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Q9BT56

- SPXN_HUMAN

UniProt

Q9BT56 - SPXN_HUMAN

Protein

Spexin

Gene

SPX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays a role as a central modulator of cardiovascular and renal function and nociception. Plays also a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release By similarity.By similarity
    Spexin-1: Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Also induces contraction of muscarinic-like stomach smooth muscles. Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes By similarity. Acts as a ligand for galanin receptors GALR2 and GALR3 (PubMed:17284679, PubMed:24517231).By similarity2 Publications
    Spexin-2: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei35 – 362Cleavage; by prohormone convertase 2
    Sitei52 – 532Cleavage; by prohormone convertase 2
    Sitei72 – 732Cleavage; by prohormone convertase 2

    GO - Molecular functioni

    1. neuropeptide hormone activity Source: UniProtKB
    2. type 2 galanin receptor binding Source: UniProtKB
    3. type 3 galanin receptor binding Source: UniProtKB

    GO - Biological processi

    1. long-chain fatty acid import Source: UniProtKB
    2. negative regulation of appetite Source: UniProtKB
    3. negative regulation of heart rate Source: UniProtKB
    4. negative regulation of renal sodium excretion Source: UniProtKB
    5. positive regulation of systemic arterial blood pressure Source: UniProtKB
    6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. regulation of sensory perception of pain Source: UniProtKB

    Keywords - Molecular functioni

    Hormone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spexin
    Alternative name(s):
    NPQ
    Neuropeptide Q
    Spexin hormone
    Cleaved into the following 2 chains:
    Alternative name(s):
    NPQ 53-70
    Gene namesi
    Name:SPX
    Synonyms:C12orf39
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:28139. SPX.

    Subcellular locationi

    Secreted. Secretedextracellular space. Cytoplasmic vesiclesecretory vesicle
    Note: Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide (PubMed:19193193 and PubMed:17284679). Localized extracellularly surrounding the villous trophoblastic cells. Detected in the serum.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485369.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 11690SpexinPRO_0000430213Add
    BLAST
    Propeptidei27 – 359PRO_0000363216
    Peptidei36 – 4914Spexin-1PRO_0000042159Add
    BLAST
    Propeptidei50 – 11667PRO_0000363217Add
    BLAST
    Peptidei53 – 7018Spexin-2PRO_0000430214Add
    BLAST
    Propeptidei74 – 11643PRO_0000430215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Glutamine amideCurated

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues

    Proteomic databases

    PaxDbiQ9BT56.
    PRIDEiQ9BT56.

    Expressioni

    Tissue specificityi

    Expressed in the type I glomic cells within the carotid body (at protein level). Expressed predominantly in pancreas, testis, kidney, brain and placenta. Expressed in submucosal layer of esophagus and stomach fundus.4 Publications

    Inductioni

    Down-regulated in omental and subcutaneous fat of obese subjects.1 Publication

    Gene expression databases

    ArrayExpressiQ9BT56.
    BgeeiQ9BT56.
    CleanExiHS_C12orf39.
    GenevestigatoriQ9BT56.

    Organism-specific databases

    HPAiHPA012890.

    Interactioni

    Protein-protein interaction databases

    BioGridi123297. 1 interaction.
    STRINGi9606.ENSP00000256969.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BT56.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG75104.
    HOGENOMiHOG000154403.
    HOVERGENiHBG095171.
    InParanoidiQ9BT56.
    OMAiWSAPQAH.
    OrthoDBiEOG741Z4Q.
    PhylomeDBiQ9BT56.
    TreeFamiTF333402.

    Family and domain databases

    InterProiIPR028126. Spexin.
    [Graphical view]
    PfamiPF15171. Spexin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BT56-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLRSLAAT TLALFLVFVF LGNSSCAPQR LLERRNWTPQ AMLYLKGAQG    50
    RRFISDQSRR KDLSDRPLPE RRSPNPQLLT IPEAATILLA SLQKSPEDEE 100
    KNFDQTRFLE DSLLNW 116
    Length:116
    Mass (Da):13,302
    Last modified:June 1, 2001 - v1
    Checksum:iCCBC3E7BD22E357E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027273 mRNA. Translation: BAG51298.1.
    AK075342 mRNA. Translation: BAG52117.1.
    CH471094 Genomic DNA. Translation: EAW96444.1.
    BC004336 mRNA. Translation: AAH04336.1.
    CCDSiCCDS31757.1.
    RefSeqiNP_085049.1. NM_030572.2.
    UniGeneiHs.130692.

