ID   PROK2_RAT               Reviewed;         107 AA.
AC   Q8R413;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Prokineticin-2;
DE            Short=PK2;
DE   Flags: Precursor;
GN   Name=Prok2; Synonyms=Bv8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=12054613; DOI=10.1016/s0006-291x(02)00239-5;
RA   Masuda Y., Takatsu Y., Terao Y., Kumano S., Ishibashi Y., Suenaga M.,
RA   Abe M., Fukusumi S., Watanabe T., Shintani Y., Yamada T., Hinuma S.,
RA   Inatomi N., Ohtaki T., Onda H., Fujino M.;
RT   "Isolation and identification of EG-VEGF/prokineticins as cognate ligands
RT   for two orphan G-protein-coupled receptors.";
RL   Biochem. Biophys. Res. Commun. 293:396-402(2002).
RN   [2]
RP   EFFECT ON CIRCADIAN LOCOMOTOR ACTIVITY.
RX   PubMed=12024206; DOI=10.1038/417405a;
RA   Cheng M.Y., Bullock C.M., Li C., Lee A.G., Bermak J.C., Belluzzi J.,
RA   Weaver D.R., Leslie F.M., Zhou Q.-Y.;
RT   "Prokineticin 2 transmits the behavioural circadian rhythm of the
RT   suprachiasmatic nucleus.";
RL   Nature 417:405-410(2002).
CC   -!- FUNCTION: May function as an output molecule from the suprachiasmatic
CC       nucleus (SCN) that transmits behavioral circadian rhythm. May also
CC       function locally within the SCN to synchronize output. Potently
CC       contracts gastrointestinal (GI) smooth muscle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in testis and at lower
CC       levels in brain, lung, ovary, spleen, thymus and uterus.
CC   -!- INDUCTION: Activated by CLOCK and BMAL1 heterodimers and light;
CC       inhibited by period genes (PER1, PER2 and PER3) and cryptochrome genes
CC       (CRY1 and CRY2). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AVIT (prokineticin) family. {ECO:0000305}.
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DR   EMBL; AY089984; AAM09105.1; -; mRNA.
DR   RefSeq; NP_620207.1; NM_138852.1.
DR   AlphaFoldDB; Q8R413; -.
DR   SMR; Q8R413; -.
DR   ChEMBL; CHEMBL1949485; -.
DR   Ensembl; ENSRNOT00000015075; ENSRNOP00000015075; ENSRNOG00000010898.
DR   GeneID; 192206; -.
DR   KEGG; rno:192206; -.
DR   UCSC; RGD:620280; rat.
DR   CTD; 60675; -.
DR   RGD; 620280; Prok2.
DR   GeneTree; ENSGT00940000162026; -.
DR   HOGENOM; CLU_143202_1_0_1; -.
DR   InParanoid; Q8R413; -.
DR   OrthoDB; 1517288at2759; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   PRO; PR:Q8R413; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000010898; Expressed in testis and 7 other tissues.
DR   ExpressionAtlas; Q8R413; baseline and differential.
DR   Genevisible; Q8R413; RN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IDA:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; ISO:RGD.
DR   GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR   GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR   InterPro; IPR009523; Prokineticin.
DR   InterPro; IPR023569; Prokineticin_domain.
DR   PANTHER; PTHR18821; PTHR18821; 1.
DR   Pfam; PF06607; Prokineticin; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Disulfide bond; Neuropeptide; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..107
FT                   /note="Prokineticin-2"
FT                   /id="PRO_0000025811"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..103
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  11594 MW;  BDFF316CDCB5FED0 CRC64;
     MEDPRCAPLL LLLLLPLLLT PPAGDAAVIT GACDKDSQCG GGMCCAVSIW VKSIRICTPM
     GQVGDSCHPL TRKVPFWGRR MHHTCPCLPG LACLRTSFNR FICLARK