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NMB_PIG
ID   NMB_PIG                 Reviewed;         121 AA.
AC   P01297; A0A4X1UK00;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Neuromedin-B;
DE   Contains:
DE     RecName: Full=Neuromedin-B-32;
DE   Contains:
DE     RecName: Full=Neuromedin-B-30;
DE   Contains:
DE     RecName: Full=Neuromedin-B;
DE   Flags: Precursor;
GN   Name=NMB;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000312|Proteomes:UP000314985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hannum G.I., Koren S., Schroeder S.G., Chin S.C., Nonneman D.J.,
RA   Becker S.A., Rosen B.D., Bickhart D.M., Putnam N.H., Green R.E.,
RA   Tuggle C.K., Liu H., Rohrer G.A., Warr A., Hall R., Kim K., Hume D.A.,
RA   Talbot R., Chow W., Howe K., Schwartz A.S., Watson M., Archibald A.L.,
RA   Phillippy A.M., Smith T.P.L.;
RT   "USMARCv1.0.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-56.
RX   PubMed=4026853; DOI=10.1016/0006-291x(85)90471-1;
RA   Minamino N., Sudoh T., Kangawa K., Matsuo H.;
RT   "Neuromedin B-32 and B-30: two 'big' neuromedin B identified in porcine
RT   brain and spinal cord.";
RL   Biochem. Biophys. Res. Commun. 130:685-691(1985).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-56.
RA   Minamino N., Kangawa K., Matsuo H.;
RT   "Neuromedin B and neuromedin C: two mammalian bombesin-like peptides
RT   identified in pig spinal cord and brain.";
RL   Regul. Pept. 19:127-127(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 47-56, FUNCTION, AND AMIDATION AT MET-56.
RX   PubMed=6882442; DOI=10.1016/0006-291x(83)90814-8;
RA   Minamino N., Kangawa K., Matsuo H.;
RT   "Neuromedin B: a novel bombesin-like peptide identified in porcine spinal
RT   cord.";
RL   Biochem. Biophys. Res. Commun. 114:541-548(1983).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=27010315; DOI=10.1371/journal.pone.0151871;
RA   Ma Z., Su J., Guo T., Jin M., Li X., Lei Z., Hou Y., Li X., Jia C.,
RA   Zhang Z., Ahmed E.;
RT   "Neuromedin B and Its Receptor: Gene Cloning, Tissue Distribution and
RT   Expression Levels of the Reproductive Axis in Pigs.";
RL   PLoS ONE 11:e0151871-e0151871(2016).
RN   [6]
RP   FUNCTION.
RX   PubMed=29632025; DOI=10.1530/jme-17-0242;
RA   Ma Z., Zhang Y., Su J., Yang S., Qiao W., Li X., Lei Z., Cheng L., An N.,
RA   Wang W., Feng Y., Zhang J.;
RT   "Effects of neuromedin B on steroidogenesis, cell proliferation and
RT   apoptosis in porcine Leydig cells.";
RL   J. Mol. Endocrinol. 61:13-23(2018).
CC   -!- FUNCTION: Stimulates smooth muscle contraction (PubMed:6882442).
CC       Induces sighing by acting directly on the pre-Botzinger complex, a
CC       cluster of several thousand neurons in the ventrolateral medulla
CC       responsible for inspiration during respiratory activity (By
CC       similarity). Contributes to the induction of sneezing following
CC       exposure to chemical irritants or allergens which causes release of NMB
CC       by nasal sensory neurons and activation of NMBR-expressing neurons in
CC       the sneeze-evoking region of the brainstem (By similarity). These in
CC       turn activate neurons of the caudal ventral respiratory group, giving
CC       rise to the sneezing response (By similarity). Contributes to induction
CC       of acute itch, possibly through activation of the NMBR receptor on
CC       dorsal root ganglion neurons (By similarity). Increases expression of
CC       NMBR and steroidogenic mediators STAR, CYP11A1 and HSD3B1 in Leydig
CC       cells, induces secretion of testosterone by Leydig cells and also
CC       promotes Leydig cell proliferation (PubMed:29632025). Plays a role in
CC       the innate immune response to influenza A virus infection by enhancing
CC       interferon alpha expression and reducing expression of IL6 (By
CC       similarity). Plays a role in CSF1-induced proliferation of osteoclast
CC       precursors by contributing to positive regulation of the expression of
CC       the CSF1 receptor CSF1R (By similarity). {ECO:0000250|UniProtKB:Q9CR53,
CC       ECO:0000269|PubMed:29632025, ECO:0000269|PubMed:6882442}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9CR53}. Cell
CC       projection, neuron projection {ECO:0000250|UniProtKB:Q9CR53}. Note=In
CC       neurons of the retrotrapezoid nucleus//parafacial respiratory group,
CC       expressed on neuron projections which project into the pre-Botzinger
CC       complex. {ECO:0000250|UniProtKB:Q9CR53}.
