ID   PROK2_MOUSE             Reviewed;         128 AA.
AC   Q9QXU7; B7ZMX7; Q9QXU5; Q9QXU6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Prokineticin-2;
DE            Short=PK2;
DE   AltName: Full=Protein Bv8 homolog;
DE   Flags: Precursor;
GN   Name=Prok2; Synonyms=Bv8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129/Sv;
RX   PubMed=10580115; DOI=10.1016/s0014-5793(99)01473-8;
RA   Wechselberger C., Puglisi R., Lepperdinger G., Boitani C., Kreil G.;
RT   "The mammalian homologues of frog Bv8 are mainly expressed in
RT   spermatocytes.";
RL   FEBS Lett. 462:177-181(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=129/SvJ;
RX   PubMed=11054548; DOI=10.1016/s0378-1119(00)00355-3;
RA   Jilek A., Engel E., Beier D., Lepperdinger G.;
RT   "Murine Bv8 gene maps near a synteny breakpoint of mouse chromosome 6 and
RT   human 3p21.";
RL   Gene 256:189-195(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC   STRAIN=C57BL/6J;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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, ECO:0000269|PubMed:12024206}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Bv8-a;
CC         IsoId=Q9QXU7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Bv8-b;
CC         IsoId=Q9QXU7-2; Sequence=VSP_005220;
CC       Name=3;
CC         IsoId=Q9QXU7-3; Sequence=VSP_005221;
CC   -!- TISSUE SPECIFICITY: Expressed in the SCN and among a few other discrete
CC       brain areas, including the islands of Calleja, media l preoptic area of
CC       the hypothalamus and the shell of the nucleus accumbens. Highly
CC       expressed in testis. In the SCN, expression subjected to high amplitude
CC       of circadian oscillation.
CC   -!- DEVELOPMENTAL STAGE: Expressed in mid-late pachytene spermatocytes at
CC       the stages VII, VIII and IX of the semiferous epithelial cycle.
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).
CC   -!- SIMILARITY: Belongs to the AVIT (prokineticin) family. {ECO:0000305}.
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DR   EMBL; AF182064; AAF15259.1; -; mRNA.
DR   EMBL; AF182065; AAF15260.1; -; mRNA.
DR   EMBL; AF182066; AAF15261.1; -; mRNA.
DR   EMBL; AF182068; AAG09439.1; -; Genomic_DNA.
DR   EMBL; AF182067; AAG09439.1; JOINED; Genomic_DNA.
DR   EMBL; AF487280; AAM49572.1; -; mRNA.
DR   EMBL; AK015462; BAB29857.1; -; mRNA.
DR   EMBL; BC144863; AAI44864.1; -; mRNA.
DR   CCDS; CCDS20388.1; -. [Q9QXU7-2]
DR   CCDS; CCDS20389.1; -. [Q9QXU7-1]
DR   RefSeq; NP_001032628.1; NM_001037539.2. [Q9QXU7-2]
DR   RefSeq; NP_056583.1; NM_015768.2. [Q9QXU7-1]
DR   AlphaFoldDB; Q9QXU7; -.
DR   SMR; Q9QXU7; -.
DR   BioGRID; 206046; 1.
DR   STRING; 10090.ENSMUSP00000032152; -.
DR   iPTMnet; Q9QXU7; -.
DR   PaxDb; 10090-ENSMUSP00000032152; -.
DR   ProteomicsDB; 291879; -. [Q9QXU7-1]
DR   ProteomicsDB; 291880; -. [Q9QXU7-2]
DR   ProteomicsDB; 291881; -. [Q9QXU7-3]
DR   Antibodypedia; 31927; 232 antibodies from 28 providers.
DR   DNASU; 50501; -.
DR   Ensembl; ENSMUST00000032152.14; ENSMUSP00000032152.9; ENSMUSG00000030069.16. [Q9QXU7-1]
DR   Ensembl; ENSMUST00000101120.11; ENSMUSP00000098678.5; ENSMUSG00000030069.16. [Q9QXU7-2]
DR   Ensembl; ENSMUST00000203738.2; ENSMUSP00000144760.2; ENSMUSG00000030069.16. [Q9QXU7-3]
DR   GeneID; 50501; -.
DR   KEGG; mmu:50501; -.
DR   UCSC; uc009dbt.1; mouse. [Q9QXU7-1]
DR   UCSC; uc009dbu.1; mouse. [Q9QXU7-2]
DR   UCSC; uc009dbv.1; mouse. [Q9QXU7-3]
DR   AGR; MGI:1354178; -.
DR   CTD; 60675; -.
DR   MGI; MGI:1354178; Prok2.
DR   VEuPathDB; HostDB:ENSMUSG00000030069; -.
DR   eggNOG; ENOG502SU1D; Eukaryota.
DR   GeneTree; ENSGT00940000162026; -.
DR   HOGENOM; CLU_143202_1_0_1; -.
DR   InParanoid; Q9QXU7; -.
DR   OMA; NCHPLSH; -.
DR   OrthoDB; 3012714at2759; -.
DR   PhylomeDB; Q9QXU7; -.
DR   TreeFam; TF332732; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 50501; 4 hits in 73 CRISPR screens.
DR   PRO; PR:Q9QXU7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QXU7; Protein.
DR   Bgee; ENSMUSG00000030069; Expressed in spermatocyte and 29 other cell types or tissues.
DR   ExpressionAtlas; Q9QXU7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IDA:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; TAS:DFLAT.
DR   GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0003349; P:epicardium-derived cardiac endothelial cell differentiation; TAS:DFLAT.
DR   GO; GO:0060983; P:epicardium-derived cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR   Gene3D; 2.10.80.10; Lipase, subunit A; 1.
DR   InterPro; IPR009523; Prokineticin.
DR   InterPro; IPR023569; Prokineticin_domain.
DR   PANTHER; PTHR18821; PROKINETICIN; 1.
DR   PANTHER; PTHR18821:SF8; PROKINETICIN-2; 1.
DR   Pfam; PF06607; Prokineticin; 1.
DR   SUPFAM; SSF57190; Colipase-like; 2.
DR   Genevisible; Q9QXU7; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Biological rhythms; Disulfide bond; Neuropeptide;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..128
FT                   /note="Prokineticin-2"
FT                   /id="PRO_0000025810"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..124
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         74..128
FT                   /note="SHVANGRQERRRAKRRKRKKEVPFWGRRMHHTCPCLPGLACLRTSFNRFICL
FT                   ARK -> VSVCTGILGVPSH (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11054548"
FT                   /id="VSP_005221"
FT   VAR_SEQ         74..94
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10580115,
FT                   ECO:0000303|PubMed:11054548, ECO:0000303|PubMed:12024206,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005220"
SQ   SEQUENCE   128 AA;  14185 MW;  5F08BA177FDDB58C CRC64;
     MGDPRCAPLL LLLLLPLLFT PPAGDAAVIT GACDKDSQCG GGMCCAVSIW VKSIRICTPM
     GQVGDSCHPL TRKSHVANGR QERRRAKRRK RKKEVPFWGR RMHHTCPCLP GLACLRTSFN
     RFICLARK
//