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Q9NRA1

- PDGFC_HUMAN

UniProt

Q9NRA1 - PDGFC_HUMAN

Protein

Platelet-derived growth factor C

Gene

PDGFC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.12 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei225 – 2262Cleavage
    Sitei231 – 2322CleavageSequence Analysis
    Sitei234 – 2352CleavageSequence Analysis

    GO - Molecular functioni

    1. platelet-derived growth factor receptor binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. activation of transmembrane receptor protein tyrosine kinase activity Source: Ensembl
    2. cellular response to amino acid stimulus Source: Ensembl
    3. central nervous system development Source: UniProtKB
    4. organ morphogenesis Source: Ensembl
    5. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
    6. positive regulation of cell division Source: UniProtKB-KW
    7. positive regulation of DNA replication Source: BHF-UCL
    8. positive regulation of fibroblast proliferation Source: BHF-UCL
    9. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Enzyme and pathway databases

    ReactomeiREACT_16888. Signaling by PDGF.
    SignaLinkiQ9NRA1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-derived growth factor C
    Short name:
    PDGF-C
    Alternative name(s):
    Fallotein
    Spinal cord-derived growth factor
    Short name:
    SCDGF
    VEGF-E
    Cleaved into the following 2 chains:
    Platelet-derived growth factor C, receptor-binding form
    Short name:
    PDGFC receptor-binding form
    Gene namesi
    Name:PDGFC
    Synonyms:SCDGF
    ORF Names:UNQ174/PRO200
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8801. PDGFC.

    Subcellular locationi

    Cytoplasm. Secreted. Nucleus. Cytoplasmic granule
    Note: Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: HPA
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular space Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi membrane Source: Reactome
    8. nucleus Source: UniProtKB-SubCell
    9. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi124 – 1241C → S: Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells. 1 Publication
    Mutagenesisi231 – 2311R → A: Essential for cleavage by PLAT. 1 Publication
    Mutagenesisi232 – 2321K → A: Not essential for cleavage by PLAT. 1 Publication
    Mutagenesisi234 – 2341R → A: Not essential for cleavage by PLAT. 1 Publication

    Organism-specific databases

    PharmGKBiPA33146.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343872
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 345323Platelet-derived growth factor C, latent formPRO_0000343871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi55 – 551N-linked (GlcNAc...)By similarity
    Disulfide bondi104 ↔ 124PROSITE-ProRule annotation
    Disulfide bondi250 ↔ 2941 Publication
    Disulfide bondi274 – 274Interchain (with C-286)1 Publication
    Disulfide bondi280 ↔ 3351 Publication
    Disulfide bondi286 – 286Interchain (with C-274)1 Publication
    Disulfide bondi287 ↔ 3371 Publication

    Post-translational modificationi

    Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG.
    Sumoylated with SUMO1.1 Publication
    N-glycosylated.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9NRA1.
    PRIDEiQ9NRA1.

    PTM databases

    PhosphoSiteiQ9NRA1.

    Expressioni

    Tissue specificityi

    Expressed in the fallopian tube, vascular smooth muscle cells in kidney, breast and colon and in visceral smooth muscle of the gastrointestinal tract. Highly expressed in retinal pigment epithelia. Expressed in medulloblastoma. In the kidney, constitutively expressed in parietal epithelial cells of Bowman's capsule, tubular epithelial cells and in arterial endothelial cells (at protein level). Highly expressed in the platelets, prostate, testis and uterus. Higher expression is observed in uterine leiomyomata. Weaker expression in the spleen, thymus, heart, pancreas, liver, ovary cells and small intestine, and negligible expression in the colon and peripheral blood leukocytes.9 Publications

    Developmental stagei

    In the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level).1 Publication

    Inductioni

    Up-regulated by EWS-FLI1 chimeric transcription factor in tumor derived cells. Up-regulated in podocytes and interstitial cells after injury/activation of these cells. FGF2 activates PDGFC transcription via EGR1. Up-regulated by TGFB1 in concert with FGF2.4 Publications

    Gene expression databases

    ArrayExpressiQ9NRA1.
    BgeeiQ9NRA1.
    CleanExiHS_PDGFC.
    GenevestigatoriQ9NRA1.

