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Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neutrophic factor) (HBNF) (Osteoblast-specific factor 1) (OSF-1)

 PTN_RAT                 Reviewed;         168 AA.
P63090; P20935;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
22-NOV-2017, entry version 103.
RecName: Full=Pleiotrophin;
Short=PTN;
AltName: Full=Heparin-binding brain mitogen;
Short=HBBM;
AltName: Full=Heparin-binding growth factor 8;
Short=HBGF-8;
AltName: Full=Heparin-binding growth-associated molecule;
Short=HB-GAM;
AltName: Full=Heparin-binding neutrophic factor;
Short=HBNF;
AltName: Full=Osteoblast-specific factor 1;
Short=OSF-1;
Flags: Precursor;
Name=Ptn;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Wistar; TISSUE=Brain;
PubMed=2170351;
Merenmies J., Rauvala H.;
"Molecular cloning of the 18-kDa growth-associated protein of
developing brain.";
J. Biol. Chem. 265:16721-16724(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2270483; DOI=10.1126/science.2270483;
Li Y.-S., Milner P.G., Chauhan A.K., Watson M.A., Hoffman R.M.,
Kodner C.M., Milbrandt J., Deuel T.F.;
"Cloning and expression of a developmentally regulated protein that
induces mitogenic and neurite outgrowth activity.";
Science 250:1690-1694(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 33-54.
TISSUE=Brain;
PubMed=2388713; DOI=10.1007/BF00969930;
Huber D., Gautschi-Sova P., Bohlen P.;
"Amino-terminal sequences of a novel heparin-binding protein from
human, bovine, rat, and chick brain: high interspecies homology.";
Neurochem. Res. 15:435-439(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-134.
STRAIN=Sprague-Dawley;
PubMed=1700712; DOI=10.1016/0006-291X(90)90753-A;
Kovesdi I., Fairhurst J.L., Kretschmer P.J., Boehlen P.;
"Heparin-binding neurotrophic factor (HBNF) and MK, members of a new
family of homologous, developmentally regulated proteins.";
Biochem. Biophys. Res. Commun. 172:850-854(1990).
[6]
DEVELOPMENTAL STAGE.
PubMed=1768439; DOI=10.3109/08977199109000275;
Kretschmer P.J., Fairhurst J.L., Decker M.M., Chan C.P., Gluzman Y.,
Boehlen P., Kovesdi I.;
"Cloning, characterization and developmental regulation of two members
of a novel human gene family of neurite outgrowth-promoting
proteins.";
Growth Factors 5:99-114(1991).
[7]
FUNCTION, AND INTERACTION WITH PTPRZ1.
PubMed=16814777; DOI=10.1016/j.febslet.2006.06.041;
Fukada M., Fujikawa A., Chow J.P., Ikematsu S., Sakuma S., Noda M.;
"Protein tyrosine phosphatase receptor type Z is inactivated by
ligand-induced oligomerization.";
FEBS Lett. 580:4051-4056(2006).
-!- FUNCTION: Secreted growth factor that induces neurite outgrowth
and which is mitogenic for fibroblasts, epithelial, and
endothelial cells. Binds anaplastic lymphoma kinase (ALK) which
induces MAPK pathway activation, an important step in the anti-
apoptotic signaling of PTN and regulation of cell proliferation.
Binds to cell-surface target proteins via their chondroitin
sulfate groups (By similarity). Down-regulates PTPRZ1 activity
(PubMed:16814777). {ECO:0000250|UniProtKB:P21246,
ECO:0000269|PubMed:16814777}.
-!- SUBUNIT: Interacts with ALK and NEK6 (By similarity). Interacts
with PTPRZ1 (probably via chondroitin sulfate groups)
(PubMed:16814777). {ECO:0000250|UniProtKB:P21246,
ECO:0000269|PubMed:16814777}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}.
-!- TISSUE SPECIFICITY: Expressed in brain.
-!- DEVELOPMENTAL STAGE: Expressed at low levels in the brain in early
embryonic stages. Levels increase to a maximum before or just
after birth, and are lower in adult brain.
{ECO:0000269|PubMed:1768439}.
-!- PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P21246}.
-!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M55601; AAA41310.1; -; mRNA.
EMBL; M68916; AAA41311.1; -; mRNA.
EMBL; BC062013; AAH62013.1; -; mRNA.
PIR; B37780; B37780.
RefSeq; NP_058762.1; NM_017066.2.
UniGene; Rn.1653; -.
ProteinModelPortal; P63090; -.
BioGrid; 247030; 1.
STRING; 10116.ENSRNOP00000016088; -.
PaxDb; P63090; -.
PRIDE; P63090; -.
