MK_XENTR
ID MK_XENTR Reviewed; 142 AA.
AC Q6P8F3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Midkine {ECO:0000250|UniProtKB:P21741, ECO:0000250|UniProtKB:P48530, ECO:0000312|EMBL:AAH61275.1};
DE Short=MK {ECO:0000250|UniProtKB:P21741, ECO:0000250|UniProtKB:P48530};
DE Flags: Precursor;
GN Name=mdk {ECO:0000312|Xenbase:XB-GENE-488502};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH61275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH61275.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in
CC development of the neuromuscular junction (NMJ). Has antibacterial
CC activity against both Gram-positive and Gram-negative bacteria (By
CC similarity). {ECO:0000250|UniProtKB:P21741,
CC ECO:0000250|UniProtKB:P48530}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21741}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000255}.
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DR EMBL; BC061275; AAH61275.1; -; mRNA.
DR RefSeq; NP_989074.1; NM_203743.1.
DR AlphaFoldDB; Q6P8F3; -.
DR SMR; Q6P8F3; -.
DR STRING; 8364.ENSXETP00000010258; -.
DR PaxDb; Q6P8F3; -.
DR DNASU; 394671; -.
DR GeneID; 394671; -.
DR KEGG; xtr:394671; -.
DR CTD; 4192; -.
DR Xenbase; XB-GENE-488502; mdk.
DR eggNOG; ENOG502S022; Eukaryota.
DR HOGENOM; CLU_136864_0_0_1; -.
DR InParanoid; Q6P8F3; -.
DR OMA; CASKMKS; -.
DR OrthoDB; 1489280at2759; -.
DR PhylomeDB; Q6P8F3; -.
DR TreeFam; TF332376; -.
DR Reactome; R-XTR-201556; Signaling by ALK.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000001967; Expressed in neurula embryo and 12 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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; Differentiation;
KW Disulfide bond; Growth factor; Heparin-binding; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..142
FT /note="Midkine"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398805"
FT DISULFID 36..60
FT /evidence="ECO:0000250|UniProtKB:P21741"
FT DISULFID 44..69
FT /evidence="ECO:0000250|UniProtKB:P21741"
FT DISULFID 51..73
FT /evidence="ECO:0000250|UniProtKB:P21741"
FT DISULFID 83..115
FT /evidence="ECO:0000250|UniProtKB:P21741"
FT DISULFID 93..125
FT /evidence="ECO:0000250|UniProtKB:P21741"
SQ SEQUENCE 142 AA; 15684 MW; 4D036A91833899A2 CRC64;
MELRAFCVIL LITFLAVSSQ AAKNKKEKGK KGASDCTEWT WGRCIPNSKD CGAGTREGTC
KEETRKLKCK IPCNWKKAFG ADCKYKFENW GECNATTGQK VRSGTLKKAL YNADCQQTVE
ATKPCSLKTK SKSKGKKGKG KE