PTNB_XENLA
ID PTNB_XENLA Reviewed; 161 AA.
AC P48533; Q6DDL1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pleiotrophin-B {ECO:0000305};
DE Short=PTN-B;
DE AltName: Full=Pleiotrophic factor-beta-2;
DE Short=PTF-beta-2;
DE Short=X-PTF-beta2;
DE Flags: Precursor;
GN Name=ptn-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS LEU-3; MET-17;
RP THR-68 AND LEU-138.
RC TISSUE=Brain;
RX PubMed=7677748; DOI=10.1006/bbrc.1995.2305;
RA Tsujimura A., Yasojima K., Kuboki Y., Suzuki A., Ueno N., Shiokawa K.,
RA Hashimoto-Gotoh T.;
RT "Developmental and differential regulations in gene expression of Xenopus
RT pleiotrophic factors-alpha and -beta.";
RL Biochem. Biophys. Res. Commun. 214:432-439(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-68.
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=20308059; DOI=10.1074/jbc.m109.081232;
RA Svensson S.L., Pasupuleti M., Walse B., Malmsten M., Morgelin M.,
RA Sjogren C., Olin A.I., Collin M., Schmidtchen A., Palmer R., Egesten A.;
RT "Midkine and pleiotrophin have bactericidal properties: preserved
RT antibacterial activity in a family of heparin-binding growth factors during
RT evolution.";
RL J. Biol. Chem. 285:16105-16115(2010).
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 (By similarity). Has antibacterial activity against both
CC Gram-positive and Gram-negative bacteria (PubMed:20308059).
CC {ECO:0000250|UniProtKB:P21246, ECO:0000269|PubMed:20308059}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}.
CC -!- TISSUE SPECIFICITY: Expressed in high levels in brain and eye. Lower
CC levels in bone. In the tailbud embryo stage, it is expressed
CC exclusively in the central nervous system, especially in the hind
CC region of the brain. {ECO:0000269|PubMed:7677748}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; D42060; BAA07660.1; -; mRNA.
DR EMBL; BC077546; AAH77546.1; -; mRNA.
DR PIR; JC4275; JC4275.
DR RefSeq; NP_001184206.1; NM_001197277.1.
DR RefSeq; NP_001184208.1; NM_001197279.1.
DR AlphaFoldDB; P48533; -.
DR SMR; P48533; -.
DR DNASU; 100505443; -.
DR GeneID; 100505441; -.
DR GeneID; 100505443; -.
DR KEGG; xla:100505441; -.
DR CTD; 100505441; -.
DR Xenbase; XB-GENE-17344052; ptn.S.
DR OrthoDB; 1489280at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 100505441; Expressed in brain and 6 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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:0009617; P:response to bacterium; 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 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Developmental protein; Disulfide bond;
KW Growth factor; Heparin-binding; Mitogen; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..161
FT /note="Pleiotrophin-B"
FT /id="PRO_0000024669"
FT REGION 86..93
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 117..125
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 136..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..161
FT /note="Chondroitin sulfate A binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT COMPBIAS 140..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 41..70
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 49..79
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 56..83
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 93..125
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 103..135
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT VARIANT 3
FT /note="H -> L (in variant 1)"
FT /evidence="ECO:0000269|PubMed:7677748"
FT VARIANT 17
FT /note="L -> M (in variants 2 and 3)"
FT /evidence="ECO:0000269|PubMed:7677748"
FT VARIANT 68
FT /note="K -> T (in variants 2, 3 and 4)"
FT /evidence="ECO:0000269|PubMed:7677748, ECO:0000269|Ref.2"
FT VARIANT 138
FT /note="V -> L (in variant 2)"
FT /evidence="ECO:0000269|PubMed:7677748"
FT CONFLICT 4
FT /note="Q -> H (in Ref. 2; AAH77546)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="A -> T (in Ref. 2; AAH77546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18173 MW; 1C0EF43227EA9D14 CRC64;
MHHQHGLFML ALLAFLLVMT VLGTDTGKKD KQEKKVKKSD CGDWQWSVCV PTSGDCGLGT
REGTRSGKEC KQTIKTQKCK IPCNWKKQFG AECKYQFQEW GDCDPETGLK TRNGNLKRAL
HNAECQKTVT LSKPCGKVTK PKLQESKKKK KEGKNKEKLL D
