MKA_XENLA
ID MKA_XENLA Reviewed; 142 AA.
AC P48530; Q32N64; Q91547; Q91676;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Midkine-A {ECO:0000305};
DE Short=MK-A;
DE Short=XMK;
DE AltName: Full=Pleiotrophic factor-alpha-1 {ECO:0000303|PubMed:7677748};
DE Short=PTF-alpha-1;
DE Short=X-PTF-alpha1;
DE Flags: Precursor;
GN Name=mdk-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].
RC TISSUE=Embryonic head;
RX PubMed=8076838; DOI=10.1016/0378-1119(94)90312-3;
RA Fu C., Maminta-Smith L.D., Guo C., Deuel T.F.;
RT "Cloning and sequence of the Xenopus laevis homologue of the midkine
RT cDNA.";
RL Gene 146:311-312(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8537332; DOI=10.1093/oxfordjournals.jbchem.a124898;
RA Sekiguchi K., Yokota C., Asashima M., Kaname T., Fan Q.W., Muramatsu T.,
RA Kadomatsu K.;
RT "Restricted expression of Xenopus midkine gene during early development.";
RL J. Biochem. 118:94-100(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Tail bud;
RX PubMed=9361288; DOI=10.1006/mcne.1997.0638;
RA Zhou H., Muramatsu T., Halfter W., Tsim K.W., Peng H.B.;
RT "A role of midkine in the development of the neuromuscular junction.";
RL Mol. Cell. Neurosci. 10:56-70(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=9538212; DOI=10.1093/oxfordjournals.jbchem.a021942;
RA Yokota C., Takahashi S., Eisaki A., Asashima M., Akhter S., Muramatsu T.,
RA Kadomatsu K.;
RT "Midkine counteracts the activin signal in mesoderm induction and promotes
RT neural formation.";
RL J. Biochem. 123:339-346(1998).
RN [7]
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 protein that functions as cytokine and growth factor
CC and mediates its signal through cell-surface proteoglycan and non-
CC proteoglycan receptors. Binds cell-surface proteoglycan receptors via
CC their chondroitin sulfate (CS) groups. Thereby regulates many processes
CC like inflammatory response, cell proliferation, cell adhesion, cell
CC growth, cell survival, tissue regeneration, cell differentiation and
CC cell migration (By similarity). Inhibits mesoderm formation and
CC promotes neural formation during development (PubMed:9538212). Plays a
CC role in development of the neuromuscular junction (NMJ)
CC (PubMed:9361288). Has antibacterial activity against both Gram-positive
CC and Gram-negative bacteria (PubMed:20308059).
CC {ECO:0000250|UniProtKB:P21741, ECO:0000269|PubMed:20308059,
CC ECO:0000269|PubMed:9361288, ECO:0000269|PubMed:9538212}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression at the mid-gastrula stage begins in the
CC neural anlage, and becomes increasingly prominent in the central
CC nervous system and head mesenchyme during neurula stages. Although the
CC mRNA is localized to the developing central nervous system (CNS), the
CC protein is deposited at the neuromuscular junction (NMJ). In the
CC tailbud stage embryo, expressed in the head and tail regions as well as
CC in the CNS. In adults, expression is highest in the brain, eye and
CC bone, with lower expression in the heart and lung. Not expressed in the
CC ovary. {ECO:0000269|PubMed:7677748, ECO:0000269|PubMed:8537332,
CC ECO:0000269|PubMed:9361288}.
CC -!- DEVELOPMENTAL STAGE: Expressed zygotically from the mid-gastrula stage.
CC {ECO:0000269|PubMed:9361288}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; U06048; AAA57319.1; -; mRNA.
DR EMBL; D42058; BAA07658.1; -; mRNA.
DR EMBL; S80453; AAB35853.2; -; mRNA.
DR EMBL; BC108811; AAI08812.1; -; mRNA.
DR PIR; I51651; I51651.
DR PIR; JC4168; JC4168.
DR PIR; JC4272; JC4272.
DR RefSeq; NP_001081356.1; NM_001087887.1.
DR RefSeq; XP_018114941.1; XM_018259452.1.
DR RefSeq; XP_018114942.1; XM_018259453.1.
DR AlphaFoldDB; P48530; -.
DR SMR; P48530; -.
DR DNASU; 397791; -.
DR GeneID; 397791; -.
DR KEGG; xla:397791; -.
DR CTD; 397791; -.
DR Xenbase; XB-GENE-488506; mdk.S.
DR OMA; CASKMKS; -.
DR OrthoDB; 1489280at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 397791; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA: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:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..142
FT /note="Midkine-A"
FT /id="PRO_0000024666"
FT DISULFID 36..60
FT /evidence="ECO:0000250"
FT DISULFID 44..69
FT /evidence="ECO:0000250"
FT DISULFID 51..73
FT /evidence="ECO:0000250"
FT DISULFID 83..115
FT /evidence="ECO:0000250"
FT DISULFID 93..125
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="V -> I (in Ref. 3; AAB35853)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="P -> L (in Ref. 1; AAA57319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15567 MW; B6036490298929B8 CRC64;
MELRAFCVIL LITVLAVSSQ AAKNKKEKGK KGASDCTEWT WGSCIPNSKD CGAGTREGTC
KEETRKLKCK IPCNWKKAFG ADCKYKFENW GECNATTGQK VRSGTLKKAL YNADCQQTVE
ATKPCSLKTK SKSKGKKGKG KE
