ID NGF_MOUSE Reviewed; 241 AA. AC P01139; Q63864; Q6LDB7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=Beta-nerve growth factor; DE Short=Beta-NGF; DE Flags: Precursor; GN Name=Ngf; Synonyms=Ngfb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Submandibular gland; RX PubMed=6336309; DOI=10.1038/302538a0; RA Scott J., Selby M.J., Urdea M.S., Quiroga M., Bell G.I., Rutter W.J.; RT "Isolation and nucleotide sequence of a cDNA encoding the precursor of RT mouse nerve growth factor."; RL Nature 302:538-540(1983). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6688123; DOI=10.1038/303821a0; RA Ullrich A., Gray A., Berman C., Dull T.J.; RT "Human beta-nerve growth factor gene sequence highly homologous to that of RT mouse."; RL Nature 303:821-825(1983). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6327169; DOI=10.1101/sqb.1983.048.01.048; RA Ullrich A., Gray A., Berman C., Coussens L., Dull T.J.; RT "Sequence homology of human and mouse beta-NGF subunit genes."; RL Cold Spring Harb. Symp. Quant. Biol. 48:435-442(1983). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6J; TISSUE=Submandibular gland; RX PubMed=3670305; DOI=10.1128/mcb.7.9.3057-3064.1987; RA Selby M.J., Edwards R., Sharp F., Rutter W.J.; RT "Mouse nerve growth factor gene: structure and expression."; RL Mol. Cell. Biol. 7:3057-3064(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Skeletal muscle; RX PubMed=1284621; DOI=10.1016/0197-0186(92)90155-k; RA Yamamoto T., Yamakuni T., Okabe N., Amano T.; RT "Production and secretion of nerve growth factor by clonal striated muscle RT cell line, G8-1."; RL Neurochem. Int. 21:251-258(1992). RN [6] RP PROTEIN SEQUENCE OF 122-239. RX PubMed=4566923; DOI=10.1021/bi00725a018; RA Angeletti R.H., Hermodson M.A., Bradshaw R.A.; RT "Amino acid sequences of mouse 2.5S nerve growth factor. II. Isolation and RT characterization of the thermolytic and peptic peptides and the complete RT covalent structure."; RL Biochemistry 12:100-115(1973). RN [7] RP FUNCTION, AND INTERACTION WITH SORCS2 AND NGFR. RX PubMed=22155786; DOI=10.1126/scisignal.2002060; RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A., RA Chao M.V., Hempstead B.L.; RT "Neuronal growth cone retraction relies on proneurotrophin receptor RT signaling through Rac."; RL Sci. Signal. 4:RA82-RA82(2011). RN [8] RP INDUCTION. RX PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013; RA Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., RA Sassone-Corsi P., Ptacek L.J., Akassoglou K.; RT "p75 neurotrophin receptor is a clock gene that regulates oscillatory RT components of circadian and metabolic networks."; RL J. Neurosci. 33:10221-10234(2013). RN [9] RP INTERACTION WITH SORCS2. RX PubMed=24908487; DOI=10.1016/j.neuron.2014.04.022; RA Glerup S., Olsen D., Vaegter C.B., Gustafsen C., Sjoegaard S.S., Hermey G., RA Kjolby M., Molgaard S., Ulrichsen M., Boggild S., Skeldal S., RA Fjorback A.N., Nyengaard J.R., Jacobsen J., Bender D., Bjarkam C.R., RA Soerensen E.S., Fuechtbauer E.M., Eichele G., Madsen P., Willnow T.E., RA Petersen C.M., Nykjaer A.; RT "SorCS2 regulates dopaminergic wiring and is processed into an apoptotic RT two-chain receptor in peripheral glia."; RL Neuron 82:1074-1087(2014). RN [10] {ECO:0007744|PDB:1BET} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 131-237, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=1956407; DOI=10.1038/354411a0; RA McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., RA Blundell T.L.; RT "New protein fold revealed by a 2.3-A resolution crystal structure of nerve RT growth factor."; RL Nature 354:411-414(1991). RN [11] {ECO:0007744|PDB:1BTG} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 130-239, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=8201620; DOI=10.1006/jmbi.1994.1380; RA