    Organism-specific databases

    HPAiHPA009134.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB domain) with PLAT (via kringle domain).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDGFRAP162342EBI-8833587,EBI-2861522

    Protein-protein interaction databases

    BioGridi121032. 5 interactions.
    DIPiDIP-59339N.
    IntActiQ9NRA1. 1 interaction.
    STRINGi9606.ENSP00000274071.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRA1.
    SMRiQ9NRA1. Positions 49-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 163118CUBPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDGF/VEGF growth factor family.Curated
    Contains 1 CUB domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG74970.
    HOGENOMiHOG000185996.
    HOVERGENiHBG057324.
    InParanoidiQ9NRA1.
    KOiK05450.
    OMAiDCVCRGN.
    OrthoDBiEOG7VB2FN.
    PhylomeDBiQ9NRA1.
    TreeFamiTF332130.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    2.60.120.290. 1 hit.
    InterProiIPR000859. CUB_dom.
    IPR029034. Cystine-knot_cytokine.
    IPR000072. PDGF/VEGF_dom.
    [Graphical view]
    PfamiPF00431. CUB. 1 hit.
    PF00341. PDGF. 1 hit.
    [Graphical view]
    SMARTiSM00042. CUB. 1 hit.
    SM00141. PDGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 1 hit.
    SSF57501. SSF57501. 1 hit.
    PROSITEiPS01180. CUB. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRA1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLFGLLLLT SALAGQRQGT QAESNLSSKF QFSSNKEQNG VQDPQHERII    50
    TVSTNGSIHS PRFPHTYPRN TVLVWRLVAV EENVWIQLTF DERFGLEDPE 100
    DDICKYDFVE VEEPSDGTIL GRWCGSGTVP GKQISKGNQI RIRFVSDEYF 150
    PSEPGFCIHY NIVMPQFTEA VSPSVLPPSA LPLDLLNNAI TAFSTLEDLI 200
    RYLEPERWQL DLEDLYRPTW QLLGKAFVFG RKSRVVDLNL LTEEVRLYSC 250
    TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPSK 300
    VTKKYHEVLQ LRPKTGVRGL HKSLTDVALE HHEECDCVCR GSTGG 345
    Length:345
    Mass (Da):39,029
    Last modified:July 22, 2008 - v2
    Checksum:iCDE9E51F40633E78
    GO
    Isoform 2 (identifier: Q9NRA1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         244-306: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:282
    Mass (Da):31,808
    Checksum:i8426CEB8FF9AA45B
    GO
    Isoform 3 (identifier: Q9NRA1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-167: GFCIHYNIVMPQF → SNRGGKIIQLHTS
         168-345: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:167
    Mass (Da):18,784
    Checksum:i60023851D9FE5E65
    GO
    Isoform 4 (identifier: Q9NRA1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:182
    Mass (Da):20,609
    Checksum:iF5B9733D3794B1B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91L → V in AAF80597. (PubMed:10806482)Curated
    Sequence conflicti18 – 181Q → R in AAF80597. (PubMed:10806482)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 163163Missing in isoform 4. 2 PublicationsVSP_047606Add
    BLAST
    Alternative sequencei155 – 16713GFCIH…VMPQF → SNRGGKIIQLHTS in isoform 3. CuratedVSP_034701Add
    BLAST
    Alternative sequencei168 – 345178Missing in isoform 3. CuratedVSP_034702Add
    BLAST
    Alternative sequencei244 – 30663Missing in isoform 2. CuratedVSP_034703Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091434 mRNA. Translation: AAF00049.1.
    AB033831 mRNA. Translation: BAB03266.1.
    AF244813 mRNA. Translation: AAF80597.1.
    AF260738 mRNA. Translation: AAK51637.1.
    AM922296 mRNA. Translation: CAP58278.1.
    AY358493 mRNA. Translation: AAQ88857.1.
    AK300480 mRNA. Translation: BAG62196.1.
    AC092608 Genomic DNA. Translation: AAY40906.1.
    AC093325 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04874.1.
    CH471056 Genomic DNA. Translation: EAX04875.1.
    BC136662 mRNA. Translation: AAI36663.1.
    CCDSiCCDS3795.1. [Q9NRA1-1]
    RefSeqiNP_057289.1. NM_016205.2. [Q9NRA1-1]
    UniGeneiHs.570855.

