ID DDR1_RAT Reviewed; 910 AA.
AC Q63474;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 111.
DE RecName: Full=Epithelial discoidin domain-containing receptor 1;
DE Short=Epithelial discoidin domain receptor 1;
DE EC=2.7.10.1;
DE AltName: Full=CD167 antigen-like family member A;
DE AltName: Full=Cell adhesion kinase;
DE AltName: Full=Discoidin receptor tyrosine kinase;
DE AltName: Full=Protein-tyrosine kinase 3;
DE AltName: Full=Tyrosine kinase DDR;
DE AltName: Full=Tyrosine-protein kinase CAK;
DE AltName: CD_antigen=CD167a;
DE Flags: Precursor;
GN Name=Ddr1; Synonyms=Eddr1, Ptk3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8127887; DOI=10.1073/pnas.91.5.1819;
RA Sanchez M.P., Tapley P., Saini S.S., He B., Pulido D., Barbacid M.;
RT "Multiple tyrosine protein kinases in rat hippocampal neurons:
RT isolation of Ptk-3, a receptor expressed in proliferative zones of the
RT developing brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1819-1823(1994).
CC -!- FUNCTION: Tyrosine kinase that functions as cell surface receptor
CC for fibrillar collagen and regulates cell attachment to the
CC extracellular matrix, remodeling of the extracellular matrix, cell
CC migration, differentiation, survival and cell proliferation.
CC Collagen binding triggers a signaling pathway that involves SRC
CC and leads to the activation of MAP kinases. Regulates remodeling
CC of the extracellular matrix by up-regulation of the matrix
CC metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates
CC cell migration and wound healing. Promotes smooth muscle cell
CC migration, and thereby contributes to arterial wound healing. Also
CC plays a role in tumor cell invasion. Phosphorylates PTPN11.
CC Required for normal blastocyst implantation during pregnancy, for
CC normal mammary gland differentiation and normal lactation.
CC Required for normal ear morphology and normal hearing (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
CC -!- SUBUNIT: Homodimer. Interacts (via PPxY motif) with WWC1 (via WW
CC domains) in a collagen-regulated manner. Forms a tripartite
CC complex with WWC1 and PRKCZ, but predominantly in the absence of
CC collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts
CC with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with
CC PTPN11. Interacts with NCK2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (By similarity).
CC -!- TISSUE SPECIFICITY: Various embryonic and adult tissues; also
CC proliferative zones of the developing brain; hippocampal neurons.
CC -!- PTM: Autophosphorylated in response to fibrillar collagen binding
CC (By similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC -!- SIMILARITY: Contains 1 F5/8 type C domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; L26525; AAA21089.1; -; Genomic_DNA.
DR IPI; IPI00209121; -.
DR PIR; A53137; A53137.
DR UniGene; Rn.7807; -.
DR ProteinModelPortal; Q63474; -.
DR SMR; Q63474; 28-187.
DR PhosphoSite; Q63474; -.
DR PaxDb; Q63474; -.
DR UCSC; RGD:2252; rat.
DR RGD; 2252; Ddr1.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000043102; -.
DR HOVERGEN; HBG005461; -.
DR InParanoid; Q63474; -.
DR BRENDA; 2.7.10.1; 5301.
DR ArrayExpress; Q63474; -.
DR Genevestigator; Q63474; -.
DR GermOnline; ENSRNOG00000000830; Rattus norvegicus.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR GO; GO:0031100; P:organ regeneration; IEP:RGD.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
DR GO; GO:0010715; P:regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; IEP:RGD.
DR GO; GO:0014909; P:smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0061302; P:smooth muscle cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR InterPro; IPR000421; Coagulation_fac_5/8-C_type_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Cell membrane; Complete proteome;
KW Disulfide bond; Glycoprotein; Kinase; Lactation; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Pregnancy;
KW Receptor; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 910 Epithelial discoidin domain-containing
FT receptor 1.
FT /FTId=PRO_0000016745.
FT TOPO_DOM 22 414 Extracellular (Potential).
FT TRANSMEM 415 435 Helical; (Potential).
FT TOPO_DOM 436 910 Cytoplasmic (Potential).
FT DOMAIN 32 186 F5/8 type C.
FT DOMAIN 607 902 Protein kinase.
FT NP_BIND 613 621 ATP (By similarity).
FT REGION 193 368 DS-like domain (By similarity).
FT MOTIF 478 481 PPxY motif.
FT COMPBIAS 378 412 Gly/Pro-rich.
FT COMPBIAS 473 598 Gly/Pro-rich.
FT ACT_SITE 763 763 Proton acceptor (By similarity).
FT METAL 212 212 Calcium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 231 231 Calcium 1 (By similarity).
FT METAL 231 231 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 234 234 Calcium 2 (By similarity).
FT METAL 236 236 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 254 254 Calcium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 256 256 Calcium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 361 361 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 362 362 Calcium 2 (By similarity).
FT BINDING 652 652 ATP (By similarity).
FT MOD_RES 510 510 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 737 737 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 789 789 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 793 793 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 794 794 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT CARBOHYD 212 212 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 261 261 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 371 371 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 391 391 N-linked (GlcNAc...) (Potential).
FT DISULFID 32 186 By similarity.
FT DISULFID 75 178 By similarity.
FT DISULFID 304 349 By similarity.
SQ SEQUENCE 910 AA; 101165 MW; 7E7FFA1DCB029806 CRC64;
MGTGTLSSLL LLLLLVTIGD ADMKGHFDPA KCRYALGMQD RTIPDSDISV SSSWSDSTAA
RHSRLESSDG DGAWCPAGPV FPKEEEYLQV DLRRLHLVAL VGTQGRHAGG LGKEFSRSYR
LRYSRDGRRW MDWKDRWGQE VISGNEDPGG VVLKDLGPPM VARLVRFYPR ADRVMSVCLR
VELYGCLWRD GLLSYTAPVG QTMQLSEMVY LNDSTYDGYT AGGLQYGGLG QLADGVVGLD
DFRQSQELRV WPGYDYVGWS NHSFPSGYVE MEFEFDRLRS FQTMQVHCNN MHTLGARLPG
GVECRFKRGP AMAWEGEPVH HALGGSLGDP RARAISVPLG GHVGRFLQCR FLFAGPWLLF
SEISFISDVV NDSSDTFPPA PWWPPGPPPT NFSSLELEPR GQQPVAKAEG SPTAILIGCL
VAIILLLLLI IALMLWRLHW RRLLSKAERR VLEEELTVHL SVPGDTILIN NRPGPREPPP
YQEPRPRGTP THSAPCVPNG SALLLSNPAY RLLLATYARP PRGPGPPTPA WAKPTNTQAC
SGDYMEPEKP GAPLLPPPPQ NSVPHYAEAD IVTLQGVTGG NTYAVPALPP GAVGDGPPRV
DFPRSRLRFK EKLGEGQFGE VHLCEVEDPQ DLVTSDFPIS VQKGHPLLVA VKILRPDATK
NARNDFLKEV KIMSRLKDLN IIRLLGVCVQ DDPLCMITDY MENGDLNQFL SAHQLENKVT
QGLPGDRESD QGPTISYPML LHVGAQIASG MRYLATLNFV HRDLATRNCL VGENFTIKIA
DFGMSRNLYA GDYYRVQGRA VLPIRWMAWE CILMGKFTTA SDVWAFGVTL WEVLMLCRSQ
PFGQLTDEQV IENAGEFFRD QGRQVYLSRP PACPQTLYEL MLRCWSREPE QRPPFSQLHR
FLADDALNTV
//