Holland D.R., Cousens L.S., Meng W., Matthews B.W.; RT "Nerve growth factor in different crystal forms displays structural RT flexibility and reveals zinc binding sites."; RL J. Mol. Biol. 239:385-400(1994). RN [12] {ECO:0007744|PDB:1SGF} RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 122-239 OF 7S COMPLEX. RC STRAIN=Swiss Webster; TISSUE=Submandibular gland; RX PubMed=9351801; DOI=10.1016/s0969-2126(97)00280-3; RA Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.; RT "Structure of mouse 7S NGF: a complex of nerve growth factor with four RT binding proteins."; RL Structure 5:1275-1285(1997). RN [13] {ECO:0007744|PDB:3IJ2} RP X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS) OF 19-241 IN COMPLEX WITH NGFR, RP FUNCTION, SUBUNIT, INTERACTION WITH SORT1 AND NGFR, SUBCELLULAR LOCATION, RP PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF 49-ARG-ARG-50; 79-ARG-LYS-80 AND RP 120-ARG-LYS-121, AND DISULFIDE BONDS. RX PubMed=20036257; DOI=10.1016/j.jmb.2009.12.030; RA Feng D., Kim T., Ozkan E., Light M., Torkin R., Teng K.K., Hempstead B.L., RA Garcia K.C.; RT "Molecular and structural insight into proNGF engagement of p75NTR and RT sortilin."; RL J. Mol. Biol. 396:967-984(2010). RN [14] {ECO:0007744|PDB:4EAX} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 122-241 IN COMPLEX WITH RP LYSOPHOSPHATIDYLSERINE, FUNCTION, INTERACTION WITH NTRK1, SUBUNIT, RP LIPID-BINDING, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-209. RX PubMed=22649032; DOI=10.1096/fj.12-207316; RA Tong Q., Wang F., Zhou H.Z., Sun H.L., Song H., Shu Y.Y., Gong Y., RA Zhang W.T., Cai T.X., Yang F.Q., Tang J., Jiang T.; RT "Structural and functional insights into lipid-bound nerve growth RT factors."; RL FASEB J. 26:3811-3821(2012). RN [15] {ECO:0007744|PDB:4XPJ} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 122-241 IN COMPLEX WITH RP LYSOPHOSPHATIDYLINOSITOL, FUNCTION, SUBUNIT, LIPID-BINDING, AND DISULFIDE RP BONDS. RX PubMed=26144237; DOI=10.1107/s2053230x15008870; RA Sun H.L., Jiang T.; RT "The structure of nerve growth factor in complex with RT lysophosphatidylinositol."; RL Acta Crystallogr. F 71:906-912(2015). RN [16] {ECO:0007744|PDB:6FFY} RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) OF 122-238 IN COMPLEX WITH SORCS2, RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=30061605; DOI=10.1038/s41467-018-05405-z; RA Leloup N., Chataigner L.M.P., Janssen B.J.C.; RT "Structural insights into SorCS2-Nerve Growth Factor complex formation."; RL Nat. Commun. 9:2979-2979(2018). CC -!- FUNCTION: Nerve growth factor is important for the development and CC maintenance of the sympathetic and sensory nervous systems CC (PubMed:20036257). Extracellular ligand for the NTRK1 and NGFR CC receptors, activates cellular signaling cascades to regulate neuronal CC proliferation, differentiation and survival (PubMed:22649032). The CC immature NGF precursor (proNGF) functions as a ligand for the CC heterodimeric receptor formed by SORCS2 and NGFR, and activates CC cellular signaling cascades that lead to inactivation of RAC1 and/or CC RAC2, reorganization of the actin cytoskeleton and neuronal growth cone CC collapse (PubMed:22155786). In contrast to mature NGF, the precursor CC form (proNGF) promotes neuronal apoptosis (in vitro) (PubMed:20036257). CC Inhibits metalloproteinase-dependent proteolysis of platelet CC glycoprotein VI (By similarity). Binds lysophosphatidylinositol and CC lysophosphatidylserine between the two chains of the homodimer CC (PubMed:22649032, PubMed:26144237). The lipid-bound form promotes CC histamine relase from mast cells, contrary to the lipid-free form CC (PubMed:22649032). {ECO:0000250|UniProtKB:P01138, CC ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786, CC ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237}. CC -!