MK_CHICK
ID MK_CHICK Reviewed; 142 AA.
AC P24052;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Midkine;
DE AltName: Full=Retinoic acid-induced heparin-binding protein;
DE Short=RI-HB;
DE Flags: Precursor;
GN Name=RIHB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 80-85; 112-118 AND
RP 121-133.
RC TISSUE=Embryo;
RX PubMed=2018506; DOI=10.1016/0006-291x(91)91610-o;
RA Urios P., Duprez D., le Caer J.-P., Courtois Y., Vigny M., Laurent M.;
RT "Molecular cloning of RI-HB, a heparin binding protein regulated by
RT retinoic acid.";
RL Biochem. Biophys. Res. Commun. 175:617-624(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7925417; DOI=10.1111/j.1432-1033.1994.00931.x;
RA Duprez D., Treagger J., Pecqueur C., Vigny M.R.;
RT "Organisation and promoter activity of the retinoic-acid-induced-heparin-
RT binding (RIHB) gene.";
RL Eur. J. Biochem. 224:931-941(1994).
RN [3]
RP PROTEIN SEQUENCE OF 22-77.
RX PubMed=1993066; DOI=10.1016/0006-291x(91)91475-r;
RA Raulais D., Lagente-Chevallier O., Guettet C., Duprez D., Courtois Y.,
RA Vigny M.;
RT "A new heparin binding protein regulated by retinoic acid from chick
RT embryo.";
RL Biochem. Biophys. Res. Commun. 174:708-715(1991).
RN [4]
RP PROTEIN SEQUENCE OF 22-77.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=2558016; DOI=10.1111/j.1432-1033.1989.tb15267.x;
RA Vigny M., Raulais D., Puzenat N., Duprez D., Hartman M.P., Jeanny J.C.,
RA Courtois Y.;
RT "Identification of a new heparin-binding protein localized within chick
RT basement membranes.";
RL Eur. J. Biochem. 186:733-740(1989).
CC -!- FUNCTION: Has mitogenic activity, and neurite extension activity for
CC PC12 cells.
CC -!- SUBCELLULAR LOCATION: Cell surface. Secreted, extracellular space,
CC extracellular matrix, basement membrane. Note=Basement membranes in
CC early embryonic tissues, and cell surface of neuroectodermal cells.
CC -!- DEVELOPMENTAL STAGE: Essentially expressed during embryogenesis.
CC -!- INDUCTION: By retinoic acid.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; M61754; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X76482; CAA54020.1; -; Genomic_DNA.
DR PIR; JT0573; JT0573.
DR RefSeq; NP_001106760.1; NM_001113289.1.
DR AlphaFoldDB; P24052; -.
DR SMR; P24052; -.
DR STRING; 9031.ENSGALP00000013607; -.
DR PaxDb; P24052; -.
DR PRIDE; P24052; -.
DR GeneID; 423196; -.
DR KEGG; gga:423196; -.
DR CTD; 4192; -.
DR VEuPathDB; HostDB:geneid_423196; -.
DR eggNOG; ENOG502S022; Eukaryota.
DR InParanoid; P24052; -.
DR OrthoDB; 1489280at2759; -.
DR PhylomeDB; P24052; -.
DR PRO; PR:P24052; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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 Basement membrane; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Growth factor; Heparin-binding; Mitogen; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:1993066,
FT ECO:0000269|PubMed:2558016"
FT CHAIN 22..142
FT /note="Midkine"
FT /id="PRO_0000024665"
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 89
FT /note="S -> R (in Ref. 2; CAA54020)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="C -> G (in Ref. 2; CAA54020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15579 MW; 9D05CAFB9558451B CRC64;
MQPRGLLLLL ALLLLAAAAE AAKAKKEKMK KEGSECQDWH WGPCIPNSKD CGLGYREGSC
GDESRKLKCK IPCNWKKKFG ADCKYKFESW GGCSAKTGVK TRSGILKKAL YNAECEEVVY
VSKPCTAKMK AKAKAKKGKG KD