    Genome annotation databases

    EnsembliENST00000256969; ENSP00000256969; ENSG00000134548.
    GeneIDi80763.
    KEGGihsa:80763.
    UCSCiuc001rfa.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027273 mRNA. Translation: BAG51298.1 .
    AK075342 mRNA. Translation: BAG52117.1 .
    CH471094 Genomic DNA. Translation: EAW96444.1 .
    BC004336 mRNA. Translation: AAH04336.1 .
    CCDSi CCDS31757.1.
    RefSeqi NP_085049.1. NM_030572.2.
    UniGenei Hs.130692.

    3D structure databases

    ProteinModelPortali Q9BT56.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123297. 1 interaction.
    STRINGi 9606.ENSP00000256969.

    Proteomic databases

    PaxDbi Q9BT56.
    PRIDEi Q9BT56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256969 ; ENSP00000256969 ; ENSG00000134548 .
    GeneIDi 80763.
    KEGGi hsa:80763.
    UCSCi uc001rfa.1. human.

    Organism-specific databases

    CTDi 80763.
    GeneCardsi GC12P021679.
    HGNCi HGNC:28139. SPX.
    HPAi HPA012890.
    neXtProti NX_Q9BT56.
    PharmGKBi PA143485369.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75104.
    HOGENOMi HOG000154403.
    HOVERGENi HBG095171.
    InParanoidi Q9BT56.
    OMAi WSAPQAH.
    OrthoDBi EOG741Z4Q.
    PhylomeDBi Q9BT56.
    TreeFami TF333402.

    Miscellaneous databases

    GenomeRNAii 80763.
    NextBioi 71141.

    Gene expression databases

    ArrayExpressi Q9BT56.
    Bgeei Q9BT56.
    CleanExi HS_C12orf39.
    Genevestigatori Q9BT56.

    Family and domain databases

    InterProi IPR028126. Spexin.
    [Graphical view ]
    Pfami PF15171. Spexin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    5. "Identification of novel peptide hormones in the human proteome by hidden Markov model screening."
      Mirabeau O., Perlas E., Severini C., Audero E., Gascuel O., Possenti R., Birney E., Rosenthal N., Gross C.
      Genome Res. 17:320-327(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (SPEXIN-1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "C12ORF39, a novel secreted prot ein with a typical amidation processing signal."
      Wan B., Wang X.R., Zhou Y.B., Zhang X., Huo K., Han Z.G.
      Biosci. Rep. 30:1-10(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "Spexin is expressed in the carotid body and is upregulated by postnatal hyperoxia exposure."
      Porzionato A., Rucinski M., Macchi V., Stecco C., Sarasin G., Sfriso M.M., Di Giulio C., Malendowicz L.K., De Caro R.
      Adv. Exp. Med. Biol. 758:207-213(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Peptides derived from the prohormone proNPQ/spexin are potent central modulators of cardiovascular and renal function and nociception."
      Toll L., Khroyan T.V., Sonmez K., Ozawa A., Lindberg I., McLaughlin J.P., Eans S.O., Shahien A.A., Kapusta D.R.
      FASEB J. 26:947-954(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING (SPEXIN-1 AND SPEXIN-2).
    9. "Coevolution of the spexin/galanin/kisspeptin family: Spexin activates galanin receptor type II and III."
      Kim D.K., Yun S., Son G.H., Hwang J.I., Park C.R., Kim J.I., Kim K., Vaudry H., Seong J.Y.
      Endocrinology 155:1864-1873(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (SPEXIN-1), PHYLOGENY.
    10. "Spexin is a novel human peptide that reduces adipocyte uptake of long chain fatty acids and causes weight loss in rodents with diet-induced obesity."
      Walewski J.L., Ge F., Lobdell H. IV, Levin N., Schwartz G.J., Vasselli J.R., Pomp A., Dakin G., Berk P.D.
      Obesity 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.

    Entry informationi

    Entry nameiSPXN_HUMAN
    AccessioniPrimary (citable) accession number: Q9BT56
    Secondary accession number(s): B3KND6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM

    External Data

    Dasty 3