- SUBUNIT: Homodimer (PubMed:1956407, PubMed:8201620, PubMed:20036257, CC PubMed:22649032, PubMed:26144237, PubMed:30061605). The homodimer CC interacts with a single NTRK1 chain (PubMed:22649032). The homodimer CC interacts with a single NGFR chain (By similarity). The NGF dimer CC interacts with a single SORCS2 chain (via extracellular domain) CC (PubMed:30061605). The NGF precursor (proNGF) binds to a receptor CC complex formed by SORT1 and NGFR, which leads to NGF endocytosis CC (PubMed:20036257). Both mature NGF and the immature NGF precursor CC (proNGF) interact with SORCS2 and with the heterodimer formed by SORCS2 CC and NGFR (via extracellular domains) (PubMed:22155786, CC PubMed:30061605). The NGF precursor (proNGF) has much higher affinity CC for SORCS2 than mature NGF (PubMed:24908487). The NGF precursor CC (proNGF) has much higher affinity for SORT1 than mature NGF CC (PubMed:20036257). Interacts with ADAM10 in a divalent cation-dependent CC manner (By similarity). {ECO:0000250|UniProtKB:P01138, CC ECO:0000269|PubMed:1956407, ECO:0000269|PubMed:20036257, CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:22649032, CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:26144237, CC ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1284621}. Endosome CC lumen {ECO:0000269|PubMed:20036257}. Note=ProNGF is endocytosed after CC binding to the cell surface receptor formed by SORT1 and NGFR. CC {ECO:0000269|PubMed:20036257}. CC -!- TISSUE SPECIFICITY: Detected in submaxillary gland (at protein level) CC (PubMed:1284621). Highly expressed in male submaxillary gland. Levels CC are much lower in female submaxillary gland (PubMed:6336309, CC PubMed:1284621). {ECO:0000269|PubMed:1284621, CC ECO:0000269|PubMed:6336309}. CC -!- INDUCTION: Expression oscillates in a circadian manner in the CC suprachiasmatic nucleus (SCN) of the brain. CC {ECO:0000269|PubMed:23785138}. CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA37687.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAA39818.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAA39820.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAA39821.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA24221.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35075; AAA39818.1; ALT_INIT; mRNA. DR EMBL; V00836; CAA24221.1; ALT_INIT; mRNA. DR EMBL; K01759; AAA39820.1; ALT_INIT; mRNA. DR EMBL; M14805; AAA39821.1; ALT_INIT; mRNA. DR EMBL; M17298; AAA37687.1; ALT_INIT; Genomic_DNA. DR EMBL; M17296; AAA37687.1; JOINED; Genomic_DNA. DR EMBL; M17297; AAA37687.1; JOINED; Genomic_DNA. DR EMBL; S62089; AAB26820.2; -; mRNA. DR CCDS; CCDS51025.1; -. DR RefSeq; NP_001106168.1; NM_001112698.2. DR RefSeq; NP_038637.1; NM_013609.3. DR RefSeq; XP_006501171.1; XM_006501108.3. DR PDB; 1BET; X-ray; 2.30 A; A=131-237. DR PDB; 1BTG; X-ray; 2.50 A; A/B/C=130-239. DR PDB; 1SGF; X-ray; 3.15 A; B/Y=122-239. DR PDB; 3IJ2; X-ray; 3.75 A; A/B=19-241. DR PDB; 4EAX; X-ray; 2.30 A; A/B/C/D=122-241. DR PDB; 4XPJ; X-ray; 2.60 A; A/B=122-241. DR PDB; 5LSD; NMR; -; A/B=122-239. DR PDB; 6FFY; X-ray; 3.90 A; B/C=122-238. DR PDBsum; 1BET; -. DR PDBsum; 1BTG; -. DR PDBsum; 1SGF; -. DR PDBsum; 3IJ2; -. DR PDBsum; 4EAX; -. DR PDBsum; 4XPJ; -. DR PDBsum; 5LSD; -. DR PDBsum; 6FFY; -. DR AlphaFoldDB; P01139; -. DR SMR; P01139; -. DR BioGRID; 201764; 6. DR DIP; DIP-59840N; -. DR IntAct; P01139; 4. DR STRING; 10090.ENSMUSP00000102538; -. DR GlyCosmos; P01139; 2 sites, No reported glycans. DR GlyGen; P01139; 2 sites. DR PhosphoSitePlus; P01139; -. DR MaxQB; P01139; -. DR PaxDb; 10090-ENSMUSP00000102538; -. DR PeptideAtlas; P01139; -. DR ProteomicsDB; 252833; -. DR ABCD; P01139; 53 sequenced antibodies. DR Antibodypedia; 20173; 1453 antibodies from 44 providers. DR DNASU; 