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Database: UniProt
Entry: S9YX81_CAMFR
LinkDB: S9YX81_CAMFR
Original site: S9YX81_CAMFR 
ID   S9YX81_CAMFR            Unreviewed;      1110 AA.
AC   S9YX81;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Platelet-derived growth factor receptor beta {ECO:0000256|ARBA:ARBA00020507, ECO:0000256|PIRNR:PIRNR500948};
DE            Short=PDGF-R-beta {ECO:0000256|PIRNR:PIRNR500948};
DE            Short=PDGFR-beta {ECO:0000256|PIRNR:PIRNR500948};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR500948};
DE   AltName: Full=Beta platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029696, ECO:0000256|PIRNR:PIRNR500948};
DE   AltName: Full=Beta-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00032009, ECO:0000256|PIRNR:PIRNR500948};
GN   ORFNames=CB1_000163034 {ECO:0000313|EMBL:EPY88625.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY88625.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY88625.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC       for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
CC       and PDGFB, and plays an essential role in the regulation of embryonic
CC       development, cell proliferation, survival, differentiation, chemotaxis
CC       and migration. Plays an essential role in blood vessel development by
CC       promoting proliferation, migration and recruitment of pericytes and
CC       smooth muscle cells to endothelial cells.
CC       {ECO:0000256|PIRNR:PIRNR500948}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171,
CC         ECO:0000256|PIRNR:PIRNR500948};
CC   -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC       heterodimers formed by PDGFA and PDGFB.
CC       {ECO:0000256|PIRNR:PIRNR500948}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR500948};
CC       Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR500948}.
CC       Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR500948}. Lysosome lumen
CC       {ECO:0000256|PIRNR:PIRNR500948}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU000311}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC       {ECO:0000256|PIRNR:PIRNR500948, ECO:0000256|RuleBase:RU000311}.
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DR   EMBL; KB016459; EPY88625.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9YX81; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027288; PGFRB.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR500948};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR500948}; Chemotaxis {ECO:0000256|PIRNR:PIRNR500948};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR500948};
KW   Developmental protein {ECO:0000256|PIRNR:PIRNR500948};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|PIRNR:PIRNR500948};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228, ECO:0000256|PIRNR:PIRNR500948};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500948};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500948,
KW   ECO:0000256|PIRSR:PIRSR000615-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500948};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR500948};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR500948}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           41..1110
FT                   /note="Platelet-derived growth factor receptor beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004561645"
FT   TRANSMEM        539..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          222..314
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          607..969
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1025..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        833
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         586
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         613..621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500948-2"
FT   BINDING         614..621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         689..695
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         837
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         838
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         851
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1110 AA;  124275 MW;  A27759D229ED6489 CRC64;
     MRMCVQDTMW LPSAMPAPVL KGQELLLPLL LLLGPQASWG LVITPPGPEL VLNLSSTFVL
     TCSGPAPVVW ERMSQNPPQE ITKTQDGTFS SKLTLANVTG LHTGEYFCTY NGSHGLEASE
     RKRLYIFVPD PTIGFLPVDP EELFIFLTEI TEITIPCRVT DPRLVVTLHE KKVDVPLPIS
     YDHQRGFSGT FEDKTYVCKT TIGDREVDSD AYYVYSLQVS SINVSVSAVQ TVVRQGENIT
     IMCIVTGNEV VNFEWTYPRM ESGRLVEPVT DFLFEMPHIR SILHIPSAEL GDSGTYICNV
     SDSVSDHRDE KAINVTVVES GYVQLLEELD PVQFAELHRS RTLHVVFEAY PPPTVMWFKD
     NRTLGDSSAG EIVLSTRNVS ETRYVSELTL VRVKVAEAGS YTMRAFHEDA EAQLSFQLQV
     NVPVRVLELS ESHPASGEQT VRCRGRGMPQ PHLTWSTCSD LKRCPRELPP TPLGNSSQEE
     SQLETNVTYW AEEQEFEVVS TLRLRRVDQP LSVRCTLHNL LGHDMQEVTV VPHSLPFKVV
     VISAILALVV LTIISLIILI MLWQKKPRYE IRWKVIESVS SDGHEYIYVD PMQLPYDSTW
     ELPRDQLVLG RTLGSGAFGQ VVEATAHGLS HSQATMKVAV KMLKSTARSS EKQALMSELK
     IMSHLGPHLN VVNLLGACTK GGPIYIITEY CRYGDLVDYL HRNKHTFLQR CSDKRRPPSA
     ELYSNALPGG LPLLSHVSLP GESDGGYMDM SKDESVDYVP MLDMKGDVKY ADIESSNYMA
     PYDNYVPSAP ERTCRATLIN ESPVLSYTDL VGFSYQVANG MEFLASKNCV HRDLAARNVL
     ICEGKLVKIC DFGLARDIMR DSNYISKGST FLPLKWMAPE SIFNSLYTTL SDVWSFGILL
     WEIFTLGGTP YPELPMNEQF YNAIKRGYRM AQPAHASDEI YEIMQKCWEE KFEIRPPFSQ
     LVLLLERLLG EGYKKKYQQV DEEFLRSDHP AVLRSQARLP GFHGLRSPLD TSSVLYTAVQ
     PEGDNDYIIP LPDPKPEVAD EGPLEGSPSL ASSTLNEVNT SSTISCDSPL EPQEEPEPQP
     ECQVEPEPEP ERSPDSSCLG PRAEAEDSFL
//
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