PTN_MOUSE
ID PTN_MOUSE Reviewed; 168 AA.
AC P63089; P20935;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pleiotrophin {ECO:0000250|UniProtKB:P21246};
DE Short=PTN {ECO:0000250|UniProtKB:P21246};
DE AltName: Full=Heparin-binding brain mitogen {ECO:0000250|UniProtKB:P21246};
DE Short=HBBM {ECO:0000250|UniProtKB:P21246};
DE AltName: Full=Heparin-binding growth factor 8 {ECO:0000250|UniProtKB:P21782};
DE Short=HBGF-8 {ECO:0000250|UniProtKB:P21782};
DE AltName: Full=Heparin-binding growth-associated molecule {ECO:0000250|UniProtKB:P63090};
DE Short=HB-GAM {ECO:0000250|UniProtKB:P63090};
DE AltName: Full=Heparin-binding neutrophic factor {ECO:0000250|UniProtKB:P21246};
DE Short=HBNF {ECO:0000250|UniProtKB:P21246};
DE AltName: Full=Osteoblast-specific factor 1 {ECO:0000303|PubMed:1701634};
DE Short=OSF-1 {ECO:0000303|PubMed:1701634};
DE Flags: Precursor;
GN Name=Ptn {ECO:0000312|MGI:MGI:97804};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1701634; DOI=10.1016/s0006-291x(05)81048-4;
RA Tezuka K.I., Takeshita S., Hakeda Y., Kumegawa M., Kikuno R.,
RA Hashimoto-Gotoh T.;
RT "Isolation of mouse and human cDNA clones encoding a protein expressed
RT specifically in osteoblasts and brain tissues.";
RL Biochem. Biophys. Res. Commun. 173:246-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=1457042; DOI=10.1089/dna.1992.11.735;
RA Katoh K., Takeshita S., Sato M., Ito T., Amann E.;
RT "Genomic organization of the mouse OSF-1 gene.";
RL DNA Cell Biol. 11:735-743(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5; 34-44; 92-102; 146-156 AND
RP 165-168, AND GENOMIC ORGANIZATION.
RX PubMed=1550576; DOI=10.1016/0006-291x(92)90539-w;
RA Naito A., Yoshikura H., Iwamoto A.;
RT "Similarity of the genomic structure between the two members in a new
RT family of heparin-binding factors.";
RL Biochem. Biophys. Res. Commun. 183:701-707(1992).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=1768439; DOI=10.3109/08977199109000275;
RA Kretschmer P.J., Fairhurst J.L., Decker M.M., Chan C.P., Gluzman Y.,
RA Boehlen P., Kovesdi I.;
RT "Cloning, characterization and developmental regulation of two members of a
RT novel human gene family of neurite outgrowth-promoting proteins.";
RL Growth Factors 5:99-114(1991).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11414790; DOI=10.1006/mcne.2001.0998;
RA Amet L.E., Lauri S.E., Hienola A., Croll S.D., Lu Y., Levorse J.M.,
RA Prabhakaran B., Taira T., Rauvala H., Vogt T.F.;
RT "Enhanced hippocampal long-term potentiation in mice lacking heparin-
RT binding growth-associated molecule.";
RL Mol. Cell. Neurosci. 17:1014-1024(2001).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12093164; DOI=10.1006/mcne.2002.1104;
RA Pavlov I., Voikar V., Kaksonen M., Lauri S.E., Hienola A., Taira T.,
RA Rauvala H.;
RT "Role of heparin-binding growth-associated molecule (HB-GAM) in hippocampal
RT LTP and spatial learning revealed by studies on overexpressing and knockout
RT mice.";
RL Mol. Cell. Neurosci. 20:330-342(2002).
RN [9]
RP FUNCTION.
RX PubMed=15121180; DOI=10.1016/j.mcn.2004.01.018;
RA Hienola A., Pekkanen M., Raulo E., Vanttola P., Rauvala H.;
RT "HB-GAM inhibits proliferation and enhances differentiation of neural stem
RT cells.";
RL Mol. Cell. Neurosci. 26:75-88(2004).
RN [10]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RX PubMed=17121547; DOI=10.1111/j.1365-2443.2006.01028.x;
RA Muramatsu H., Zou P., Kurosawa N., Ichihara-Tanaka K., Maruyama K.,
RA Inoh K., Sakai T., Chen L., Sato M., Muramatsu T.;
RT "Female infertility in mice deficient in midkine and pleiotrophin, which
RT form a distinct family of growth factors.";
RL Genes Cells 11:1405-1417(2006).
