NGF_PIG
ID NGF_PIG Reviewed; 229 AA.
AC Q29074;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Beta-nerve growth factor;
DE Short=Beta-NGF;
DE Flags: Precursor; Fragment;
GN Name=NGF; Synonyms=NGFB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white; TISSUE=Blood;
RX PubMed=8039422; DOI=10.1159/000133811;
RA Lahbib-Mansais Y., Mellink C., Yerle M., Gellin J.;
RT "A new marker (NGFB) on pig chromosome 4, isolated by using a consensus
RT sequence conserved among species.";
RL Cytogenet. Cell Genet. 67:120-125(1994).
CC -!- FUNCTION: Nerve growth factor is important for the development and
CC maintenance of the sympathetic and sensory nervous systems.
CC Extracellular ligand for the NTRK1 and NGFR receptors, activates
CC cellular signaling cascades to regulate neuronal proliferation,
CC differentiation and survival (By similarity). The immature NGF
CC precursor (proNGF) functions as ligand for the heterodimeric receptor
CC formed by SORCS2 and NGFR, and activates cellular signaling cascades
CC that lead to inactivation of RAC1 and/or RAC2, reorganization of the
CC actin cytoskeleton and neuronal growth cone collapse. In contrast to
CC mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in
CC vitro) (By similarity). Inhibits metalloproteinase-dependent
CC proteolysis of platelet glycoprotein VI (By similarity). Binds
CC lysophosphatidylinositol and lysophosphatidylserine between the two
CC chains of the homodimer. The lipid-bound form promotes histamine relase
CC from mast cells, contrary to the lipid-free form (By similarity).
CC {ECO:0000250|UniProtKB:P01138, ECO:0000250|UniProtKB:P01139}.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with a single NTRK1 chain.
CC The homodimer interacts with a single NGFR chain (By similarity). The
CC NGF dimer interacts with a single SORCS2 chain (via extracellular
CC domain). The NGF precursor (proNGF) binds to a receptor complex formed
CC by SORT1 and NGFR, which leads to NGF endocytosis. Both mature NGF and
CC the immature NGF precursor (proNGF) interact with SORCS2 and with the
CC heterodimer formed by SORCS2 and NGFR (via extracellular domains). The
CC NGF precursor (proNGF) has much higher affinity for SORCS2 than mature
CC NGF. The NGF precursor (proNGF) has much higher affinity for SORT1 than
CC mature NGF (By similarity). Interacts with ADAM10 in a divalent cation-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:P01138,
CC ECO:0000250|UniProtKB:P01139}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01138}. Endosome
CC lumen {ECO:0000250|UniProtKB:P01139}. Note=ProNGF is endocytosed after
CC binding to the cell surface receptor formed by SORT1 and NGFR.
CC {ECO:0000250|UniProtKB:P01139}.
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR EMBL; L31898; AAA21301.1; -; Genomic_DNA.
DR PIR; I46614; I46614.
DR AlphaFoldDB; Q29074; -.
DR SMR; Q29074; -.
DR STRING; 9823.ENSSSCP00000007197; -.
DR PaxDb; Q29074; -.
DR eggNOG; ENOG502RYPU; Eukaryota.
DR InParanoid; Q29074; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005163; F:nerve growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0007613; P:memory; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
DR GO; GO:0021675; P:nerve development; IBA:GO_Central.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR020408; Nerve_growth_factor-like.
DR InterPro; IPR002072; Nerve_growth_factor-rel.
DR InterPro; IPR020425; Nerve_growth_factor_bsu.
DR InterPro; IPR020437; Nerve_growth_factor_bsu_mml.
DR InterPro; IPR019846; Nerve_growth_factor_CS.
DR PANTHER; PTHR11589; PTHR11589; 1.
DR Pfam; PF00243; NGF; 1.
DR PIRSF; PIRSF001789; NGF; 1.
DR PRINTS; PR01925; MAMLNGFBETA.
DR PRINTS; PR00268; NGF.
DR PRINTS; PR01913; NGFBETA.
DR SMART; SM00140; NGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00248; NGF_1; 1.
DR PROSITE; PS50270; NGF_2; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein;
KW Growth factor; Lipid-binding; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL <1..6
FT /evidence="ECO:0000255"
FT PROPEP 7..109
FT /evidence="ECO:0000250"
FT /id="PRO_0000019605"
FT CHAIN 110..229
FT /note="Beta-nerve growth factor"
FT /id="PRO_0000019606"
FT REGION 77..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol)"
FT /ligand_id="ChEBI:CHEBI:64771"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P01139"
FT BINDING 197
FT /ligand="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol)"
FT /ligand_id="ChEBI:CHEBI:64771"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P01139"
FT BINDING 197
FT /ligand="a 1-acyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:64379"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P01139"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..189
FT /evidence="ECO:0000250|UniProtKB:P01138"
FT DISULFID 167..217
FT /evidence="ECO:0000250|UniProtKB:P01138"
FT DISULFID 177..219
FT /evidence="ECO:0000250|UniProtKB:P01138"
FT NON_TER 1
SQ SEQUENCE 229 AA; 25276 MW; FE8890771CBA3189 CRC64;
LIGIQAEPHT ESNVPAGHAI PQAHWTKLQH SLDTALRRAH SAPAGANSAR VAGQTRNITV
DPKLFKKRRL RSPRVLFSTQ PPPVAADTQD PDLEASGAAS FNRTHRSKRS SSHPVFHRGE
FSVCDSVSVW VGDKTTATDI KGKEVMVLGE VNINNSVFKQ YFFETKCRDP NPVDSGCRGI
DSKHWNSYCT TTHTFVKALT MDGKQAAWRF IRIDTACVCV LSRKAGRRA
