NEUT_CANLF
ID NEUT_CANLF Reviewed; 170 AA.
AC P10673; Q9TS28;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=NT-tail;
DE Contains:
DE RecName: Full=Tail peptide;
DE Flags: Precursor;
GN Name=NTS;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3472221; DOI=10.1073/pnas.84.10.3516;
RA Dobner P.R., Barber D.L., Villa-Komaroff L., McKiernan C.;
RT "Cloning and sequence analysis of cDNA for the canine
RT neurotensin/neuromedin N precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3516-3520(1987).
RN [2]
RP PROTEIN SEQUENCE OF 128-148.
RX PubMed=2341398; DOI=10.1016/s0021-9258(19)38933-1;
RA Carraway R.E., Mitra S.P.;
RT "Differential processing of neurotensin/neuromedin N precursor(s) in canine
RT brain and intestine.";
RL J. Biol. Chem. 265:8627-8631(1990).
RN [3]
RP PROTEIN SEQUENCE OF 24-43.
RC TISSUE=Intestine;
RX PubMed=1883359; DOI=10.1016/0006-291x(91)91369-n;
RA Carraway R.E., Mitra S.P.;
RT "Purification of large neuromedin N (NMN) from canine intestine and its
RT identification as NMN-125.";
RL Biochem. Biophys. Res. Commun. 179:301-308(1991).
RN [4]
RP PROTEIN SEQUENCE OF 151-170.
RC TISSUE=Ileum;
RX PubMed=1494486; DOI=10.1016/0196-9781(92)90003-l;
RA Carraway R.E., Mitra S.P., Salmonsen R.;
RT "Isolation and quantitation of several new peptides from the canine
RT neurotensin/neuromedin N precursor.";
RL Peptides 13:1039-1047(1992).
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}.
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DR EMBL; M16443; AAA30878.1; -; mRNA.
DR PIR; A28025; UNDG.
DR RefSeq; NP_001300803.1; NM_001313874.1.
DR AlphaFoldDB; P10673; -.
DR STRING; 9615.ENSCAFP00000008959; -.
DR PaxDb; P10673; -.
DR Ensembl; ENSCAFT00030035712; ENSCAFP00030031144; ENSCAFG00030019410.
DR Ensembl; ENSCAFT00040025804; ENSCAFP00040022440; ENSCAFG00040013954.
DR Ensembl; ENSCAFT00845022032; ENSCAFP00845017320; ENSCAFG00845012392.
DR GeneID; 611687; -.
DR KEGG; cfa:611687; -.
DR CTD; 4922; -.
DR VEuPathDB; HostDB:ENSCAFG00845012392; -.
DR eggNOG; ENOG502RYW6; Eukaryota.
DR GeneTree; ENSGT00640000091574; -.
DR HOGENOM; CLU_133874_0_0_1; -.
DR InParanoid; P10673; -.
DR OMA; WGLCSDS; -.
DR OrthoDB; 1378763at2759; -.
DR TreeFam; TF330765; -.
DR Reactome; R-CFA-375276; Peptide ligand-binding receptors.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Proteomes; UP000002254; Chromosome 15.
DR Bgee; ENSCAFG00000005976; Expressed in jejunum and 32 other tissues.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
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 Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Reference proteome; Secreted; Signal;
KW Vasoactive.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1883359"
FT CHAIN 24..148
FT /note="Large neuromedin N"
FT /id="PRO_0000019517"
FT PEPTIDE 143..148
FT /note="Neuromedin N"
FT /id="PRO_0000019518"
FT PEPTIDE 151..170
FT /note="NT-tail"
FT /id="PRO_0000019519"
FT PEPTIDE 151..163
FT /note="Neurotensin"
FT /id="PRO_0000019520"
FT PEPTIDE 166..170
FT /note="Tail peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019521"
FT SITE 160..161
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000250|UniProtKB:P30990"
FT SITE 161..162
FT /note="Cleavage; by ACE and MME"
FT /evidence="ECO:0000250|UniProtKB:P30990"
SQ SEQUENCE 170 AA; 19863 MW; A54700163AC54962 CRC64;
MMAGMKIQLV CMILLAFSSW SLCSDSEEEM KALEADLLTN MHTSKISKAS VSSWKMTLLN
VCSFVNNLNS QAEETGEFRE EELITRRKFP TALDGFSLEA MLTIYQLQKI CHSRAFQQWE
LIQEDVLDAG NDKNEKEEVI KRKIPYILKR QLYENKPRRP YILKRGSYYY