CC   -!- TISSUE SPECIFICITY: Higher expression in the central nervous system
CC       (CNS) than in peripheral tissues. Highest levels are found in the
CC       olfactory bulb. Relatively high levels in the CNS (including the
CC       cerebral cortex, cerebellum, spinal cord, medulla oblongata, midbrain,
CC       hypothalamus, hippocampus, and hypophysis) and in peripheral tissues
CC       such as the pancreas, adrenal gland, testis, ovary and cecum. Moderate
CC       levels are found in the rectum, heart and pons with low expression
CC       levels detected in the bone marrow and duodenum. Other tissues show no
CC       or low levels of expression. {ECO:0000269|PubMed:27010315}.
CC   -!- DEVELOPMENTAL STAGE: During the sow estrus cycle, highest levels are
CC       found in the hypothalamus during proestrus, decrease during estrus and
CC       metestrus and increase again during diestrus. In the pituitary gland,
CC       levels decrease from proestrus to estrus, increase at metestrus and
CC       decrease again at diestrus. In the ovary, expression peaks at
CC       proestrus, decreases slightly at estrus, decreases significantly at
CC       metestrus and increases at diestrus. During boar postnatal development,
CC       expression peaks in the hypothalamus at day 60 and decreases
CC       thereafter. In the pituitary gland, expression peaks at day 30 and
CC       decreases thereafter. In the testis, expression peaks at day 3 with
CC       lowest levels at day 60 and expression then gradually increases from
CC       day 60 to day 120. {ECO:0000269|PubMed:27010315}.
CC   -!- SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family.
CC       {ECO:0000305}.
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DR   PIR; B60301; BSPGNB.
DR   RefSeq; NP_001116617.1; NM_001123145.1.
DR   AlphaFoldDB; P01297; -.
DR   SMR; P01297; -.
DR   STRING; 9823.ENSSSCP00000027260; -.
DR   PaxDb; P01297; -.
DR   Ensembl; ENSSSCT00025088850; ENSSSCP00025038837; ENSSSCG00025064766.
DR   Ensembl; ENSSSCT00065015100; ENSSSCP00065006159; ENSSSCG00065011355.
DR   Ensembl; ENSSSCT00070034629; ENSSSCP00070028926; ENSSSCG00070017548.
DR   GeneID; 100141313; -.
DR   KEGG; ssc:100141313; -.
DR   CTD; 4828; -.
DR   eggNOG; ENOG502S66V; Eukaryota.
DR   HOGENOM; CLU_208788_0_0_1; -.
DR   InParanoid; P01297; -.
DR   OMA; NTAEMIP; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 7.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0031710; F:neuromedin B receptor binding; IBA:GO_Central.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR   GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR   GO; GO:0160024; P:Leydig cell proliferation; IDA:UniProtKB.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   GO; GO:0046887; P:positive regulation of hormone secretion; IBA:GO_Central.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR   GO; GO:0090290; P:positive regulation of osteoclast proliferation; ISS:UniProtKB.
DR   GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; ISS:UniProtKB.
DR   GO; GO:2000845; P:positive regulation of testosterone secretion; IDA:UniProtKB.
DR   GO; GO:0160025; P:sensory perception of itch; ISS:UniProtKB.
DR   GO; GO:0160023; P:sneeze reflex; ISS:UniProtKB.
DR   InterPro; IPR000874; Bombesin.
DR   PANTHER; PTHR16866; PTHR16866; 1.
DR   Pfam; PF02044; Bombesin; 1.
DR   PROSITE; PS00257; BOMBESIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cell projection; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Immunity; Innate immunity; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:4026853, ECO:0000269|Ref.3"
FT   PEPTIDE         25..56
FT                   /note="Neuromedin-B-32"
FT                   /evidence="ECO:0000269|PubMed:4026853, ECO:0000269|Ref.3"
FT                   /id="PRO_0000045912"
FT   PEPTIDE         27..56
FT                   /note="Neuromedin-B-30"
FT                   /evidence="ECO:0000269|PubMed:4026853"
FT                   /id="PRO_0000262471"
FT   PEPTIDE         47..56
FT                   /note="Neuromedin-B"
FT                   /evidence="ECO:0000269|PubMed:6882442"
FT                   /id="PRO_0000003023"
FT   PROPEP          60..121
FT                   /evidence="ECO:0000269|PubMed:4026853,
FT                   ECO:0000269|PubMed:6882442, ECO:0000269|Ref.3"
FT                   /id="PRO_0000455630"
FT   MOD_RES         56
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:6882442"
SQ   SEQUENCE   121 AA;  13381 MW;  002616317CE14EC4 CRC64;
     MTLRARGARL LGGLLFFTLL AAGAAPLSWD LPEPRSRAGK IRVHPRGNLW ATGHFMGKKS
     LEPPNPSLLG TTHHISLRDQ RLQLSHDLLR ILLQKKALGL SLSGPASHTP YRRLLVQTLE
     K
 
 
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