RN [11]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16619002; DOI=10.1038/labinvest.3700428;
RA Zou P., Muramatsu H., Sone M., Hayashi H., Nakashima T., Muramatsu T.;
RT "Mice doubly deficient in the midkine and pleiotrophin genes exhibit
RT deficits in the expression of beta-tectorin gene and in auditory
RT response.";
RL Lab. Invest. 86:645-653(2006).
RN [12]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19442624; DOI=10.1016/j.bone.2009.01.004;
RA Imai S., Heino T.J., Hienola A., Kurata K., Bueki K., Matsusue Y.,
RA Vaeaenaenen H.K., Rauvala H.;
RT "Osteocyte-derived HB-GAM (pleiotrophin) is associated with bone formation
RT and mechanical loading.";
RL Bone 44:785-794(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION.
RX PubMed=21791434; DOI=10.1182/blood-2010-05-287235;
RA Istvanffy R., Kroeger M., Eckl C., Gitzelmann S., Vilne B., Bock F.,
RA Graf S., Schiemann M., Keller U.B., Peschel C., Oostendorp R.A.;
RT "Stromal pleiotrophin regulates repopulation behavior of hematopoietic stem
RT cells.";
RL Blood 118:2712-2722(2011).
RN [15]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25000129; DOI=10.1371/journal.pone.0100597;
RA Krellman J.W., Ruiz H.H., Marciano V.A., Mondrow B., Croll S.D.;
RT "Behavioral and neuroanatomical abnormalities in pleiotrophin knockout
RT mice.";
RL PLoS ONE 9:E100597-E100597(2014).
RN [16]
RP FUNCTION.
RX PubMed=27445335; DOI=10.1074/jbc.m116.742536;
RA Kuboyama K., Fujikawa A., Suzuki R., Tanga N., Noda M.;
RT "Role of Chondroitin Sulfate (CS) Modification in the Regulation of
RT Protein-tyrosine Phosphatase Receptor Type Z (PTPRZ) Activity:
RT PLEIOTROPHIN-PTPRZ-A SIGNALING IS INVOLVED IN OLIGODENDROCYTE
RT DIFFERENTIATION.";
RL J. Biol. Chem. 291:18117-18128(2016).
RN [17]
RP DEVELOPMENTAL STAGE, INDUCTION, AND FUNCTION.
RX PubMed=28657144; DOI=10.1002/jcp.26067;
RA Yu H.F., Tao R., Yang Z.Q., Wang K., Yue Z.P., Guo B.;
RT "Ptn functions downstream of C/EBPbeta to mediate the effects of cAMP on
RT uterine stromal cell differentiation through targeting Hand2 in response to
RT progesterone.";
RL J. Cell. Physiol. 233:1612-1626(2018).
RN [18]
RP FUNCTION.
RX PubMed=30497772; DOI=10.1016/j.neuron.2018.10.051;
RA Tang C., Wang M., Wang P., Wang L., Wu Q., Guo W.;
RT "Neural Stem Cells Behave as a Functional Niche for the Maturation of
RT Newborn Neurons through the Secretion of PTN.";
RL Neuron 101:32-44(2019).
CC -!- FUNCTION: Secreted growth factor that mediates its signal through cell-
CC surface proteoglycan and non-proteoglycan receptors (By similarity).
CC Binds cell-surface proteoglycan receptor via their chondroitin sulfate
CC (CS) groups (By similarity). Thereby regulates many processes like cell
CC proliferation, cell survival, cell growth, cell differentiation and
CC cell migration in several tissues namely neuron and bone
CC (PubMed:15121180, PubMed:30497772, PubMed:27445335, PubMed:19442624).