Ensembl; ENSRNOT00000016088; ENSRNOP00000016088; ENSRNOG00000011946.
GeneID; 24924; -.
KEGG; rno:24924; -.
UCSC; RGD:3444; rat.
CTD; 5764; -.
RGD; 3444; Ptn.
eggNOG; ENOG410IWNA; Eukaryota.
eggNOG; ENOG4111ZWP; LUCA.
GeneTree; ENSGT00390000007640; -.
HOGENOM; HOG000231473; -.
HOVERGEN; HBG008317; -.
InParanoid; P63090; -.
KO; K16642; -.
OMA; GEDICNS; -.
OrthoDB; EOG091G0VCN; -.
PhylomeDB; P63090; -.
TreeFam; TF332376; -.
PRO; PR:P63090; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000011946; -.
Genevisible; P63090; RN.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0035374; F:chondroitin sulfate binding; ISO:RGD.
GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IPI:RGD.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:RGD.
GO; GO:0008083; F:growth factor activity; IDA:RGD.
GO; GO:1904399; F:heparan sulfate binding; IPI:RGD.
GO; GO:0008201; F:heparin binding; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0043394; F:proteoglycan binding; IPI:RGD.
GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:RGD.
GO; GO:0030282; P:bone mineralization; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
GO; GO:0034644; P:cellular response to UV; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0045446; P:endothelial cell differentiation; IEP:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0030902; P:hindbrain development; IEP:RGD.
GO; GO:0007612; P:learning; IEP:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:RGD.
GO; GO:0045837; P:negative regulation of membrane potential; IDA:RGD.
GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IDA:RGD.
GO; GO:1904397; P:negative regulation of neuromuscular junction development; IDA:RGD.
GO; GO:0001503; P:ossification; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:RGD.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:RGD.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IDA:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:RGD.
GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:1904391; P:response to ciliary neurotrophic factor; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:1904373; P:response to kainic acid; IEP:RGD.
GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
GO; GO:0060221; P:retinal rod cell differentiation; IMP:RGD.
GO; GO:1904389; P:rod bipolar cell differentiation; IEP:RGD.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
GO; GO:0021794; P:thalamus development; IEP:RGD.
Gene3D; 2.20.60.10; -; 1.
InterPro; IPR000762; Midkine_heparin-bd_GF.
InterPro; IPR020090; PTN/MK_C_dom.
InterPro; IPR020091; PTN/MK_diS_sf.
InterPro; IPR020089; PTN/MK_N_dom.
InterPro; IPR037122; PTN/MK_N_dom_sf.
InterPro; IPR020092; PTN_MK_heparin-bd_GF_CS.
PANTHER; PTHR13850; PTHR13850; 1.
Pfam; PF01091; PTN_MK_C; 1.
Pfam; PF05196; PTN_MK_N; 1.
PRINTS; PR00269; PTNMIDKINE.
ProDom; PD005592; PTN_MK_hepar_bd; 1.
SMART; SM00193; PTN; 1.
SUPFAM; SSF57288; SSF57288; 2.
PROSITE; PS00619; PTN_MK_1; 1.
PROSITE; PS00620; PTN_MK_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Growth factor; Heparin-binding; Mitogen; Reference proteome; Secreted;
Signal.
SIGNAL 1 32 {ECO:0000269|PubMed:2388713}.
CHAIN 33 168 Pleiotrophin.
/FTId=PRO_0000024661.
REGION 92 99 Chondroitin sulfate binding.
{ECO:0000250|UniProtKB:P21246}.
REGION 123 131 Chondroitin sulfate binding.
{ECO:0000250|UniProtKB:P21246}.
REGION 147 168 Chondroitin sulfate A binding.
{ECO:0000250|UniProtKB:P21246}.
DISULFID 47 76 {ECO:0000250|UniProtKB:P21246}.
DISULFID 55 85 {ECO:0000250|UniProtKB:P21246}.
DISULFID 62 89 {ECO:0000250|UniProtKB:P21246}.
DISULFID 99 131 {ECO:0000250|UniProtKB:P21246}.
DISULFID 109 141 {ECO:0000250|UniProtKB:P21246}.
SEQUENCE 168 AA; 18869 MW; 2127DA167D2DD33D CRC64;
MSSQQYQQQR RKFAAAFLAL IFILAAVDTA EAGKKEKPEK KVKKSDCGEW QWSVCVPTSG
DCGLGTREGT RTGAECKQTM KTQRCKIPCN WKKQFGAECK YQFQAWGECD LNTALKTRTG
SLKRALHNAD CQKTVTISKP CGKLTKPKPQ AESKKKKKEG KKQEKMLD


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