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Protein

Prokineticin-2

Gene

Prok2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle (By similarity).By similarity

GO - Molecular functioni

  • G-protein coupled receptor binding Source: DFLAT

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • chemotaxis Source: UniProtKB
  • circadian rhythm Source: MGI
  • coronary vasculature development Source: DFLAT
  • epicardium-derived cardiac endothelial cell differentiation Source: DFLAT
  • epicardium-derived cardiac vascular smooth muscle cell differentiation Source: DFLAT
  • negative regulation of apoptotic process Source: UniProtKB
  • neuropeptide signaling pathway Source: UniProtKB-KW
  • positive regulation of smooth muscle contraction Source: UniProtKB
  • spermatogenesis Source: UniProtKB
  • vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Neuropeptide

Keywords - Biological processi

Biological rhythms

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_347934. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Prokineticin-2
Short name:
PK2
Alternative name(s):
Protein Bv8 homolog
Gene namesi
Name:Prok2
Synonyms:Bv8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1354178. Prok2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 128102Prokineticin-2PRO_0000025810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 45By similarity
Disulfide bondi39 ↔ 57By similarity
Disulfide bondi44 ↔ 106By similarity
Disulfide bondi67 ↔ 114By similarity
Disulfide bondi108 ↔ 124By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ9QXU7.

Expressioni

Tissue specificityi

Expressed in the SCN and among a few other discrete brain areas, including the islands of Calleja, media l preoptic area of the hypothalamus and the shell of the nucleus accumbens. Highly expressed in testis. In the SCN, expression subjected to high amplitude of circadian oscillation.

Developmental stagei

Expressed in mid-late pachytene spermatocytes at the stages VII, VIII and IX of the semiferous epithelial cycle.

Inductioni

Activated by CLOCK and BMAL1 heterodimers and light; inhibited by period genes (PER1, PER2 and PER3) and cryptochrome genes (CRY1 and CRY2).

Gene expression databases

BgeeiQ9QXU7.
CleanExiMM_PROK2.
ExpressionAtlasiQ9QXU7. baseline and differential.
GenevisibleiQ9QXU7. MM.

Interactioni

Protein-protein interaction databases

BioGridi206046. 1 interaction.
STRINGi10090.ENSMUSP00000032152.

Structurei

3D structure databases

ProteinModelPortaliQ9QXU7.
SMRiQ9QXU7. Positions 27-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AVIT (prokineticin) family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39081.
GeneTreeiENSGT00390000014799.
HOGENOMiHOG000004848.
HOVERGENiHBG031845.
InParanoidiQ9QXU7.
OMAiPLTRKNH.
OrthoDBiEOG7SJD78.
PhylomeDBiQ9QXU7.
TreeFamiTF332732.

Family and domain databases

InterProiIPR009523. Prokineticin.
IPR023569. Prokineticin_domain.
[Graphical view]
PANTHERiPTHR18821. PTHR18821. 1 hit.
PfamiPF06607. Prokineticin. 1 hit.
[Graphical view]
ProDomiPD059788. Prokineticin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QXU7-1) [UniParc]FASTAAdd to basket

Also known as: Bv8-a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGDPRCAPLL LLLLLPLLFT PPAGDAAVIT GACDKDSQCG GGMCCAVSIW
60 70 80 90 100
VKSIRICTPM GQVGDSCHPL TRKSHVANGR QERRRAKRRK RKKEVPFWGR
110 120
RMHHTCPCLP GLACLRTSFN RFICLARK
Length:128
Mass (Da):14,185
Last modified:May 1, 2000 - v1
Checksum:i5F08BA177FDDB58C
GO
Isoform 2 (identifier: Q9QXU7-2) [UniParc]FASTAAdd to basket

Also known as: Bv8-b

The sequence of this isoform differs from the canonical sequence as follows:
     74-94: Missing.

Show »
Length:107
Mass (Da):11,556
Checksum:i8FB79BE4D4357C70
GO
Isoform 3 (identifier: Q9QXU7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-128: SHVANGRQERRRAKRRKRKKEVPFWGRRMHHTCPCLPGLACLRTSFNRFICLARK → VSVCTGILGVPSH

Show »
Length:86
Mass (Da):8,836
Checksum:i28EACBC5E6F7706F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 12855SHVAN…CLARK → VSVCTGILGVPSH in isoform 3. 1 PublicationVSP_005221Add
BLAST
Alternative sequencei74 – 9421Missing in isoform 2. 4 PublicationsVSP_005220Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182064 mRNA. Translation: AAF15259.1.
AF182065 mRNA. Translation: AAF15260.1.
AF182066 mRNA. Translation: AAF15261.1.
AF182068, AF182067 Genomic DNA. Translation: AAG09439.1.
AF487280 mRNA. Translation: AAM49572.1.
AK015462 mRNA. Translation: BAB29857.1.
BC144863 mRNA. Translation: AAI44864.1.
CCDSiCCDS20388.1. [Q9QXU7-2]
CCDS20389.1. [Q9QXU7-1]
RefSeqiNP_001032628.1. NM_001037539.2. [Q9QXU7-2]
NP_056583.1. NM_015768.2. [Q9QXU7-1]
UniGeneiMm.87365.