CC Also plays a role in synaptic plasticity and learning-related behavior
CC by inhibiting long-term synaptic potentiation (PubMed:11414790,
CC PubMed:25000129). Binds PTPRZ1, leading to neutralization of the
CC negative charges of the CS chains of PTPRZ1, inducing PTPRZ1
CC clustering, thereby causing the dimerization and inactivation of its
CC phosphatase activity leading to increased tyrosine phosphorylation of
CC each of the PTPRZ1 substrates like ALK or AFAP1L2 in order to activate
CC the PI3K-AKT pathway (PubMed:27445335). Through PTPRZ1 binding controls
CC oligodendrocyte precursor cell differentiation by enhancing the
CC phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway
CC (PubMed:27445335). Forms a complex with PTPRZ1 and integrin alpha-
CC V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration
CC through SRC dephosphorylation and activation that consequently leads to
CC ITGB3 'Tyr-773' phosphorylation (By similarity). In adult hippocampus
CC promotes dendritic arborization, spine development, and functional
CC integration and connectivity of newborn granule neurons through ALK by
CC activating AKT signaling pathway (PubMed:30497772). Binds GPC2 and
CC chondroitin sulfate proteoglycans (CSPGs) at the neuron surface,
CC leading to abrogation of binding between PTPRS and CSPGs and neurite
CC outgrowth promotion (By similarity). Binds SDC3 and mediates bone
CC formation by recruiting and attaching osteoblasts/osteoblast precursors
CC to the sites for new bone deposition (By similarity). Binds ALK and
CC promotes cell survival and cell proliferation through MAPK pathway
CC activation (By similarity). Inhibits proliferation and enhances
CC differentiation of neural stem cells by inhibiting FGF2-induced
CC fibroblast growth factor receptor signaling pathway (PubMed:15121180).
CC Mediates regulatory mechanisms in normal hemostasis and in
CC hematopoietic regeneration and in maintaining the balance of myeloid
CC and lymphoid regeneration (PubMed:21791434). In addition may play a
CC role in the female reproductive system, auditory response and the
CC progesterone-induced decidualization pathway (PubMed:17121547,
CC PubMed:28657144, PubMed:16619002). {ECO:0000250|UniProtKB:P21246,
CC ECO:0000250|UniProtKB:P63090, ECO:0000269|PubMed:11414790,
CC ECO:0000269|PubMed:15121180, ECO:0000269|PubMed:16619002,
CC ECO:0000269|PubMed:17121547, ECO:0000269|PubMed:19442624,
CC ECO:0000269|PubMed:21791434, ECO:0000269|PubMed:25000129,
CC ECO:0000269|PubMed:27445335, ECO:0000269|PubMed:28657144,
CC ECO:0000269|PubMed:30497772}.
CC -!- SUBUNIT: Interacts with ALK and NEK6. Interacts with PTPRZ1 (via
CC chondroitin sulfate groups); promotes formation of homooligomers;
CC oligomerization impairs tyrosine phosphatase activity. Forms a complex
CC with PTPRZ1 and CTNNB1; this complex inactivates PTPRZ1 protein
CC tyrosine phosphatase activity through PTN interaction and stimulates
CC tyrosine phosphorylation of CTNNB1. Interacts with ITGB3 AND ITGA5.
CC Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3)
CC that stimulates endothelial cell migration through ITGB3 'Tyr-773'
CC phosphorylation (By similarity). Interacts with SDC3 (via heparan
CC sulfate chains); this interaction mediates the neurite outgrowth-
CC promoting signal from PTN to the cytoskeleton of growing neurites; this
CC interaction mediates osteoblast recruitment. Interacts with GPC2 (via
CC heparan sulfate); this interaction promotes neurite outgrowth through
CC binding of PTN with chondroitin sulfate of proteoglycans, thereby
CC releasing PTPRS of chondroitin sulfate proteoglycans (CSPGs) and
CC leading to binding with heparan sulfate of GPC2 (By similarity).
CC {ECO:0000250|UniProtKB:P21246, ECO:0000250|UniProtKB:P63090}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}.
CC -!- TISSUE SPECIFICITY: Osteoblast and brain (PubMed:1701634,
CC PubMed:1768439). Expressed in the follicular epithelium and granulosa
CC cells of the ovary. Strongly expressed in the uterus of newborn mice,
CC and the degree of expression decreased in one-week-old mice, although
CC the expression continues even in the uteri of adult mice. Expression
CC gradually increases from proestrus to estrus, then decreases sharply,
CC and thereafter gradually increased again (PubMed:17121547). strongly
CC expressed in the cochlea of WT mice 1 week after birth, and then the
CC expression decreased and was undetectable by week 8 after birth
CC (PubMed:16619002). Expressed around the cell soma of osteocytes and
CC apparently captured in the unmineralized interstitial matrix
CC surrounding the cells. Furthermore distributed throughout the
CC intraosseous canalicular porosity, being localized in the unmineralized
CC matrix around the cell processes. Strongly expressed in the innermost
CC layer of the periosteum (PubMed:19442624).
