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NEUT_MOUSE
ID   NEUT_MOUSE              Reviewed;         169 AA.
AC   Q9D3P9;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=11427716; DOI=10.1073/pnas.141042198;
RA   Dobner P.R., Fadel J., Deitemeyer N., Carraway R.E., Deutch A.Y.;
RT   "Neurotensin-deficient mice show altered responses to antipsychotic
RT   drugs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8048-8053(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Ahn H.-J., Cho J.-J.;
RT   "Mouse proneurotensin/proneuromedin N is induced in mast cell line after
RT   IgE cross-linking.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Neurotensin may play an endocrine or paracrine role in the
CC       regulation of fat metabolism. It causes contraction of smooth muscle
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NTSR1. Interacts with SORT1. Interacts with
CC       SORL1. {ECO:0000250|UniProtKB:P30990}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic vesicle,
CC       secretory vesicle {ECO:0000250}. Note=Packaged within secretory
CC       vesicles. {ECO:0000250}.
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; AF348489; AAK28626.1; -; Genomic_DNA.
DR   EMBL; AF304160; AAK15263.1; -; mRNA.
DR   EMBL; AK017212; BAB30636.1; -; mRNA.
DR   EMBL; BC043024; AAH43024.1; -; mRNA.
DR   CCDS; CCDS24154.1; -.
DR   RefSeq; NP_077755.1; NM_024435.2.
DR   AlphaFoldDB; Q9D3P9; -.
DR   STRING; 10090.ENSMUSP00000020040; -.
DR   PhosphoSitePlus; Q9D3P9; -.
DR   SwissPalm; Q9D3P9; -.
DR   PaxDb; Q9D3P9; -.
DR   PRIDE; Q9D3P9; -.
DR   ProteomicsDB; 287484; -.
DR   Antibodypedia; 29877; 303 antibodies from 27 providers.
DR   DNASU; 67405; -.
DR   Ensembl; ENSMUST00000020040; ENSMUSP00000020040; ENSMUSG00000019890.
DR   GeneID; 67405; -.
DR   KEGG; mmu:67405; -.
DR   UCSC; uc007gye.1; mouse.
DR   CTD; 4922; -.
DR   MGI; MGI:1328351; Nts.
DR   VEuPathDB; HostDB:ENSMUSG00000019890; -.
DR   eggNOG; ENOG502RYW6; Eukaryota.
DR   GeneTree; ENSGT00640000091574; -.
DR   HOGENOM; CLU_133874_0_0_1; -.
DR   InParanoid; Q9D3P9; -.
DR   OMA; WGLCSDS; -.
DR   OrthoDB; 1378763at2759; -.
DR   PhylomeDB; Q9D3P9; -.
DR   TreeFam; TF330765; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 67405; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Nts; mouse.
DR   PRO; PR:Q9D3P9; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9D3P9; protein.
DR   Bgee; ENSMUSG00000019890; Expressed in ileum and 133 other tissues.
DR   Genevisible; Q9D3P9; MM.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; TAS:MGI.
DR   GO; GO:0071855; F:neuropeptide receptor binding; ISO:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR   GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR   GO; GO:0008542; P:visual learning; ISO:MGI.
DR   InterPro; IPR008055; NeurotensiN.
DR   PANTHER; PTHR15356; PTHR15356; 1.
DR   Pfam; PF07421; Pro-NT_NN; 1.
DR   PRINTS; PR01668; NEUROTENSIN.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Reference proteome; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..147
FT                   /note="Large neuromedin N"
FT                   /id="PRO_0000019526"
FT   PEPTIDE         142..147
FT                   /note="Neuromedin N"
FT                   /id="PRO_0000019527"
FT   PEPTIDE         150..162
FT                   /note="Neurotensin"
FT                   /id="PRO_0000019528"
FT   PEPTIDE         165..169
FT                   /note="Tail peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019529"
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;  19608 MW;  D153319F5F0925DC CRC64;
     MRGMNLQLVC LTLLAFSSWS LCSDSEEDVR ALEADLLTNM HTSKISKASP PSWKMTLLNV
     CSLINNVNSP AEEAGDMHDD DLVGKRKLPL VLDGFSLEAM LTIFQLQKIC RSRAFQHWEI
     IQEDILDNVN DKNEKEEVIK RKIPYILKRQ LYENKPRRPY ILKRGSYYY
 
 
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