NEUT_RAT
ID NEUT_RAT Reviewed; 169 AA.
AC P20068; Q9QV80;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Neurotensin/neuromedin N;
DE Contains:
DE RecName: Full=Large neuromedin N;
DE AltName: Full=NmN-125;
DE Contains:
DE RecName: Full=Neuromedin N;
DE Short=NN;
DE Short=NmN;
DE Contains:
DE RecName: Full=Neurotensin;
DE Short=NT;
DE Contains:
DE RecName: Full=Tail peptide;
DE Flags: Precursor;
GN Name=Nts;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832414; DOI=10.1016/s0021-9258(18)68881-7;
RA Kislauskis E., Bullock B., McNeil S., Dobner P.R.;
RT "The rat gene encoding neurotensin and neuromedin N. Structure, tissue-
RT specific expression, and evolution of exon sequences.";
RL J. Biol. Chem. 263:4963-4968(1988).
RN [2]
RP PROTEIN SEQUENCE OF 23-42, AND PROTEOLYTIC PROCESSING.
RX PubMed=8471039; DOI=10.1042/bj2910225;
RA Bidard J.-N., de Nadai F., Rovere C., Moinier D., Laur J., Martinez J.,
RA Cuber J.-C., Kitabgi P.;
RT "Immunological and biochemical characterization of processing products from
RT the neurotensin/neuromedin N precursor in the rat medullary thyroid
RT carcinoma 6-23 cell line.";
RL Biochem. J. 291:225-233(1993).
RN [3]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8462460; DOI=10.1210/endo.132.4.8462460;
RA de Nadai F., Rovere C., Bidard J.-N., Laur J., Martinez J., Cuber J.-C.,
RA Kitabgi P.;
RT "Biosynthesis and posttranslational processing of the
RT neurotensin/neuromedin N precursor in the rat medullary thyroid carcinoma
RT 6-23 cell line. Effect of dexamethasone.";
RL Endocrinology 132:1614-1620(1993).
CC -!- FUNCTION: Neurotensin may play an endocrine or paracrine role in the
CC regulation of fat metabolism. It causes contraction of smooth muscle.
CC -!- SUBUNIT: Interacts with NTSR1. Interacts with SORT1. Interacts with
CC SORL1. {ECO:0000250|UniProtKB:P30990}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle.
CC Note=Packaged within secretory vesicles.
CC -!- PTM: [Neurotensin]: Neurotensin is cleaved and degraded by Angiotensin-
CC converting enzyme (ACE) and neprilysin (MME).
CC {ECO:0000250|UniProtKB:P30990}.
CC -!- SIMILARITY: Belongs to the neurotensin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M21187; AAA41712.1; ALT_INIT; Genomic_DNA.
DR EMBL; M21218; AAA41712.1; JOINED; Genomic_DNA.
DR PIR; A28146; A28146.
DR PDB; 3ZEV; X-ray; 3.00 A; C/D=157-162.
DR PDB; 4BUO; X-ray; 2.75 A; C/D=157-162.
DR PDB; 4BV0; X-ray; 3.10 A; C/D=157-162.
DR PDB; 4BWB; X-ray; 3.57 A; C/D=157-162.
DR PDB; 4GRV; X-ray; 2.80 A; B=157-162.
DR PDB; 4XEE; X-ray; 2.90 A; B=157-162.
DR PDB; 4XES; X-ray; 2.60 A; B=157-162.
DR PDB; 5T04; X-ray; 3.30 A; B=157-162.
DR PDB; 7L0P; EM; 4.10 A; D=157-162.
DR PDB; 7L0Q; EM; 4.30 A; D=157-162.
DR PDB; 7L0R; EM; 4.20 A; D=157-162.
DR PDB; 7L0S; EM; 4.50 A; D=157-162.
DR PDBsum; 3ZEV; -.
DR PDBsum; 4BUO; -.
DR PDBsum; 4BV0; -.
DR PDBsum; 4BWB; -.
DR PDBsum; 4GRV; -.
DR PDBsum; 4XEE; -.
DR PDBsum; 4XES; -.
DR PDBsum; 5T04; -.
DR PDBsum; 7L0P; -.
DR PDBsum; 7L0Q; -.
DR PDBsum; 7L0R; -.
DR PDBsum; 7L0S; -.
DR AlphaFoldDB; P20068; -.
DR SMR; P20068; -.
DR IntAct; P20068; 3.
DR STRING; 10116.ENSRNOP00000005706; -.
DR PaxDb; P20068; -.
DR UCSC; RGD:621612; rat.
DR RGD; 621612; Nts.
DR eggNOG; ENOG502RYW6; Eukaryota.
DR InParanoid; P20068; -.
DR PhylomeDB; P20068; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P20068; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0071855; F:neuropeptide receptor binding; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0097332; P:response to antipsychotic drug; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
DR GO; GO:0008542; P:visual learning; IMP:RGD.
DR InterPro; IPR008055; NeurotensiN.
DR PANTHER; PTHR15356; PTHR15356; 1.
DR Pfam; PF07421; Pro-NT_NN; 1.
DR PRINTS; PR01668; NEUROTENSIN.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Reference proteome; Secreted; Signal;
KW Vasoactive.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8471039"
FT CHAIN 23..147
FT /note="Large neuromedin N"
FT /id="PRO_0000019530"
FT PEPTIDE 142..147
FT /note="Neuromedin N"
FT /id="PRO_0000019531"
FT PEPTIDE 150..162
FT /note="Neurotensin"
FT /id="PRO_0000019532"
FT PEPTIDE 165..169
FT /note="Tail peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019533"
FT SITE 159..160
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000250|UniProtKB:P30990"
FT SITE 160..161
FT /note="Cleavage; by ACE and MME"
FT /evidence="ECO:0000250|UniProtKB:P30990"
SQ SEQUENCE 169 AA; 19564 MW; 91CF0CF68C3D3C91 CRC64;
MIGMNLQLVC LTLLAFSSWS LCSDSEEDVR ALEADLLTNM HASKVSKGSP PSWKMTLLNV
CSLINNLNSA AEEAGEMRDD DLVAKRKLPL VLDDFSLEAL LTVFQLQKIC RSRAFQHWEI
IQEDILDHGN EKTEKEEVIK RKIPYILKRQ LYENKPRRPY ILKRASYYY