    Genome annotation databases

    EnsembliENST00000422544; ENSP00000410048; ENSG00000145431. [Q9NRA1-2]
    ENST00000502773; ENSP00000422464; ENSG00000145431. [Q9NRA1-1]
    GeneIDi56034.
    KEGGihsa:56034.
    UCSCiuc003iph.2. human. [Q9NRA1-1]

    Polymorphism databases

    DMDMi205830662.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091434 mRNA. Translation: AAF00049.1 .
    AB033831 mRNA. Translation: BAB03266.1 .
    AF244813 mRNA. Translation: AAF80597.1 .
    AF260738 mRNA. Translation: AAK51637.1 .
    AM922296 mRNA. Translation: CAP58278.1 .
    AY358493 mRNA. Translation: AAQ88857.1 .
    AK300480 mRNA. Translation: BAG62196.1 .
    AC092608 Genomic DNA. Translation: AAY40906.1 .
    AC093325 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04874.1 .
    CH471056 Genomic DNA. Translation: EAX04875.1 .
    BC136662 mRNA. Translation: AAI36663.1 .
    CCDSi CCDS3795.1. [Q9NRA1-1 ]
    RefSeqi NP_057289.1. NM_016205.2. [Q9NRA1-1 ]
    UniGenei Hs.570855.

    3D structure databases

    ProteinModelPortali Q9NRA1.
    SMRi Q9NRA1. Positions 49-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121032. 5 interactions.
    DIPi DIP-59339N.
    IntActi Q9NRA1. 1 interaction.
    STRINGi 9606.ENSP00000274071.

    PTM databases

    PhosphoSitei Q9NRA1.

    Polymorphism databases

    DMDMi 205830662.

    Proteomic databases

    PaxDbi Q9NRA1.
    PRIDEi Q9NRA1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000422544 ; ENSP00000410048 ; ENSG00000145431 . [Q9NRA1-2 ]
    ENST00000502773 ; ENSP00000422464 ; ENSG00000145431 . [Q9NRA1-1 ]
    GeneIDi 56034.
    KEGGi hsa:56034.
    UCSCi uc003iph.2. human. [Q9NRA1-1 ]

    Organism-specific databases

    CTDi 56034.
    GeneCardsi GC04M157682.
    HGNCi HGNC:8801. PDGFC.
    HPAi HPA009134.
    MIMi 608452. gene.
    neXtProti NX_Q9NRA1.
    PharmGKBi PA33146.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74970.
    HOGENOMi HOG000185996.
    HOVERGENi HBG057324.
    InParanoidi Q9NRA1.
    KOi K05450.
    OMAi DCVCRGN.
    OrthoDBi EOG7VB2FN.
    PhylomeDBi Q9NRA1.
    TreeFami TF332130.

    Enzyme and pathway databases

    Reactomei REACT_16888. Signaling by PDGF.
    SignaLinki Q9NRA1.

