NENF_RAT
ID NENF_RAT Reviewed; 171 AA.
AC Q6IUR5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 {ECO:0000250|UniProtKB:Q9CQ45};
GN Synonyms=Scirp10 {ECO:0000312|EMBL:AAT39544.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAT39544.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu S., Li X., Wang Y., Ma Z., Que H., Liu T.;
RT "Spinal cord injury related protein 10.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH PINK1 AND PARK7, AND SUBCELLULAR LOCATION.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
CC -!- FUNCTION: Acts as a neurotrophic factor in postnatal mature neurons
CC enhancing neuronal survival (PubMed:31536960). 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 ECO:0000269|PubMed:31536960}.
CC -!- SUBUNIT: Interacts with PINK1 and PARK7. {ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9CQ45}. Mitochondrion
CC {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:31536960}. 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 81. {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:0000255}.
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DR EMBL; AY623793; AAT39544.1; -; mRNA.
DR RefSeq; NP_001002851.1; NM_001002851.1.
DR AlphaFoldDB; Q6IUR5; -.
DR SMR; Q6IUR5; -.
DR STRING; 10116.ENSRNOP00000005190; -.
DR jPOST; Q6IUR5; -.
DR PaxDb; Q6IUR5; -.
DR PRIDE; Q6IUR5; -.
DR Ensembl; ENSRNOT00000005190; ENSRNOP00000005190; ENSRNOG00000003833.
DR GeneID; 289380; -.
DR KEGG; rno:289380; -.
DR CTD; 29937; -.
DR RGD; 1303289; Nenf.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000162504; -.
DR HOGENOM; CLU_134788_0_0_1; -.
DR InParanoid; Q6IUR5; -.
DR OMA; FNIRDEF; -.
DR OrthoDB; 1532459at2759; -.
DR PhylomeDB; Q6IUR5; -.
DR TreeFam; TF332131; -.
DR PRO; PR:Q6IUR5; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003833; Expressed in heart and 19 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Metal-binding;
KW Mitochondrion; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..171
FT /note="Neudesin"
FT /id="PRO_0000042834"
FT DOMAIN 43..128
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX5"
SQ SEQUENCE 171 AA; 18992 MW; 2094FD2C7594F7A8 CRC64;
MARPAPWWWL RPLAALALAL ALVRVPSARA GQMPRPAERG PPVRLFTEEE LARYSGEEED
QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL AGKDSSRGVA KMSLDPADLT HDISGLTAKE
LEALDDIFSK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F