18049; -. DR Ensembl; ENSMUST00000035952.5; ENSMUSP00000040345.4; ENSMUSG00000027859.11. DR GeneID; 18049; -. DR KEGG; mmu:18049; -. DR UCSC; uc012cuz.2; mouse. DR AGR; MGI:97321; -. DR CTD; 4803; -. DR MGI; MGI:97321; Ngf. DR VEuPathDB; HostDB:ENSMUSG00000027859; -. DR eggNOG; ENOG502RYPU; Eukaryota. DR GeneTree; ENSGT00390000007725; -. DR HOGENOM; CLU_059942_1_1_1; -. DR InParanoid; P01139; -. DR OrthoDB; 5399313at2759; -. DR PhylomeDB; P01139; -. DR Reactome; R-MMU-167060; NGF processing. DR Reactome; R-MMU-170968; Frs2-mediated activation. DR Reactome; R-MMU-170984; ARMS-mediated activation. DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling. DR Reactome; R-MMU-187042; TRKA activation by NGF. DR Reactome; R-MMU-198203; PI3K/AKT activation. DR Reactome; R-MMU-205017; NFG and proNGF binds to p75NTR. DR Reactome; R-MMU-205025; NADE modulates death signalling. DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus. DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes. DR Reactome; R-MMU-209560; NF-kB is activated and signals survival. DR Reactome; R-MMU-209563; Axonal growth stimulation. DR BioGRID-ORCS; 18049; 0 hits in 80 CRISPR screens. DR EvolutionaryTrace; P01139; -. DR PRO; PR:P01139; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P01139; Protein. DR Bgee; ENSMUSG00000027859; Expressed in submandibular gland and 70 other cell types or tissues. DR ExpressionAtlas; P01139; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central. DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI. DR GO; GO:0038177; F:death receptor agonist activity; ISO:MGI. 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; ISO:MGI. DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:BHF-UCL. DR GO; GO:0008344; P:adult locomotory behavior; ISO:MGI. DR GO; GO:0048675; P:axon extension; IMP:MGI. DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI. DR GO; GO:0007613; P:memory; ISO:MGI. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI. DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISO:MGI. DR GO; GO:0021675; P:nerve development; IBA:GO_Central. DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI. DR GO; GO:0031175; P:neuron projection development; IDA:MGI. DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI. DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI. DR GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0048672; P:positive regulation of collateral sprouting; IDA:MGI. DR GO; GO:0043388; P:positive regulation of DNA binding; IMP:ARUK-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI. DR GO; GO:0014042; P:positive regulation of neuron maturation; IDA:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:MGI. DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI. DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:ParkinsonsUK-UCL. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:MGI. DR GO; GO:0045664; P:regulation of neuron differentiation; IDA:MGI. DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IGI:MGI. DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI. DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR DisProt; DP00836; -. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 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:SF10; BETA-NERVE GROWTH FACTOR; 1. DR PANTHER; PTHR11589; NERVE GROWTH FACTOR NGF -RELATED; 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; Cystine-knot cytokines; 1. DR PROSITE; PS00248; NGF_1; 1. DR PROSITE; PS50270; NGF_2; 1. DR Genevisible; P01139; MM. PE 1: Evidence at protein level; KW 3D-structure; Cleavage on pair of basic residues; KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein; KW Growth factor; Lipid-binding; Metalloenzyme inhibitor; KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:20036257" FT PROPEP 