrillar,
glycosylated collagen, such as the GQOGVMGFO motif, where O stands
for hydroxyproline. Interacts with SRC. Interacts (tyrosine
phosphorylated) with SHC1. {ECO:0000269|PubMed:11884411}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Widely expressed. Detected in lung, ovary,
skin and in testis Leydig cells (at protein level). Widely
expressed. Detected at high levels in heart, lung, skeletal
muscle, central nervous system (CNS) and kidney, and at lower
levels in brain and testis. Detected in chondrocytes in tibia
growth plates of young mice. {ECO:0000269|PubMed:11375938,
ECO:0000269|PubMed:18483174, ECO:0000269|PubMed:19681157}.
-!- INDUCTION: Up-regulated during osteoblast differentiation (in
vitro). Up-regulated in cartilage from mice with osteoarthritis.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated in response to collagen binding.
Phosphorylated by SRC; this is required for activation and
subsequent autophosphorylation on additional tyrosine residues (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=Defects in Ddr2 are the cause of the smallie (sli)
phenotype. Smallie mice show distinct dwarfing, with reduced body
mass and reduced bone mineral content. Mice also have mild
craniofacial deformities, such as protuberant eyes and snub noses.
Smallie mice have a reduced life span, with about half of them
dying within 6 months. Matings between male and female smallie
mice do not yield any offspring. The levels of circulating steroid
hormones remain at a level corresponding to prepubertal wild-type
mice. Adult testes exhibit much reduced numbers of spermatids with
atrophy of spermatogonia, Sertoli and Leydig cells. Ovaries show
an absence of corpora lutea.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate, but fail to thrive, resulting in much reduced adult body
weight and dwarfing. They exhibit shortening of long bones,
irregular growth of flat bones and a shortened snout. Young mice
show shortened growth plates in long bones and impaired
chondrocyte proliferation. Likewise, cultured fibroblasts from
mutant mice show reduced proliferation.
{ECO:0000269|PubMed:11375938}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: According to PubMed:18483174 Ddr2 is required for male
and female fertility, since smallie mice with a 150 kb deletion
that extends into the Ddr2 gene are sterile. Smallie males have
defects in spermatogenesis (PubMed:19681157). On the other hand,
the fertility status of mice with a targeted disruption of the
Ddr2 gene has not been mentioned (PubMed:11375938). Thus, the
infertility of smallie mice may be due to some additional, not yet
identified defect. {ECO:0000305|PubMed:11375938,
ECO:0000305|PubMed:19681157}.
-!- SEQUENCE CAUTION:
Sequence=CAA54040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X76505; CAA54040.1; ALT_INIT; mRNA.
EMBL; BC138826; AAI38827.1; -; mRNA.
EMBL; BC138827; AAI38828.1; -; mRNA.
CCDS; CCDS48436.1; -.
PIR; I48859; I48859.
RefSeq; NP_072075.2; NM_022563.2.
RefSeq; XP_006496759.1; XM_006496696.3.
RefSeq; XP_006496760.1; XM_006496697.3.
RefSeq; XP_006496761.1; XM_006496698.3.
UniGene; Mm.229249; -.
ProteinModelPortal; Q62371; -.
SMR; Q62371; -.
STRING; 10090.ENSMUSP00000027985; -.
iPTMnet; Q62371; -.
PhosphoSitePlus; Q62371; -.
SwissPalm; Q62371; -.
MaxQB; Q62371; -.
PaxDb; Q62371; -.
PeptideAtlas; Q62371; -.
PRIDE; Q62371; -.
Ensembl; ENSMUST00000027985; ENSMUSP00000027985; ENSMUSG00000026674.
Ensembl; ENSMUST00000170800; ENSMUSP00000129624; ENSMUSG00000026674.
Ensembl; ENSMUST00000194690; ENSMUSP00000141443; ENSMUSG00000026674.
GeneID; 18214; -.
KEGG; mmu:18214; -.
UCSC; uc007dlu.2; mouse.
CTD; 4921; -.