    Miscellaneous databases

    GeneWikii PDGFC.
    GenomeRNAii 56034.
    NextBioi 35475084.
    PROi Q9NRA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRA1.
    Bgeei Q9NRA1.
    CleanExi HS_PDGFC.
    Genevestigatori Q9NRA1.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    2.60.120.290. 1 hit.
    InterProi IPR000859. CUB_dom.
    IPR029034. Cystine-knot_cytokine.
    IPR000072. PDGF/VEGF_dom.
    [Graphical view ]
    Pfami PF00431. CUB. 1 hit.
    PF00341. PDGF. 1 hit.
    [Graphical view ]
    SMARTi SM00042. CUB. 1 hit.
    SM00141. PDGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 1 hit.
    SSF57501. SSF57501. 1 hit.
    PROSITEi PS01180. CUB. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel platelet-derived growth factor-like gene, fallotein, in the human reproductive tract."
      Tsai Y.J., Lee R.K., Lin S.P., Chen Y.H.
      Biochim. Biophys. Acta 1492:196-202(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Uterus.
    2. "A novel gene derived from developing spinal cords, SCDGF, is a unique member of the PDGF/VEGF family."
      Hamada T., Ui-Tei K., Miyata Y.
      FEBS Lett. 475:97-102(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Lung.
    4. "Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
      Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
      J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    5. "An N-terminally truncated isoform of human PDGF-C regulates the secretion of full-length PDGF-C and is deregulated in renal cell carcinoma."
      Zhao J., Liu Z., Liu T., Nilsson S., Nister M.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Fetal brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Prostate.
    8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    11. "Chromosomal location, exon structure, and vascular expression patterns of the human PDGFC and PDGFC genes."
      Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N., Eriksson U., Alitalo K.
      Circulation 103:2242-2247(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors."
      Zwerner J.P., May W.A.
      Oncogene 20:626-633(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "Platelet-derived growth factor-B and -C and active alpha-receptors in medulloblastoma cells."
      Andrae J., Molander C., Smits A., Funa K., Nister M.
      Biochem. Biophys. Res. Commun. 296:604-611(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Characterization of platelet-derived growth factor-C (PDGF-C): expression in normal and tumor cells, biological activity and chromosomal localization."
      Dijkmans J., Xu J., Masure S., Dhanaraj S., Gosiewska A., Geesin J., Sprengel J., Harris S., Verhasselt P., Gordon R., Yon J.
      Int. J. Biochem. Cell Biol. 34:414-426(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), GLYCOSYLATION, MUTAGENESIS OF CYS-124.
    15. "Dominant negative PDGF-C inhibits growth of Ewing family tumor cell lines."
      Zwerner J.P., May W.A.
      Oncogene 21:3847-3854(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "PDGF-C expression in the developing and normal adult human kidney and in glomerular diseases."
      Eitner F., Ostendorf T., Kretzler M., Cohen C.D., Eriksson U., Grone H.J., Floege J.
      J. Am. Soc. Nephrol. 14:1145-1153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, INDUCTION.
    17. "Platelet-derived growth factor (PDGF)-C, a PDGF family member with a vascular endothelial growth factor-like structure."
      Reigstad L.J., Sande H.M., Fluge O., Bruland O., Muga A., Varhaug J.E., Martinez A., Lillehaug J.R.
      J. Biol. Chem. 278:17114-17120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF SECRETED ACTIVE FORM, SUBUNIT, DISULFIDE BONDS, 3D-STRUCTURE MODELING.
    18. "PDGF C is a selective alpha platelet-derived growth factor receptor agonist that is highly expressed in platelet alpha granules and vascular smooth muscle."
      Fang L., Yan Y., Komuves L.G., Yonkovich S., Sullivan C.M., Stringer B., Galbraith S., Lokker N.A., Hwang S.S., Nurden P., Phillips D.R., Giese N.A.
      Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    19. "Tissue plasminogen activator is a potent activator of PDGF-CC."
      Fredriksson L., Li H., Fieber C., Li X., Eriksson U.
      EMBO J. 23:3793-3802(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLAT.
    20. "Fibroblast growth factor-2 induction of platelet-derived growth factor-C chain transcription in vascular smooth muscle cells is ERK-dependent but not JNK-dependent and mediated by Egr-1."
      Midgley V.C., Khachigian L.M.
      J. Biol. Chem. 279:40289-40295(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY EGR1.
    21. "Structural and functional specificities of PDGF-C and PDGF-D, the novel members of the platelet-derived growth factors family."
      Reigstad L.J., Varhaug J.E., Lillehaug J.R.
      FEBS J. 272:5723-5741(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    22. "Structural requirements for activation of latent platelet-derived growth factor CC by tissue plasminogen activator."
      Fredriksson L., Ehnman M., Fieber C., Eriksson U.
      J. Biol. Chem. 280:26856-26862(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLAT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-231; LYS-232 AND ARG-234.
    23. "Regulation of fibrogenic/fibrolytic genes by platelet-derived growth factor C, a novel growth factor, in human dermal fibroblasts."
      Jinnin M., Ihn H., Mimura Y., Asano Y., Yamane K., Tamaki K.
      J. Cell. Physiol. 202:510-517(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: FUNCTION.
    25. "Fibroblast growth factor 2 and transforming growth factor beta1 synergism in human bronchial smooth muscle cell proliferation."
      Bosse Y., Thompson C., Stankova J., Rola-Pleszczynski M.
      Am. J. Respir. Cell Mol. Biol. 34:746-753(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    26. "Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human thyroid tissue and cell lines."
      Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.
      Exp. Cell Res. 312:782-795(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUMOYLATION.
    27. "PDGF-C and -D induced proliferation/migration of human RPE is abolished by inflammatory cytokines."
      Li R., Maminishkis A., Wang F.E., Miller S.S.
      Invest. Ophthalmol. Vis. Sci. 48:5722-5732(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    28. "Increased expression of platelet-derived growth factor C messenger ribonucleic acid in uterine leiomyomata."
      Hwu Y.M., Li S.H., Lee R.K., Tsai Y.H., Yeh T.S., Lin S.Y.
      Fertil. Steril. 89:468-471(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    29. "Plasmin is the major protease responsible for processing PDGF-C in the vitreous of patients with proliferative vitreoretinopathy."
      Lei H., Velez G., Hovland P., Hirose T., Kazlauskas A.
      Invest. Ophthalmol. Vis. Sci. 49:42-48(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY PLG.

    Entry informationi

    Entry nameiPDGFC_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRA1
    Secondary accession number(s): B4DU34
    , B9EGR8, Q4W5M9, Q9UL22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    A lower molecular weight form (around 43 kDa) is present in patients with papillary thyroid carcinoma.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3