ID   PTNA_XENLA              Reviewed;         161 AA.
AC   P48532; Q6GLN4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pleiotrophin-A {ECO:0000305};
DE            Short=PTN-A;
DE   AltName: Full=Pleiotrophic factor-beta-1;
DE            Short=PTF-beta-1;
DE            Short=X-PTF-beta1;
DE   Flags: Precursor;
GN   Name=ptn-a;
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], AND TISSUE SPECIFICITY.
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].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P21246, ECO:0000250|UniProtKB:P48533}.
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; D42059; BAA07659.1; -; mRNA.
DR   EMBL; BC074426; AAH74426.1; -; mRNA.
DR   PIR; JC4274; JC4274.
DR   RefSeq; NP_001086286.1; NM_001092817.1.
DR   AlphaFoldDB; P48532; -.
DR   SMR; P48532; -.
DR   DNASU; 444715; -.
DR   GeneID; 444715; -.
DR   KEGG; xla:444715; -.
DR   CTD; 444715; -.
DR   Xenbase; XB-GENE-865472; ptn.L.
DR   OrthoDB; 1489280at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 444715; Expressed in internal ear and 8 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; ISS: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-A"
FT                   /id="PRO_0000024668"
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"
SQ   SEQUENCE   161 AA;  18154 MW;  57AA0A6C64949D0A CRC64;
     MRHQHGLFML ALLAFLFVIT VLGTDSGKKE KQEKKVKKSD CGEWQWSVCV PTSGDCGLGT
     REGTRSGKEC KQTIKTQKCK IPCNWKKQFG AECKYQFQEW GDCDPDTGLK TRSGSLKRAL
     HNAECQKTVT LSKPCGKVTK PKLQESKKKK KEGKNKEKLL D