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GDNF_DANRE
ID   GDNF_DANRE              Reviewed;         235 AA.
AC   Q98TU0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glial cell line-derived neurotrophic factor;
DE            Short=zGDNF;
DE   Flags: Precursor;
GN   Name=gdnf {ECO:0000312|EMBL:AAK11259.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK11259.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Glial cell {ECO:0000269|PubMed:11237470};
RX   PubMed=11237470; DOI=10.1006/dbio.2000.0145;
RA   Shepherd I.T., Beattie C.E., Raible D.W.;
RT   "Functional analysis of zebrafish GDNF.";
RL   Dev. Biol. 231:420-435(2001).
CC   -!- FUNCTION: Neurotrophic factor that enhances survival and morphological
CC       differentiation of dopaminergic neurons and increases their high-
CC       affinity dopamine uptake (By similarity). Essential for the development
CC       of the enteric nervous system, but appears dispensable for the
CC       development of the kidney and primary motor neuron. {ECO:0000250,
CC       ECO:0000269|PubMed:11237470}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q07731}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: First expressed at 14 hours post-fertilization
CC       (hpf) in the ventral half of anterior somites and in intermediate
CC       mesoderm. Ventral somitic expression persists and extends more
CC       posteriorly over the next 12 hours. Expressed throughout the ventral
CC       trunk mesoderm and endoderm at 24 hpf. By 30 hpf, somitic expression
CC       ceases and by 36 hpf, expression becomes restricted to the endodermal
CC       cells forming the gut, with expression along the whole length of the
CC       developing gut tube at 72 hpf. {ECO:0000269|PubMed:11237470}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.
CC       {ECO:0000255}.
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DR   EMBL; AF329853; AAK11259.1; -; mRNA.
DR   PDB; 7AB8; X-ray; 2.20 A; B=138-235.
DR   PDB; 7AML; EM; 3.50 A; C/F=135-235.
DR   PDBsum; 7AB8; -.
DR   PDBsum; 7AML; -.
DR   AlphaFoldDB; Q98TU0; -.
DR   SMR; Q98TU0; -.
DR   STRING; 7955.ENSDARP00000124666; -.
DR   PaxDb; Q98TU0; -.
DR   ZFIN; ZDB-GENE-010226-1; gdnfa.
DR   eggNOG; ENOG502QWCH; Eukaryota.
DR   InParanoid; Q98TU0; -.
DR   PhylomeDB; Q98TU0; -.
DR   Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-DRE-8853659; RET signaling.
DR   PRO; PR:Q98TU0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030116; F:glial cell-derived neurotrophic factor receptor binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:ZFIN.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:InterPro.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048484; P:enteric nervous system development; IMP:ZFIN.
DR   GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR   GO; GO:0030432; P:peristalsis; ISS:UniProtKB.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0032770; P:positive regulation of monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0072107; P:positive regulation of ureteric bud formation; ISS:UniProtKB.
DR   GO; GO:0021784; P:postganglionic parasympathetic fiber development; ISS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; IPI:ZFIN.
DR   GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; ISS:UniProtKB.
DR   GO; GO:0060688; P:regulation of morphogenesis of a branching structure; ISS:UniProtKB.
DR   GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR016649; GDNF.
DR   InterPro; IPR043401; GDNF_fam.
DR   InterPro; IPR001839; TGF-b_C.
DR   PANTHER; PTHR12173; PTHR12173; 1.
DR   PANTHER; PTHR12173:SF1; PTHR12173:SF1; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   PIRSF; PIRSF016238; GDNF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..87
FT                   /evidence="ECO:0000250|UniProtKB:Q07731"
FT                   /id="PRO_0000292932"
FT   CHAIN           90..235
FT                   /note="Glial cell line-derived neurotrophic factor"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000292933"
FT   REGION          34..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        142..203
FT                   /evidence="ECO:0000250|UniProtKB:Q07731"
FT   DISULFID        169..232
FT                   /evidence="ECO:0000250|UniProtKB:Q07731"
FT   DISULFID        173..234
FT                   /evidence="ECO:0000250|UniProtKB:Q07731"
FT   DISULFID        202
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q07731"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   STRAND          163..171
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   HELIX           179..190
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   TURN            191..195
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:7AB8"
FT   STRAND          228..234
FT                   /evidence="ECO:0007829|PDB:7AB8"
SQ   SEQUENCE   235 AA;  26829 MW;  EB711B38D755F329 CRC64;
     MKLWDILATC LLLLSSVSTR PLFHKLQPSK RAVVRSESPA LDPIIDSQPE TSNPKQASME
     EQYDLTGLYP EQFEDVMDFI EATLGRLRRS SDVEPQMKRD RVRQKAAANT EKSGGRGRGE
     RKRSRGRARS RDDRVKGQGR GCLLKEIHLN VTDLDLGYRT KEELIFRYCS GPCHDAETNY
     DKILNNLTHN KKLDKDTPSR TCCRPIAFDD DISFLDDSLE YHTLKKHSAK KCACV
 
 
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