NENF_BOVIN
ID NENF_BOVIN Reviewed; 169 AA.
AC Q1JQA5;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Neudesin;
DE AltName: Full=Neuron-derived neurotrophic factor;
DE AltName: Full=SCIRP10-related protein;
DE AltName: Full=Spinal cord injury-related protein 10;
DE Flags: Precursor;
GN Name=NENF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a neurotrophic factor in postnatal mature neurons
CC enhancing neuronal survival (By similarity). Promotes cell
CC proliferation and neurogenesis in undifferentiated neural progenitor
CC cells at the embryonic stage and inhibits differentiation of astrocytes
CC (By similarity). Its neurotrophic activity is exerted via MAPK1/ERK2,
CC MAPK3/ERK1 and AKT1/AKT pathways (By similarity). Neurotrophic activity
CC is enhanced by binding to heme (By similarity). Acts also as an
CC anorexigenic neurotrophic factor that contributes to energy balance (By
CC similarity). {ECO:0000250|UniProtKB:Q9CQ45}.
CC -!- SUBUNIT: Interacts with PINK1 and PARK7.
CC {ECO:0000250|UniProtKB:Q9UMX5}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9CQ45}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9UMX5}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9UMX5}. Note=Localized to mitochondria and
CC endoplasmic reticulum by PINK1 and PARK7.
CC {ECO:0000250|UniProtKB:Q9UMX5}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain was proven to bind heme,
CC although it lacks the conserved iron-binding His residue at position
CC 79. {ECO:0000250}.
CC -!- MISCELLANEOUS: Non-classical progesterone receptors involved in
CC extranuclear signaling are classified in 2 groups: the class II
CC progestin and adipoQ receptor (PAQR) family (also called mPRs) (PAQR5,
CC PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like heme/steroid-binding
CC protein family (also called MAPRs) (PGRMC1, PGRMC2, NENF and CYB5D2).
CC {ECO:0000250|UniProtKB:Q9UMX5}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; BC116106; AAI16107.1; -; mRNA.
DR RefSeq; NP_001069887.1; NM_001076419.1.
DR AlphaFoldDB; Q1JQA5; -.
DR SMR; Q1JQA5; -.
DR STRING; 9913.ENSBTAP00000001007; -.
DR PaxDb; Q1JQA5; -.
DR PRIDE; Q1JQA5; -.
DR Ensembl; ENSBTAT00000001007; ENSBTAP00000001007; ENSBTAG00000000759.
DR GeneID; 616334; -.
DR KEGG; bta:616334; -.
DR CTD; 29937; -.
DR VEuPathDB; HostDB:ENSBTAG00000000759; -.
DR VGNC; VGNC:32006; NENF.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000162504; -.
DR HOGENOM; CLU_134788_0_0_1; -.
DR InParanoid; Q1JQA5; -.
DR OMA; FNIRDEF; -.
DR OrthoDB; 1532459at2759; -.
DR TreeFam; TF332131; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000000759; Expressed in laryngeal cartilage and 106 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0032099; P:negative regulation of appetite; ISS:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Metal-binding;
KW Mitochondrion; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..169
FT /note="Neudesin"
FT /id="PRO_0000350625"
FT DOMAIN 41..126
FT /note="Cytochrome b5 heme-binding"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX5"
SQ SEQUENCE 169 AA; 18313 MW; 1BB40E1B7DFEFF2F CRC64;
MAGPAPGRRL VALALIVALA VGLPTAGAGQ APRPAERGPP VRLFTEEELA RYGGEEEDQP
IYMAVKGVVF DVTSGKEFYG RGAPYNALTG KDSTRGVAKM SLDPADLTHD TTGLTAEELE
SLDDVFTRVY KAKYPIVGYT ARRILNEDGS PNLDFKPEDQ PHFDIKDEF