MGI; MGI:1345277; Ddr2.
eggNOG; KOG1094; Eukaryota.
eggNOG; ENOG410XQAI; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000043102; -.
HOVERGEN; HBG005461; -.
InParanoid; Q62371; -.
KO; K05125; -.
OMA; MSGGHIP; -.
OrthoDB; EOG091G05Y8; -.
PhylomeDB; Q62371; -.
TreeFam; TF317840; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
PRO; PR:Q62371; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026674; -.
CleanEx; MM_DDR2; -.
CleanEx; MM_TKT; -.
ExpressionAtlas; Q62371; baseline and differential.
Genevisible; Q62371; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IDA:MGI.
GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
GO; GO:0035988; P:chondrocyte proliferation; IMP:UniProtKB.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:UniProtKB.
GO; GO:0003416; P:endochondral bone growth; IMP:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:MGI.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR034299; DDR2.
InterPro; IPR000421; FA58C.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
PANTHER; PTHR24416:SF295; PTHR24416:SF295; 1.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00231; FA58C; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS01286; FA58C_2; 1.
PROSITE; PS50022; FA58C_3; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Osteogenesis;
Phosphoprotein; Receptor; Reference proteome; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 854 Discoidin domain-containing receptor 2.
/FTId=PRO_0000016747.
TOPO_DOM 22 399 Extracellular. {ECO:0000255}.
TRANSMEM 400 421 Helical. {ECO:0000255}.
TOPO_DOM 422 854 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 185 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
DOMAIN 563 848 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 569 577 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 709 709 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 608 608 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 471 471 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000269|PubMed:11884411}.
MOD_RES 735 735 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000250|UniProtKB:Q16832}.
MOD_RES 739 739 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000250|UniProtKB:Q16832}.
MOD_RES 740 740 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000250|UniProtKB:Q16832}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 185 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 73 177 {ECO:0000255|PROSITE-ProRule:PRU00081}.
MUTAGEN 471 471 Y->F: Reduces tyrosine phosphorylation by
90%; when associated with E-608.
{ECO:0000269|PubMed:11884411}.
MUTAGEN 608 608 K->E: Abolishes kinase activity. Reduces
tyrosine phosphorylation by 90%; when
associated with F-471.
{ECO:0000269|PubMed:11884411}.
SEQUENCE 854 AA; 96482 MW; 45CFD2BE9ED524D4 CRC64;
MIPIPRMPLV LLLLLLILGS AKAQVNPAIC RYPLGMSGGH IPDEDITASS QWSESTAAKY
GRLDSEEGDG AWCPEIPVQP DDLKEFLQID LRTLHFITLV GTQGRHAGGH GIEFAPMYKI
NYSRDGSRWI SWRNRHGKQV LDGNSNPYDV FLKDLEPPIV ARFVRLIPVT DHSMNVCMRV
ELYGCVWLDG LVSYNAPAGQ QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD
DFTQTHEYHV WPGYDYVGWR NESATNGFIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK
EVQCYFRSEA SEWEPTAVYF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY HFADTWMMFS
EITFQSDAAM YNNSGALPTS PMAPTTYDPM LKVDDSNTRI LIGCLVAIIF ILLAIIVIIL
WRQFWQKMLE KASRRMLDDE MTVSLSLPSE SSMFNNNRSS SPSEQESNST YDRIFPLRPD
YQEPSRLIRK LPEFAPGEEE SGCSGVVKPA QPNGPEGVPH YAEADIVNLQ GVTGGNTYCV
PAVTMDLLSG KDVAVEEFPR KLLAFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN
QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIRL LAVCITEDPL CMITEYMENG
DLNQFLSRHE PLSSCSSDAT VSYANLKFMA TQIASGMKYL SSLNFVHRDL ATRNCLVGKN
YTIKIADFGM SRNLYSGDYY RIQGRAVLPI RWMSWESILL GKFTTASDVW AFGVTLWETF
TFCQEQPYSQ LSDEQVIENT GEFFRDQGRQ IYLPQPALCP DSVYKLMLSC WRRETKHRPS
FQEIHLLLLQ QGAE


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