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Database: UniProt
Entry: Q63474
LinkDB: Q63474
Original site: Q63474 
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   01-OCT-2014, entry version 121.
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 F5/8 type C domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00081}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; L26525; AAA21089.1; -; Genomic_DNA.
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   PhylomeDB; Q63474; -.
DR   BRENDA; 2.7.10.1; 5301.
DR   PRO; PR:Q63474; -.
DR   Genevestigator; Q63474; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR   GO; GO:0016021; C:integral component of 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:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; 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   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR000421; Coagulation_fac_5/8-C_type_dom.
DR   InterPro; IPR029566; DDR1.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_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   PANTHER; PTHR24416:SF65; PTHR24416:SF65; 1.
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; SSF49785; 1.
DR   SUPFAM; SSF56112; SSF56112; 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       {ECO:0000255}.
FT   CHAIN        20    910       Epithelial discoidin domain-containing
FT                                receptor 1.
FT                                /FTId=PRO_0000016745.
FT   TOPO_DOM     22    414       Extracellular. {ECO:0000255}.
FT   TRANSMEM    415    435       Helical. {ECO:0000255}.
FT   TOPO_DOM    436    910       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       32    186       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      607    902       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     613    621       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      193    368       DS-like domain. {ECO:0000250}.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   METAL       212    212       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       231    231       Calcium 1. {ECO:0000250}.
FT   METAL       231    231       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       234    234       Calcium 2. {ECO:0000250}.
FT   METAL       236    236       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       254    254       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       256    256       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       361    361       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       362    362       Calcium 2. {ECO:0000250}.
FT   BINDING     652    652       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     481    481       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     510    510       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     517    517       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     737    737       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     789    789       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     793    793       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     794    794       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    261    261       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     32    186       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID     75    178       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID    304    349       {ECO:0000255|PROSITE-ProRule:PRU00081}.
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
//
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