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MKB_XENLA
ID   MKB_XENLA               Reviewed;         142 AA.
AC   P48531; Q6GQG8;
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=Midkine-B {ECO:0000305};
DE            Short=MK-B;
DE   AltName: Full=Pleiotrophic factor-alpha-2 {ECO:0000303|PubMed:7677748};
DE            Short=PTF-alpha-2;
DE            Short=X-PTF-alpha2;
DE   Flags: Precursor;
GN   Name=mdk-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], 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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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}.
CC   -!- TISSUE SPECIFICITY: In adults, expression is highest in the brain, eye
CC       and bone, with lower expression in the heart and lung. Not expressed in
CC       the ovary. In the tailbud stage embryo, expressed in the head and tail
CC       regions as well as in the central nervous system (CNS).
CC       {ECO:0000269|PubMed:7677748}.
CC   -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR   EMBL; D42057; BAA07657.1; -; mRNA.
DR   EMBL; BC072776; AAH72776.1; -; mRNA.
DR   PIR; JC4273; JC4273.
DR   RefSeq; NP_001084019.1; NM_001090550.1.
DR   RefSeq; XP_018112064.1; XM_018256575.1.
DR   RefSeq; XP_018112065.1; XM_018256576.1.
DR   AlphaFoldDB; P48531; -.
DR   SMR; P48531; -.
DR   PRIDE; P48531; -.
DR   DNASU; 399256; -.
DR   GeneID; 399256; -.
DR   KEGG; xla:399256; -.
DR   CTD; 399256; -.
DR   Xenbase; XB-GENE-6254190; mdk.L.
DR   OMA; ATECAEW; -.
DR   OrthoDB; 1489280at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 399256; 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; 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: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; 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-B"
FT                   /id="PRO_0000024667"
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"
SQ   SEQUENCE   142 AA;  15595 MW;  BB47060745F88B28 CRC64;
     MELRAFCVIL LITILAVSSQ AAKNKKEKGK KGASDCTEWT WGSCIPNSKD CGAGTREGTC
     KEETRKLKCK IPCNWKKDFG ADCKYKFENW GECNATTGQK VRSGTLKKAL YNADCQQTVE
     AAKPCSLKTK SKSKGKKGKG KE
 
 
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