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Protein

Prokineticin-1

Gene

PROK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis.5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiR-HSA-375276. Peptide ligand-binding receptors.
R-HSA-416476. G alpha (q) signalling events.
SIGNORiP58294.

Names & Taxonomyi

Protein namesi
Recommended name:
Prokineticin-1
Alternative name(s):
Endocrine-gland-derived vascular endothelial growth factor
Short name:
EG-VEGF
Mambakine
Gene namesi
Name:PROK1
ORF Names:UNQ600/PRO1186
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18454. PROK1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38539.

Polymorphism and mutation databases

BioMutaiPROK1.
DMDMi17380189.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 10586Prokineticin-1PRO_0000025807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 38By similarity
Disulfide bondi32 ↔ 50By similarity
Disulfide bondi37 ↔ 78By similarity
Disulfide bondi60 ↔ 86By similarity
Disulfide bondi80 ↔ 96By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP58294.
PRIDEiP58294.

PTM databases

iPTMnetiP58294.

Expressioni

Tissue specificityi

Localizes to glandular epithelium, stroma and vascular epithelial cells of first trimester decidua (at protein level). Up-regulated in first trimester decidua when compared with non-pregnant endometrium. Expressed in the steroidogenic glands, ovary, testis, adrenal and placenta.3 Publications

Developmental stagei

In adult testis, is strongly expressed only in Leydig cells. In testicular tumors, expressed specifically in Leydig cell tumors (at protein level). Expressed from 14 weeks until birth in fetal testis.

Gene expression databases

BgeeiP58294.
CleanExiHS_PROK1.
ExpressionAtlasiP58294. baseline and differential.
GenevisibleiP58294. HS.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9606.ENSP00000271331.

Structurei

3D structure databases

ProteinModelPortaliP58294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AVIT (prokineticin) family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IYYQ. Eukaryota.
ENOG4111YK9. LUCA.
GeneTreeiENSGT00390000014799.
HOGENOMiHOG000004848.
HOVERGENiHBG031845.
InParanoidiP58294.
OMAiRKRQHHT.
OrthoDBiEOG7SJD78.
PhylomeDBiP58294.
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]

Sequencei

Sequence statusi: Complete.

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

P58294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGATRVSIM LLLVTVSDCA VITGACERDV QCGAGTCCAI SLWLRGLRMC
60 70 80 90 100
TPLGREGEEC HPGSHKVPFF RKRKHHTCPC LPNLLCSRFP DGRYRCSMDL

KNINF
Length:105
Mass (Da):11,715
Last modified:September 26, 2001 - v1
Checksum:iC7E3FDE30EFB416A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671V → I.1 Publication
Corresponds to variant rs7514102 [ dbSNP | Ensembl ].
VAR_053610

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333024 mRNA. Translation: AAK49918.1.
AY029225 mRNA. Translation: AAK33111.1.
AY358683 mRNA. Translation: AAQ89046.1.
AL358215, AL390797 Genomic DNA. Translation: CAH74102.1.
AL390797, AL358215 Genomic DNA. Translation: CAH71489.1.
CH471122 Genomic DNA. Translation: EAW56449.1.
BC025399 mRNA. Translation: AAH25399.1.
CCDSiCCDS825.1.
RefSeqiNP_115790.1. NM_032414.2.
UniGeneiHs.514793.

Genome annotation databases

EnsembliENST00000271331; ENSP00000271331; ENSG00000143125.
GeneIDi84432.
KEGGihsa:84432.
UCSCiuc001dzs.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333024 mRNA. Translation: AAK49918.1.
AY029225 mRNA. Translation: AAK33111.1.
AY358683 mRNA. Translation: AAQ89046.1.
AL358215, AL390797 Genomic DNA. Translation: CAH74102.1.
AL390797, AL358215 Genomic DNA. Translation: CAH71489.1.
CH471122 Genomic DNA. Translation: EAW56449.1.
BC025399 mRNA. Translation: AAH25399.1.
CCDSiCCDS825.1.
RefSeqiNP_115790.1. NM_032414.2.
UniGeneiHs.514793.

3D structure databases

ProteinModelPortaliP58294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000271331.

PTM databases

iPTMnetiP58294.

Polymorphism and mutation databases

BioMutaiPROK1.
DMDMi17380189.

Proteomic databases

PaxDbiP58294.
PRIDEiP58294.

Protocols and materials databases

DNASUi84432.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271331; ENSP00000271331; ENSG00000143125.
GeneIDi84432.
KEGGihsa:84432.
UCSCiuc001dzs.4. human.

Organism-specific databases

CTDi84432.
GeneCardsiPROK1.
HGNCiHGNC:18454. PROK1.
MIMi606233. gene.
neXtProtiNX_P58294.
PharmGKBiPA38539.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYYQ. Eukaryota.
ENOG4111YK9. LUCA.
GeneTreeiENSGT00390000014799.
HOGENOMiHOG000004848.
HOVERGENiHBG031845.
InParanoidiP58294.
OMAiRKRQHHT.
OrthoDBiEOG7SJD78.
PhylomeDBiP58294.
TreeFamiTF332732.

Enzyme and pathway databases

ReactomeiR-HSA-375276. Peptide ligand-binding receptors.
R-HSA-416476. G alpha (q) signalling events.
SIGNORiP58294.

Miscellaneous databases

GenomeRNAii84432.
PROiP58294.
SOURCEiSearch...

Gene expression databases

BgeeiP58294.
CleanExiHS_PROK1.
ExpressionAtlasiP58294. baseline and differential.
GenevisibleiP58294. HS.

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. "Identification of two prokineticin cDNAs: recombinant proteins potently contract gastrointestinal smooth muscle."
    Li M., Bullock C.M., Knauer D.J., Ehlert F.J., Zhou Q.-Y.
    Mol. Pharmacol. 59:692-698(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. "Mambakine, a snake venom related endocrine hormone that controls macrophages."
    Fraser C.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT ILE-67.
    Tissue: Testis.
  8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-34.
  9. "Human endocrine gland-derived vascular endothelial growth factor: expression early in development and in Leydig cell tumors suggests roles in normal and pathological testis angiogenesis."
    Samson M., Peale F.V. Jr., Frantz G., Rioux-Leclercq N., Rajpert-De Meyts E., Ferrara N.
    J. Clin. Endocrinol. Metab. 89:4078-4088(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Implications of endocrine gland-derived vascular endothelial growth factor/prokineticin-1 signaling in human neuroblastoma progression."
    Ngan E.S.W., Sit F.Y.L., Lee K.L., Miao X., Yuan Z., Wang W., Nicholls J.M., Wong K.K.Y., Garcia-Barcelo M., Lui V.C.H., Tam P.K.H.
    Clin. Cancer Res. 13:868-875(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Prokineticin 1 signaling and gene regulation in early human pregnancy."
    Evans J., Catalano R.D., Morgan K., Critchley H.O.D., Millar R.P., Jabbour H.N.
    Endocrinology 149:2877-2887(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPROK1_HUMAN
AccessioniPrimary (citable) accession number: P58294
Secondary accession number(s): Q5VWD4, Q8TC69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: June 8, 2016
This is version 111 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.