SPXN_CARAU
ID SPXN_CARAU Reviewed; 102 AA.
AC I7C2V3; I3RSB9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Spexin prohormone 1 {ECO:0000305};
DE AltName: Full=Spexin hormone;
DE Contains:
DE RecName: Full=Spexin-1;
DE Flags: Precursor;
GN Name=spx;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 36-48,
RP FUNCTION (SPEXIN-1), AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=23715729; DOI=10.1152/ajpendo.00141.2013;
RA Wong M.K., Sze K.H., Chen T., Cho C.K., Law H.C., Chu I.K., Wong A.O.;
RT "Goldfish spexin: solution structure and novel function as a satiety factor
RT in feeding control.";
RL Am. J. Physiol. 305:E348-E366(2013).
RN [2]
RP FUNCTION (SPEXIN-1), INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23623870; DOI=10.1016/j.mce.2013.04.008;
RA Liu Y., Li S., Qi X., Zhou W., Liu X., Lin H., Zhang Y., Cheng C.H.;
RT "A novel neuropeptide in suppressing luteinizing hormone release in
RT goldfish, Carassius auratus.";
RL Mol. Cell. Endocrinol. 374:65-72(2013).
CC -!- FUNCTION: Plays a role in the regulation of food intake and body weight
CC and in reproduction. May also play a role as a central modulator of
CC cardiovascular and renal function and nociception (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: [Spexin-1]: Brain administration of the peptide inhibits food
CC consumption. May function as a satiety factor for feeding control.
CC Involved in the negative regulation of the reproductive axis by
CC inhibiting luteinizing hormone secretion from pituitary cells
CC (PubMed:23715729, PubMed:23623870). {ECO:0000269|PubMed:23623870,
CC ECO:0000269|PubMed:23715729}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular
CC space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the anterior hypothalamus,
CC ventromedial thalamic nucleus and medial longitudinal fasciculus of the
CC brain (at protein level). Widely expressed. Expressed predominantly in
CC the spleen, kidney, liver and testis. Expressed in olfactory bulb,
CC pituitary, telencephalon, diencephalons, spinal cord, optic tectum,
CC cerebellum and hypothalamus of the brain. {ECO:0000269|PubMed:23623870,
CC ECO:0000269|PubMed:23715729}.
CC -!- INDUCTION: Up-regulated during female seasonal sexual maturation and
CC after ovariectomy. Up-regulated by food intake in brain areas involved
CC in appetit control. {ECO:0000269|PubMed:23623870}.
CC -!- MISCELLANEOUS: Amidated and nonamidated form of Spexin-1 had similar
CC effects on food intake/feeding behaviors.
CC -!- SIMILARITY: Belongs to the spexin family. {ECO:0000305}.
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DR EMBL; JX035990; AFO59751.1; -; Genomic_DNA.
DR EMBL; JQ894857; AFK29204.1; -; mRNA.
DR AlphaFoldDB; I7C2V3; -.
DR Ensembl; ENSCART00000049946; ENSCARP00000047862; ENSCARG00000020580.
DR Proteomes; UP000515129; Genome assembly.
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: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 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..102
FT /note="Spexin prohormone 1"
FT /id="PRO_0000430228"
FT PROPEP 27..35
FT /evidence="ECO:0000269|PubMed:23715729"
FT /id="PRO_0000430229"
FT PEPTIDE 36..49
FT /note="Spexin-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000430230"
FT PROPEP 50..102
FT /evidence="ECO:0000250"
FT /id="PRO_0000430231"
FT SITE 35..36
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 102 AA; 11580 MW; 787E75785028DFD5 CRC64;
MKDLRTLAAY ALALLLLATF VSYSRSAPMG SFQRRNWTPQ AMLYLKGTQG RRFVSEDRNE
GDLYDTIRLE SQSQNTENLS ISKAAAFLLN VLQQARDEGE PY