NEUT_BOVIN
ID NEUT_BOVIN Reviewed; 170 AA.
AC P01156; Q3ZCG0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 130.
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 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 [MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Reddick K.D., Schmutz S.M.;
RT "Polymorphism identification in the neurotensin gene of cattle.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 151-163.
RC TISSUE=Hypothalamus;
RX PubMed=1167549; DOI=10.1016/s0021-9258(19)41780-8;
RA Carraway R., Leeman S.E.;
RT "The amino acid sequence of a hypothalamic peptide, neurotensin.";
RL J. Biol. Chem. 250:1907-1911(1975).
RN [5]
RP SYNTHESIS OF NEUROTENSIN.
RX PubMed=1112838; DOI=10.1016/s0021-9258(19)41781-x;
RA Carraway R., Leeman S.E.;
RT "The synthesis of neurotensin.";
RL J. Biol. Chem. 250:1912-1918(1975).
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 -!- TISSUE SPECIFICITY: Brain and gut.
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=AAA30668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M18621; AAA30668.1; ALT_INIT; mRNA.
DR EMBL; DQ515198; ABF72466.1; -; mRNA.
DR EMBL; BC102381; AAI02382.1; -; mRNA.
DR PIR; A01420; UNBO.
DR RefSeq; NP_776370.2; NM_173945.4.
DR AlphaFoldDB; P01156; -.
DR STRING; 9913.ENSBTAP00000006980; -.
DR PaxDb; P01156; -.
DR Ensembl; ENSBTAT00000006980; ENSBTAP00000006980; ENSBTAG00000005305.
DR GeneID; 280881; -.
DR KEGG; bta:280881; -.
DR CTD; 4922; -.
DR VEuPathDB; HostDB:ENSBTAG00000005305; -.
DR VGNC; VGNC:32311; NTS.
DR eggNOG; ENOG502RYW6; Eukaryota.
DR GeneTree; ENSGT00640000091574; -.
DR HOGENOM; CLU_133874_0_0_1; -.
DR InParanoid; P01156; -.
DR OMA; WGLCSDS; -.
DR OrthoDB; 1378763at2759; -.
DR TreeFam; TF330765; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000005305; Expressed in fornix of vagina and 79 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:0000255"
FT CHAIN 24..148
FT /note="Large neuromedin N"
FT /id="PRO_0000019513"
FT PEPTIDE 143..148
FT /note="Neuromedin N"
FT /id="PRO_0000019514"
FT PEPTIDE 151..163
FT /note="Neurotensin"
FT /id="PRO_0000019515"
FT PEPTIDE 166..170
FT /note="Tail peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019516"
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; 19843 MW; C6ED46ED9A41D468 CRC64;
MMAGMKIQLV CMILLAFSSW SLCSDSEEEM KALETDLLTN MHTSKISKAS VPSWKMSLLN
VCSLINNLNS QAEETGEFHE EELITRRKFP AALDGFSLEA MLTIYQLQKI CHSRAFQHWE
LIQEDILDAG NDKNEKEEVI KRKIPYILKR QLYENKPRRP YILKRGSYYY
