SPXN_MOUSE
ID SPXN_MOUSE Reviewed; 116 AA.
AC D3Z752;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Spexin;
DE AltName: Full=NPQ;
DE AltName: Full=Neuropeptide Q;
DE AltName: Full=Spexin hormone;
DE Contains:
DE RecName: Full=Spexin-1;
DE Contains:
DE RecName: Full=Spexin-2;
DE Flags: Precursor;
GN Name=Spx;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION (SPEXIN-1), SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24550067; DOI=10.1002/oby.20725;
RA Walewski J.L., Ge F., Lobdell H. IV, Levin N., Schwartz G.J.,
RA Vasselli J.R., Pomp A., Dakin G., Berk P.D.;
RT "Spexin is a novel human peptide that reduces adipocyte uptake of long
RT chain fatty acids and causes weight loss in rodents with diet-induced
RT obesity.";
RL Obesity 22:1643-1652(2014).
CC -!- FUNCTION: Plays a role as a central modulator of cardiovascular and
CC renal function and nociception. Also plays a role in energy metabolism
CC and storage. Inhibits adrenocortical cell proliferation with minor
CC stimulation on corticosteroid release (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Spexin-1]: Acts as a ligand for galanin receptors GALR2 and
CC GALR3. Intracerebroventricular administration of the peptide induces an
CC increase in arterial blood pressure, a decrease in both heart rate and
CC renal excretion and delayed natriuresis. Intraventricular
CC administration of the peptide induces antinociceptive activity. Also
CC induces contraction of muscarinic-like stomach smooth muscles (By
CC similarity). Intraperitoneal administration of the peptide induces a
CC reduction in food consumption and body weight. Inhibits long chain
CC fatty acid uptake into adipocytes (PubMed:24550067). {ECO:0000250,
CC ECO:0000269|PubMed:24550067}.
CC -!- FUNCTION: [Spexin-2]: Intracerebroventricular administration of the
CC peptide induces a decrease in heart rate, but no change in arterial
CC pressure, and an increase in urine flow rate. Intraventricular
CC administration of the peptide induces antinociceptive activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24550067}. Secreted,
CC extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory
CC vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-
CC dependent pathway into the extracellular medium largely as a full-
CC length protein without the signal peptide, and not as a hydrolyzed and
CC amidated peptide. Localized extracellularly surrounding the villous
CC trophoblastic cells (By similarity). Detected in the serum.
CC {ECO:0000250}.
CC -!- INDUCTION: Down-regulated in omental and subcutaneous fat of obese
CC animals. {ECO:0000269|PubMed:24550067}.
CC -!- SIMILARITY: Belongs to the spexin family. {ECO:0000305}.
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DR EMBL; AC142413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS90134.1; -.
DR RefSeq; XP_006507032.1; XM_006506969.3.
DR AlphaFoldDB; D3Z752; -.
DR SMR; D3Z752; -.
DR STRING; 10090.ENSMUSP00000085597; -.
DR PaxDb; D3Z752; -.
DR PRIDE; D3Z752; -.
DR Antibodypedia; 2438; 24 antibodies from 10 providers.
DR Ensembl; ENSMUST00000211094; ENSMUSP00000147302; ENSMUSG00000071112.
DR UCSC; uc009eph.2; mouse.
DR MGI; MGI:2442262; Spx.
DR VEuPathDB; HostDB:ENSMUSG00000071112; -.
DR eggNOG; ENOG502SAD1; Eukaryota.
DR GeneTree; ENSGT00390000012501; -.
DR HOGENOM; CLU_169090_0_0_1; -.
DR InParanoid; D3Z752; -.
DR PhylomeDB; D3Z752; -.
DR TreeFam; TF333402; -.
DR BioGRID-ORCS; 319552; 1 hit in 33 CRISPR screens.
DR PRO; PR:D3Z752; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; D3Z752; protein.
DR Bgee; ENSMUSG00000071112; Expressed in habenula and 94 other tissues.
DR ExpressionAtlas; D3Z752; baseline and differential.
DR Genevisible; D3Z752; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031045; C:dense core granule; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0031765; F:type 2 galanin receptor binding; ISS:UniProtKB.
DR GO; GO:0031766; F:type 3 galanin receptor binding; ISS:UniProtKB.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:UniProtKB.
DR GO; GO:0032099; P:negative regulation of appetite; IDA:UniProtKB.
DR GO; GO:0010459; P:negative regulation of heart rate; ISS:UniProtKB.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISS:UniProtKB.
DR GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR InterPro; IPR028126; Spexin.
DR PANTHER; PTHR28590; PTHR28590; 1.
DR Pfam; PF15171; Spexin; 1.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..116
FT /note="Spexin"
FT /id="PRO_0000430216"
FT PROPEP 27..35
FT /evidence="ECO:0000250"
FT /id="PRO_0000430217"
FT PEPTIDE 36..49
FT /note="Spexin-1"
FT /id="PRO_0000430218"
FT PROPEP 50..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000430219"
FT PEPTIDE 53..70
FT /note="Spexin-2"
FT /id="PRO_0000430220"
FT PROPEP 74..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000430221"
FT REGION 52..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 35..36
FT /note="Cleavage; by prohormone convertase 2"
FT /evidence="ECO:0000250"
FT SITE 52..53
FT /note="Cleavage; by prohormone convertase 2"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage; by prohormone convertase 2"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Glutamine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 13004 MW; 2D0D985038A8FE7B CRC64;
MKGPSVLAVT AVVLLLVLSA LENSSGAPQR LSEKRNWTPQ AMLYLKGAQG RRFLSDQSRR
KELADRPPPE RRNPDLELLT LPEAAALFLA SLEKSQKDEG GNFDKSELLE DRLFNW
