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Q63474 (DDR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Epithelial discoidin domain-containing receptor 1

Short name=Epithelial discoidin domain receptor 1
EC=2.7.10.1
Alternative name(s):
CD167 antigen-like family member A
Cell adhesion kinase
Discoidin receptor tyrosine kinase
Protein-tyrosine kinase 3
Tyrosine kinase DDR
Tyrosine-protein kinase CAK
CD_antigen=CD167a
Gene names
Name:Ddr1
Synonyms:Eddr1, Ptk3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing By similarity.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Homodimer. Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner. Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with PTPN11. Interacts with NCK2 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Various embryonic and adult tissues; also proliferative zones of the developing brain; hippocampal neurons.

Post-translational modification

Autophosphorylated in response to fibrillar collagen binding By similarity.

Sequence similarities

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

Contains 1 F5/8 type C domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processLactation
Pregnancy
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen-activated tyrosine kinase receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

female pregnancy

Inferred from electronic annotation. Source: UniProtKB-KW

lactation

Inferred from electronic annotation. Source: UniProtKB-KW

organ regeneration

Inferred from expression pattern PubMed 15218324. Source: RGD

peptidyl-tyrosine autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of extracellular matrix disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

skin development

Inferred from expression pattern PubMed 11304604. Source: RGD

smooth muscle cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

smooth muscle cell-matrix adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

wound healing, spreading of cells

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 15218324. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

collagen binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase collagen receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 910891Epithelial discoidin domain-containing receptor 1
PRO_0000016745

Regions

Topological domain22 – 414393Extracellular Potential
Transmembrane415 – 43521Helical; Potential
Topological domain436 – 910475Cytoplasmic Potential
Domain32 – 186155F5/8 type C
Domain607 – 902296Protein kinase
Nucleotide binding613 – 6219ATP By similarity
Region193 – 368176DS-like domain By similarity
Motif478 – 4814PPxY motif
Compositional bias378 – 41235Gly/Pro-rich
Compositional bias473 – 598126Gly/Pro-rich

Sites

Active site7631Proton acceptor By similarity
Metal binding2121Calcium 1; via carbonyl oxygen By similarity
Metal binding2311Calcium 1 By similarity
Metal binding2311Calcium 2; via carbonyl oxygen By similarity
Metal binding2341Calcium 2 By similarity
Metal binding2361Calcium 2; via carbonyl oxygen By similarity
Metal binding2541Calcium 1; via carbonyl oxygen By similarity
Metal binding2561Calcium 1; via carbonyl oxygen By similarity
Metal binding3611Calcium 2; via carbonyl oxygen By similarity
Metal binding3621Calcium 2 By similarity
Binding site6521ATP By similarity

Amino acid modifications

Modified residue5101Phosphotyrosine; by autocatalysis By similarity
Modified residue7371Phosphotyrosine; by autocatalysis By similarity
Modified residue7891Phosphotyrosine; by autocatalysis By similarity
Modified residue7931Phosphotyrosine; by autocatalysis By similarity
Modified residue7941Phosphotyrosine; by autocatalysis By similarity
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 186 By similarity
Disulfide bond75 ↔ 178 By similarity
Disulfide bond304 ↔ 349 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63474 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7E7FFA1DCB029806

FASTA910101,165
        10         20         30         40         50         60 
MGTGTLSSLL LLLLLVTIGD ADMKGHFDPA KCRYALGMQD RTIPDSDISV SSSWSDSTAA 

        70         80         90        100        110        120 
RHSRLESSDG DGAWCPAGPV FPKEEEYLQV DLRRLHLVAL VGTQGRHAGG LGKEFSRSYR 

       130        140        150        160        170        180 
LRYSRDGRRW MDWKDRWGQE VISGNEDPGG VVLKDLGPPM VARLVRFYPR ADRVMSVCLR 

       190        200        210        220        230        240 
VELYGCLWRD GLLSYTAPVG QTMQLSEMVY LNDSTYDGYT AGGLQYGGLG QLADGVVGLD 

       250        260        270        280        290        300 
DFRQSQELRV WPGYDYVGWS NHSFPSGYVE MEFEFDRLRS FQTMQVHCNN MHTLGARLPG 

       310        320        330        340        350        360 
GVECRFKRGP AMAWEGEPVH HALGGSLGDP RARAISVPLG GHVGRFLQCR FLFAGPWLLF 

       370        380        390        400        410        420 
SEISFISDVV NDSSDTFPPA PWWPPGPPPT NFSSLELEPR GQQPVAKAEG SPTAILIGCL 

       430        440        450        460        470        480 
VAIILLLLLI IALMLWRLHW RRLLSKAERR VLEEELTVHL SVPGDTILIN NRPGPREPPP 

       490        500        510        520        530        540 
YQEPRPRGTP THSAPCVPNG SALLLSNPAY RLLLATYARP PRGPGPPTPA WAKPTNTQAC 

       550        560        570        580        590        600 
SGDYMEPEKP GAPLLPPPPQ NSVPHYAEAD IVTLQGVTGG NTYAVPALPP GAVGDGPPRV 

       610        620        630        640        650        660 
DFPRSRLRFK EKLGEGQFGE VHLCEVEDPQ DLVTSDFPIS VQKGHPLLVA VKILRPDATK 

       670        680        690        700        710        720 
NARNDFLKEV KIMSRLKDLN IIRLLGVCVQ DDPLCMITDY MENGDLNQFL SAHQLENKVT 

       730        740        750        760        770        780 
QGLPGDRESD QGPTISYPML LHVGAQIASG MRYLATLNFV HRDLATRNCL VGENFTIKIA 

       790        800        810        820        830        840 
DFGMSRNLYA GDYYRVQGRA VLPIRWMAWE CILMGKFTTA SDVWAFGVTL WEVLMLCRSQ 

       850        860        870        880        890        900 
PFGQLTDEQV IENAGEFFRD QGRQVYLSRP PACPQTLYEL MLRCWSREPE QRPPFSQLHR 

       910 
FLADDALNTV 

« Hide

References

[1]"Multiple tyrosine protein kinases in rat hippocampal neurons: isolation of Ptk-3, a receptor expressed in proliferative zones of the developing brain."
Sanchez M.P., Tapley P., Saini S.S., He B., Pulido D., Barbacid M.
Proc. Natl. Acad. Sci. U.S.A. 91:1819-1823(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26525 Genomic DNA. Translation: AAA21089.1.
PIRA53137.
UniGeneRn.7807.

3D structure databases

ProteinModelPortalQ63474.
SMRQ63474. Positions 28-187.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ63474.

Proteomic databases

PaxDbQ63474.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2252. rat.

Organism-specific databases

RGD2252. Ddr1.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000043102.
HOVERGENHBG005461.
InParanoidQ63474.
PhylomeDBQ63474.

Enzyme and pathway databases

BRENDA2.7.10.1. 5301.

Gene expression databases

GenevestigatorQ63474.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ63474.

Entry information

Entry nameDDR1_RAT
AccessionPrimary (citable) accession number: Q63474
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 119 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