SPXN_BOVIN
ID SPXN_BOVIN Reviewed; 116 AA.
AC Q0VC44;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 AltName: Full=NPQ 53-70;
DE Flags: Precursor;
GN Name=SPX;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC Intraperitoneal administration of the peptide induces a reduction in
CC food consumption and body weight. Inhibits long chain fatty acid uptake
CC into adipocytes (By similarity). {ECO:0000250}.
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:0000250}. Secreted, extracellular
CC space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent
CC pathway into the extracellular medium largely as a full-length protein
CC without the signal peptide, and not as a hydrolyzed and amidated
CC peptide. Localized extracellularly surrounding the villous
CC trophoblastic cells. Detected in the serum (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the spexin family. {ECO:0000305}.
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DR EMBL; BC120360; AAI20361.1; -; mRNA.
DR RefSeq; NP_001068875.1; NM_001075407.1.
DR AlphaFoldDB; Q0VC44; -.
DR STRING; 9913.ENSBTAP00000000491; -.
DR PaxDb; Q0VC44; -.
DR Ensembl; ENSBTAT00000070012; ENSBTAP00000065237; ENSBTAG00000053951.
DR GeneID; 509493; -.
DR KEGG; bta:509493; -.
DR CTD; 80763; -.
DR VEuPathDB; HostDB:ENSBTAG00000053951; -.
DR VGNC; VGNC:35262; SPX.
DR eggNOG; ENOG502SAD1; Eukaryota.
DR GeneTree; ENSGT00390000012501; -.
DR HOGENOM; CLU_169090_0_0_1; -.
DR InParanoid; Q0VC44; -.
DR OMA; LETRSHN; -.
DR OrthoDB; 1579616at2759; -.
DR TreeFam; TF333402; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000053951; Expressed in infraspinatus muscle and 102 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0032099; P:negative regulation of appetite; ISS: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 3: Inferred from homology;
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_0000430210"
FT PROPEP 27..35
FT /evidence="ECO:0000250"
FT /id="PRO_0000363213"
FT PEPTIDE 36..49
FT /note="Spexin-1"
FT /id="PRO_0000363214"
FT PROPEP 50..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000363215"
FT PEPTIDE 53..70
FT /note="Spexin-2"
FT /id="PRO_0000430211"
FT PROPEP 74..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000430212"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
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; 13390 MW; A2FFFA79E5A959EE CRC64;
MKGFKSLVVM TLTLFLVFSF MGNCNSAPQR LFERRNWTPQ AMLYLKGAQG RRFLSDQSRR
KDLSDRPPLE RRSPNSQQLT LPEAAAVLLA FLQKPQEAGD ENLDQTRFLE DSLLNW