19..121 FT /evidence="ECO:0000305|PubMed:20036257, FT ECO:0000305|PubMed:4566923" FT /id="PRO_0000019601" FT CHAIN 122..241 FT /note="Beta-nerve growth factor" FT /id="PRO_0000019602" FT BINDING 171 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:0000269|PubMed:26144237, FT ECO:0007744|PDB:4XPJ" FT BINDING 171 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 /note="in other chain" FT /evidence="ECO:0000269|PubMed:22649032, FT ECO:0007744|PDB:4EAX" FT BINDING 173 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:0000269|PubMed:26144237, FT ECO:0007744|PDB:4XPJ" FT BINDING 209 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:0000269|PubMed:26144237, FT ECO:0007744|PDB:4XPJ" FT BINDING 209 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:0000269|PubMed:22649032, FT ECO:0007744|PDB:4EAX" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 114 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 136..201 FT /evidence="ECO:0000269|PubMed:1956407, FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237, FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620, FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG, FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2, FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ, FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY" FT DISULFID 179..229 FT /evidence="ECO:0000269|PubMed:1956407, FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237, FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620, FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG, FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2, FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ, FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY" FT DISULFID 189..231 FT /evidence="ECO:0000269|PubMed:1956407, FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237, FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620, FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG, FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2, FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ, FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY" FT MUTAGEN 49..50 FT /note="RR->AA: Abolishes production of the mature chain and FT promotes apoptosis of superior cervical ganglion neurons; FT when associated with 79-A-A-80 and 120-A-A-121." FT /evidence="ECO:0000269|PubMed:20036257" FT MUTAGEN 79..80 FT /note="KR->AA: Abolishes production of the mature chain and FT promotes apoptosis of superior cervical ganglion neurons; FT when associated with 49-A-A-50 and 120-A-A-121." FT /evidence="ECO:0000269|PubMed:20036257" FT MUTAGEN 120..121 FT /note="KR->AA: Abolishes production of the mature chain and FT promotes apoptosis of superior cervical ganglion neurons; FT when associated with 49-A-A-50 and 79-A-A-80." FT /evidence="ECO:0000269|PubMed:20036257" FT MUTAGEN 209 FT /note="K->L: Near loss of the ability to trigger histamine FT release from mast cells. No effect on interaction with FT NTRK1." FT /evidence="ECO:0000269|PubMed:22649032" FT CONFLICT 233..241 FT /note="LSRKATRRG -> CSAGRLQEEADLPAAPFPTCPLHTLLGPSLPQPVNYFKL FT (in Ref. 5; AAB26820)" FT /evidence="ECO:0000305" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:5LSD" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:4EAX" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 174..180 FT /evidence="ECO:0007829|PDB:1BET" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 197..213 FT /evidence="ECO:0007829|PDB:1BET" FT STRAND 218..235 FT /evidence="ECO:0007829|PDB:1BET" SQ SEQUENCE 241 AA; 27077 MW; 164465E1DC550081 CRC64; MSMLFYTLIT AFLIGVQAEP YTDSNVPEGD SVPEAHWTKL QHSLDTALRR ARSAPTAPIA ARVTGQTRNI TVDPRLFKKR RLHSPRVLFS TQPPPTSSDT LDLDFQAHGT IPFNRTHRSK RSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G //