CC {ECO:0000269|PubMed:16619002, ECO:0000269|PubMed:1701634,
CC ECO:0000269|PubMed:17121547, ECO:0000269|PubMed:1768439,
CC ECO:0000269|PubMed:19442624}.
CC -!- DEVELOPMENTAL STAGE: NoT detected in the uteri from days 1-3 of
CC pregnancy. On day 4 of pregnancy, localizes in the luminal and
CC glandular epithelium as well as in the uterine stromal cells. On day 5,
CC a high level is observed in the subluminal stroma surrounding the
CC implanting blastocyst, while there is no expression at the inter-
CC implantation sites. From day 6-8 of pregnancy, strongly expressed in
CC the decidua. Expression is gradually increased as the progression of
CC pregnancy and reached a maximum on day 8. Elevated expression is
CC observed at implantation sites from days 5-8 of pregnancy.
CC {ECO:0000269|PubMed:28657144}.
CC -!- INDUCTION: Enhanced up to 3 days after the administration of chorionic
CC gonadotropin to induce ovulation (PubMed:17121547). Up-regulated by
CC progesterone in the uterine stromal cells through cAMP
CC (PubMed:28657144). {ECO:0000269|PubMed:17121547,
CC ECO:0000269|PubMed:28657144}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P21246}.
CC -!- DISRUPTION PHENOTYPE: Homozygous PTN knockout mice are viable and
CC fertile and show no gross anatomical abnormalities. The hippocampal
CC structure as well as basal excitatory synaptic transmission in the area
CC CA1 appear normal. The skeletal structure of homozygous PTN knockout
CC mice develops normally. However, a growth retardation of the weight-
CC bearing bones is observed by 2 months of age. Adult homozygous PTN
CC knockout mice are characterized by low bone formation and osteopenia,
CC as well as resistance to immobilization-dependent bone remodeling
CC (PubMed:11414790, PubMed:12093164). Mice show faster learning in water
CC maze and decreased anxiety in elevated plus-maze test
CC (PubMed:12093164). Homozygous PTN knockout mice exhibit cognitive
CC rigidity, heightened anxiety, behavioral reticence in novel contexts
CC and novel social interactions. Initial learning of spatial and other
CC associative tasks, as well as vascular density in the lateral
CC entorhinal cortex, are normal (PubMed:25000129). PTN and MDK double
CC knockout mice are born in only one third the number expected by
CC Mendelian segregation and 4 weeks after birth weigh about half as much
CC as wild-type mice. Most of the female are infertile. Both male and
CC female one-month-old mice show a defect in spontaneous locomotive
CC activity of 50-60% of that of wild-type mice. Although the difference
CC in activity decrease with age, the activity of 3-month-old male double
CC knockout mice is still about 80% of that of the wild-type mice. The
CC diestrus and proestrus periods are long and the estrus period is short.
CC Furthermore, vaginal abnormality is found in about half of the double
CC deficient mice (PubMed:17121547). PTN and MDK double knockout mice have
CC a deficit of auditory response (PubMed:16619002).
CC {ECO:0000269|PubMed:11414790, ECO:0000269|PubMed:12093164,
CC ECO:0000269|PubMed:16619002, ECO:0000269|PubMed:17121547,
CC ECO:0000269|PubMed:25000129}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; D90225; BAA14260.1; -; mRNA.
DR EMBL; S52357; AAB24477.1; -; Genomic_DNA.
DR EMBL; S52338; AAB24477.1; JOINED; Genomic_DNA.
DR EMBL; S52345; AAB24477.1; JOINED; Genomic_DNA.
DR EMBL; S52353; AAB24477.1; JOINED; Genomic_DNA.
DR EMBL; AK011346; BAB27557.1; -; mRNA.
DR EMBL; BC002064; AAH02064.1; -; mRNA.
DR EMBL; BC061695; AAH61695.1; -; mRNA.
DR EMBL; S88460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S88462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S88464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S88466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S88468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20005.1; -.
DR PIR; A37087; A37087.
DR RefSeq; NP_032999.1; NM_008973.2.
DR RefSeq; XP_006505820.2; XM_006505757.3.
DR AlphaFoldDB; P63089; -.
DR SMR; P63089; -.
DR BioGRID; 202472; 8.
DR IntAct; P63089; 1.
DR STRING; 10090.ENSMUSP00000099073; -.
