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Protein

Epithelial discoidin domain-containing receptor 1

Gene

Ddr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi212 – 2121Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi231 – 2311Calcium 1By similarity
Metal bindingi231 – 2311Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi234 – 2341Calcium 2By similarity
Metal bindingi236 – 2361Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi254 – 2541Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi256 – 2561Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi361 – 3611Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi362 – 3621Calcium 2By similarity
Binding sitei652 – 6521ATPPROSITE-ProRule annotation
Active sitei763 – 7631Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi613 – 6219ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Lactation, Pregnancy

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Epithelial discoidin domain-containing receptor 1 (EC:2.7.10.1)
Short name:
Epithelial discoidin domain receptor 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 namesi
Name:Ddr1
Synonyms:Eddr1, Ptk3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2252. Ddr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 414393ExtracellularSequence AnalysisAdd
BLAST
Transmembranei415 – 43521HelicalSequence AnalysisAdd
BLAST
Topological domaini436 – 910475CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: RGD
  • integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 910891Epithelial discoidin domain-containing receptor 1PRO_0000016745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 186PROSITE-ProRule annotation
Disulfide bondi75 ↔ 178PROSITE-ProRule annotation
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi304 ↔ 349PROSITE-ProRule annotation
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
Modified residuei481 – 4811Phosphotyrosine; by autocatalysisBy similarity
Modified residuei510 – 5101Phosphotyrosine; by autocatalysisBy similarity
Modified residuei517 – 5171Phosphotyrosine; by autocatalysisBy similarity
Modified residuei737 – 7371Phosphotyrosine; by autocatalysisBy similarity
Modified residuei789 – 7891Phosphotyrosine; by autocatalysisBy similarity
Modified residuei793 – 7931Phosphotyrosine; by autocatalysisBy similarity
Modified residuei794 – 7941Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated in response to fibrillar collagen binding.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63474.

PTM databases

PhosphoSiteiQ63474.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ63474.

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ63474.
SMRiQ63474. Positions 28-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 186155F5/8 type CPROSITE-ProRule annotationAdd
BLAST
Domaini607 – 902296Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 368176DS-like domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi478 – 4814PPxY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi378 – 41235Gly/Pro-richAdd
BLAST
Compositional biasi473 – 598126Gly/Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ63474.
PhylomeDBiQ63474.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029566. DDR1.
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]
PANTHERiPTHR24416:SF65. PTHR24416:SF65. 1 hit.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS01285. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTGTLSSLL LLLLLVTIGD ADMKGHFDPA KCRYALGMQD RTIPDSDISV
60 70 80 90 100
SSSWSDSTAA RHSRLESSDG DGAWCPAGPV FPKEEEYLQV DLRRLHLVAL
110 120 130 140 150
VGTQGRHAGG LGKEFSRSYR LRYSRDGRRW MDWKDRWGQE VISGNEDPGG
160 170 180 190 200
VVLKDLGPPM VARLVRFYPR ADRVMSVCLR VELYGCLWRD GLLSYTAPVG
210 220 230 240 250
QTMQLSEMVY LNDSTYDGYT AGGLQYGGLG QLADGVVGLD DFRQSQELRV
260 270 280 290 300
WPGYDYVGWS NHSFPSGYVE MEFEFDRLRS FQTMQVHCNN MHTLGARLPG
310 320 330 340 350
GVECRFKRGP AMAWEGEPVH HALGGSLGDP RARAISVPLG GHVGRFLQCR
360 370 380 390 400
FLFAGPWLLF SEISFISDVV NDSSDTFPPA PWWPPGPPPT NFSSLELEPR
410 420 430 440 450
GQQPVAKAEG SPTAILIGCL VAIILLLLLI IALMLWRLHW RRLLSKAERR
460 470 480 490 500
VLEEELTVHL SVPGDTILIN NRPGPREPPP YQEPRPRGTP THSAPCVPNG
510 520 530 540 550
SALLLSNPAY RLLLATYARP PRGPGPPTPA WAKPTNTQAC SGDYMEPEKP
560 570 580 590 600
GAPLLPPPPQ NSVPHYAEAD IVTLQGVTGG NTYAVPALPP GAVGDGPPRV
610 620 630 640 650
DFPRSRLRFK EKLGEGQFGE VHLCEVEDPQ DLVTSDFPIS VQKGHPLLVA
660 670 680 690 700
VKILRPDATK NARNDFLKEV KIMSRLKDLN IIRLLGVCVQ DDPLCMITDY
710 720 730 740 750
MENGDLNQFL SAHQLENKVT QGLPGDRESD QGPTISYPML LHVGAQIASG
760 770 780 790 800
MRYLATLNFV HRDLATRNCL VGENFTIKIA DFGMSRNLYA GDYYRVQGRA
810 820 830 840 850
VLPIRWMAWE CILMGKFTTA SDVWAFGVTL WEVLMLCRSQ PFGQLTDEQV
860 870 880 890 900
IENAGEFFRD QGRQVYLSRP PACPQTLYEL MLRCWSREPE QRPPFSQLHR
910
FLADDALNTV
Length:910
Mass (Da):101,165
Last modified:November 1, 1996 - v1
Checksum:i7E7FFA1DCB029806
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26525 Genomic DNA. Translation: AAA21089.1.
PIRiA53137.
UniGeneiRn.7807.

Genome annotation databases

UCSCiRGD:2252. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26525 Genomic DNA. Translation: AAA21089.1.
PIRiA53137.
UniGeneiRn.7807.

3D structure databases

ProteinModelPortaliQ63474.
SMRiQ63474. Positions 28-187.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ63474.

Proteomic databases

PaxDbiQ63474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2252. rat.

Organism-specific databases

RGDi2252. Ddr1.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000043102.
HOVERGENiHBG005461.
InParanoidiQ63474.
PhylomeDBiQ63474.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

PROiQ63474.

Gene expression databases

GenevestigatoriQ63474.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR029566. DDR1.
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]
PANTHERiPTHR24416:SF65. PTHR24416:SF65. 1 hit.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS01285. 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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDDR1_RAT
AccessioniPrimary (citable) accession number: Q63474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.