Genome annotation databases

EnsembliENSMUST00000032152; ENSMUSP00000032152; ENSMUSG00000030069. [Q9QXU7-1]
ENSMUST00000101120; ENSMUSP00000098678; ENSMUSG00000030069. [Q9QXU7-2]
GeneIDi50501.
KEGGimmu:50501.
UCSCiuc009dbt.1. mouse. [Q9QXU7-1]
uc009dbu.1. mouse. [Q9QXU7-2]
uc009dbv.1. mouse. [Q9QXU7-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182064 mRNA. Translation: AAF15259.1.
AF182065 mRNA. Translation: AAF15260.1.
AF182066 mRNA. Translation: AAF15261.1.
AF182068, AF182067 Genomic DNA. Translation: AAG09439.1.
AF487280 mRNA. Translation: AAM49572.1.
AK015462 mRNA. Translation: BAB29857.1.
BC144863 mRNA. Translation: AAI44864.1.
CCDSiCCDS20388.1. [Q9QXU7-2]
CCDS20389.1. [Q9QXU7-1]
RefSeqiNP_001032628.1. NM_001037539.2. [Q9QXU7-2]
NP_056583.1. NM_015768.2. [Q9QXU7-1]
UniGeneiMm.87365.

3D structure databases

ProteinModelPortaliQ9QXU7.
SMRiQ9QXU7. Positions 27-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206046. 1 interaction.
STRINGi10090.ENSMUSP00000032152.

Proteomic databases

PRIDEiQ9QXU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032152; ENSMUSP00000032152; ENSMUSG00000030069. [Q9QXU7-1]
ENSMUST00000101120; ENSMUSP00000098678; ENSMUSG00000030069. [Q9QXU7-2]
GeneIDi50501.
KEGGimmu:50501.
UCSCiuc009dbt.1. mouse. [Q9QXU7-1]
uc009dbu.1. mouse. [Q9QXU7-2]
uc009dbv.1. mouse. [Q9QXU7-3]

Organism-specific databases

CTDi60675.
MGIiMGI:1354178. Prok2.

Phylogenomic databases

eggNOGiNOG39081.
GeneTreeiENSGT00390000014799.
HOGENOMiHOG000004848.
HOVERGENiHBG031845.
InParanoidiQ9QXU7.
OMAiPLTRKNH.
OrthoDBiEOG7SJD78.
PhylomeDBiQ9QXU7.
TreeFamiTF332732.

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_347934. G alpha (q) signalling events.

Miscellaneous databases

NextBioi307502.
PROiQ9QXU7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXU7.
CleanExiMM_PROK2.
ExpressionAtlasiQ9QXU7. baseline and differential.
GenevisibleiQ9QXU7. MM.

Family and domain databases

InterProiIPR009523. Prokineticin.
IPR023569. Prokineticin_domain.
[Graphical view]
PANTHERiPTHR18821. PTHR18821. 1 hit.
PfamiPF06607. Prokineticin. 1 hit.
[Graphical view]
ProDomiPD059788. Prokineticin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mammalian homologues of frog Bv8 are mainly expressed in spermatocytes."
    Wechselberger C., Puglisi R., Lepperdinger G., Boitani C., Kreil G.
    FEBS Lett. 462:177-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: 129/Sv.
  2. "Murine Bv8 gene maps near a synteny breakpoint of mouse chromosome 6 and human 3p21."
    Jilek A., Engel E., Beier D., Lepperdinger G.
    Gene 256:189-195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: 129/SvJ.
  3. "Prokineticin 2 transmits the behavioural circadian rhythm of the suprachiasmatic nucleus."
    Cheng M.Y., Bullock C.M., Li C., Lee A.G., Bermak J.C., Belluzzi J., Weaver D.R., Leslie F.M., Zhou Q.-Y.
    Nature 417:405-410(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
    Strain: C57BL/6.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Testis.
  5. "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] (ISOFORM 2).
    Tissue: Testis.

Entry informationi

Entry nameiPROK2_MOUSE
AccessioniPrimary (citable) accession number: Q9QXU7
Secondary accession number(s): B7ZMX7, Q9QXU5, Q9QXU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.