DR PhosphoSitePlus; P63089; -.
DR PaxDb; P63089; -.
DR PRIDE; P63089; -.
DR ProteomicsDB; 301960; -.
DR Antibodypedia; 4323; 542 antibodies from 40 providers.
DR DNASU; 19242; -.
DR Ensembl; ENSMUST00000101534; ENSMUSP00000099073; ENSMUSG00000029838.
DR GeneID; 19242; -.
DR KEGG; mmu:19242; -.
DR UCSC; uc009bja.1; mouse.
DR CTD; 5764; -.
DR MGI; MGI:97804; Ptn.
DR VEuPathDB; HostDB:ENSMUSG00000029838; -.
DR eggNOG; ENOG502RXV7; Eukaryota.
DR GeneTree; ENSGT00390000007640; -.
DR HOGENOM; CLU_136864_1_0_1; -.
DR InParanoid; P63089; -.
DR OMA; PKWRERR; -.
DR OrthoDB; 1489280at2759; -.
DR PhylomeDB; P63089; -.
DR TreeFam; TF332376; -.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR BioGRID-ORCS; 19242; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ptn; mouse.
DR PRO; PR:P63089; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P63089; protein.
DR Bgee; ENSMUSG00000029838; Expressed in embryonic brain and 257 other tissues.
DR ExpressionAtlas; P63089; baseline and differential.
DR Genevisible; P63089; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; TAS:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:1904399; F:heparan sulfate binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0045545; F:syndecan binding; ISO:MGI.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IDA:MGI.
DR GO; GO:0046697; P:decidualization; IMP:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; IMP:UniProtKB.
DR GO; GO:0031104; P:dendrite regeneration; ISS:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0045837; P:negative regulation of membrane potential; ISO:MGI.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; ISO:MGI.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:1904397; P:negative regulation of neuromuscular junction development; ISO:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0001503; P:ossification; IDA:MGI.
DR GO; GO:0043932; P:ossification involved in bone remodeling; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0048680; P:positive regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IMP:UniProtKB.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:UniProtKB.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISO:MGI.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1903706; P:regulation of hemopoiesis; IMP:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0010996; P:response to auditory stimulus; IMP:UniProtKB.
DR GO; GO:0060221; P:retinal rod cell differentiation; ISO:MGI.
DR GO; GO:0042246; P:tissue regeneration; IMP:UniProtKB.
DR Gene3D; 2.20.60.10; -; 1.
DR Gene3D; 2.30.90.10; -; 1.
DR InterPro; IPR000762; Midkine_heparin-bd_GF.
DR InterPro; IPR020090; PTN/MK_C_dom.
DR InterPro; IPR038130; PTN/MK_C_dom_sf.
DR InterPro; IPR020091; PTN/MK_diS_sf.
DR InterPro; IPR020089; PTN/MK_N_dom.
DR InterPro; IPR037122; PTN/MK_N_dom_sf.
DR InterPro; IPR020092; PTN_MK_heparin-bd_GF_CS.
DR PANTHER; PTHR13850; PTHR13850; 1.
DR Pfam; PF01091; PTN_MK_C; 1.
DR Pfam; PF05196; PTN_MK_N; 1.
DR PRINTS; PR00269; PTNMIDKINE.
DR SMART; SM00193; PTN; 1.
DR SUPFAM; SSF57288; SSF57288; 2.
DR PROSITE; PS00619; PTN_MK_1; 1.
DR PROSITE; PS00620; PTN_MK_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Growth factor; Heparin-binding; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT CHAIN 33..168
FT /note="Pleiotrophin"
FT /id="PRO_0000024660"
FT REGION 92..99
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 123..131
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 139..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..168
FT /note="Chondroitin sulfate A binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT COMPBIAS 148..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..76
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 55..85
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 62..89
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 99..131
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 109..141
FT /evidence="ECO:0000250|UniProtKB:P21246"
SQ SEQUENCE 168 AA; 18869 MW; 2127DA167D2DD33D CRC64;
MSSQQYQQQR RKFAAAFLAL IFILAAVDTA EAGKKEKPEK KVKKSDCGEW QWSVCVPTSG
DCGLGTREGT RTGAECKQTM KTQRCKIPCN WKKQFGAECK YQFQAWGECD LNTALKTRTG
SLKRALHNAD CQKTVTISKP CGKLTKPKPQ AESKKKKKEG KKQEKMLD
