ID DDRA_CAEEL Reviewed; 766 AA.
AC Q18163;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Discoidin domain-containing receptor A {ECO:0000303|PubMed:23147028};
DE Flags: Precursor;
GN Name=ddr-1 {ECO:0000312|WormBase:C25F6.4};
GN ORFNames=C25F6.4 {ECO:0000312|WormBase:C25F6.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23147028; DOI=10.1016/j.ydbio.2012.11.001;
RA Unsoeld T., Park J.O., Hutter H.;
RT "Discoidin domain receptors guide axons along longitudinal tracts in C.
RT elegans.";
RL Dev. Biol. 374:142-152(2013).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27984580; DOI=10.1371/journal.pgen.1006475;
RA Hisamoto N., Nagamori Y., Shimizu T., Pastuhov S.I., Matsumoto K.;
RT "The C. elegans discoidin domain receptor DDR-2 modulates the Met-like RTK-
RT JNK signaling pathway in axon regeneration.";
RL PLoS Genet. 12:E1006475-E1006475(2016).
CC -!- FUNCTION: Receptor which, together with svh-4, is involved in axon
CC guidance to establish the tracts for the ventral and dorsal nerve cords
CC during nervous system development (PubMed:23147028). May play a role in
CC axon regeneration following injury in D-type motor neurons
CC (PubMed:27984580). {ECO:0000269|PubMed:23147028,
CC ECO:0000269|PubMed:27984580}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell projection, axon
CC {ECO:0000269|PubMed:23147028}. Perikaryon
CC {ECO:0000269|PubMed:23147028}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons in head and tail, some
CC motoneurons in ventral nerve cord, in PVP interneurons, pharynx and
CC stomato-intestinal muscle. {ECO:0000269|PubMed:23147028}.
CC -!- DEVELOPMENTAL STAGE: Expression begins during bean stage in hypodermal
CC cells. At the 2-fold stage, also expressed in a few head and tail
CC neurons. {ECO:0000269|PubMed:23147028}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Viable. No effect on axon regeneration 24 hours
CC following injury of D-type motor neurons. Double knockout with svh-4
CC results in a more enhanced axon regeneration defect of D-type motor
CC neurons as compared to the svh-4 single mutant.
CC {ECO:0000269|PubMed:27984580}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000305}.
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DR EMBL; BX284606; CCD65687.1; -; Genomic_DNA.
DR RefSeq; NP_508926.2; NM_076525.2.
DR AlphaFoldDB; Q18163; -.
DR SMR; Q18163; -.
DR STRING; 6239.C25F6.4.1; -.
DR GlyCosmos; Q18163; 7 sites, No reported glycans.
DR EPD; Q18163; -.
DR PaxDb; 6239-C25F6-4; -.
DR EnsemblMetazoa; C25F6.4.1; C25F6.4.1; WBGene00016104.
DR GeneID; 180817; -.
DR KEGG; cel:CELE_C25F6.4; -.
DR UCSC; C25F6.4; c. elegans.
DR AGR; WB:WBGene00016104; -.
DR WormBase; C25F6.4; CE45027; WBGene00016104; ddr-1.
DR eggNOG; KOG1094; Eukaryota.
DR GeneTree; ENSGT00970000196593; -.
DR HOGENOM; CLU_008873_1_0_1; -.
DR InParanoid; Q18163; -.
DR OMA; VNNEFTH; -.
DR OrthoDB; 2999496at2759; -.
DR PhylomeDB; Q18163; -.
DR PRO; PR:Q18163; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00016104; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IGI:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF372; TYROSINE-PROTEIN KINASE SHARK; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00231; FA58C; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Nucleotide-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..766
FT /note="Discoidin domain-containing receptor A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434038"
FT TOPO_DOM 19..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..180
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 195..351
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 519..766
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 475..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 24..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
SQ SEQUENCE 766 AA; 86196 MW; 31BDA3C9E13C7ABC CRC64;
MQIALVLLAI YGTTTTNTLR IDQCGENALG MQNGDIADSQ ITASSSFDKQ SVGPQNARLH
SELASGAWCP KPQINSKSYE FLQVTLNDTF LITSVETQGR YGNGTGREFA SHYMIDYLRP
GSQWIRYKNR TGHVYMDGNF DTTTPVIRVL DPPIVASRIR FVPSSKNTRT VCMRAEIHGC
KHEGVTYYST VPDGSRLDTL DFKDSMFEDS QIYTESGIKR GLGLLTDGFV AQASPFEKNQ
MNNSWIGWNR DTTDGRITIL FEFEEVHNFT DVVLATFGNR IDGIDVIFSQ DGKTFPLFSQ
ISSSERQSLN NTSRRYDFRV PLHNRAGRKV RISIKFSSDW MFLTEVHFTS AANLTLLSEK
IPPPSSAATQ QLLVVCGIIF LTIFACVAYC VSVCLKRRQK NKSVDSNVKK DLIITHMGNK
PTCHVFPSNG KLSNGHYEVA NDILYARSQK STLLSVSSKS TFSCRAIPPT WTDFNFPPPP
EGREEHTYSQ PVSPENSSNG SYKSVRKIQA LKKYPSSALL IGKAIGEGKF TMIKECIIFG
GLKCAHKSTK EEDCVHGTRA LGDEIACLLQ CGRHPRIVEL FGVDESYNLL LEHVEYGCIR
NFWMASEAPL DTEFLVRICK DIYSAMAYLE SIRIVHGHFT PNNILMDGEF HAKVCSPRGP
SHHAQLRYSA PESIVNNEFT HKSDAWAVAT TVYEMAYQCR QRPYEELTNE QIVDNACALL
DHQPNAVVPL MPTVFNYEIL QLLTRCFRVD QLERPTFERL VKPFQD
//
