Reviewed, UniProtKB/Swiss-Prot P01213 (PDYN_HUMAN)

Names and origin

Protein names

Recommended name:
    Proenkephalin-B
Alternative name(s):
    Beta-neoendorphin-dynorphin
    Preprodynorphin
Cleaved into the following 9 chains:
    1- Recommended name:
            Alpha-neoendorphin
    2- Recommended name:
            Beta-neoendorphin
    3- Recommended name:
            Big dynorphin
                Short name=Big Dyn
    4- Recommended name:
            Dynorphin A(1-17)
                Short name=Dynorphin A
                Short name=Dyn-A17
    5- Recommended name:
            Dynorphin A(1-13)
    6- Recommended name:
            Dynorphin A(1-8)
    7- Recommended name:
            Leu-enkephalin
    8- Recommended name:
            Rimorphin
        Alternative name(s):
            Dynorphin B
              Short name=Dyn-B
            Dynorphin B(1-13)
    9- Recommended name:
            Leumorphin
        Alternative name(s):
            Dynorphin B-29

Gene names

Name:

PDYN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress By similarity. Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin By similarity. Leumorphin has a typical opiod activity and may have anti-apoptotic effect By similarity.
Subcellular location	Secreted.
Post-translational modification	The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
Sequence similarities	Belongs to the opioid neuropeptide precursor family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endorphin Neuropeptide Neurotransmitter Opioid peptide
PTM	Cleavage on pair of basic residues Disulfide bond
Gene Ontology (GO)
Biological process	neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	opioid peptide activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Propeptide	21 – 172	152			PRO_0000008176
	Peptide	175 – 184	10	Alpha-neoendorphin		PRO_0000306347
	Peptide	175 – 183	9	Beta-neoendorphin		PRO_0000008177
	Peptide	175 – 179	5	Leu-enkephalin By similarity		PRO_0000306348
	Propeptide	186 – 204	19			PRO_0000008178
	Peptide	207 – 238	32	Big dynorphin		PRO_0000306349
	Peptide	207 – 223	17	Dynorphin A(1-17)		PRO_0000008179
	Peptide	207 – 219	13	Dynorphin A(1-13) By similarity		PRO_0000306350
	Peptide	207 – 214	8	Dynorphin A(1-8) By similarity		PRO_0000306351
	Peptide	207 – 211	5	Leu-enkephalin By similarity		PRO_0000306352
	Peptide	226 – 254	29	Leumorphin		PRO_0000008180
	Peptide	226 – 238	13	Rimorphin		PRO_0000008181
	Peptide	226 – 230	5	Leu-enkephalin		PRO_0000008182

Sequences

	Sequence		Length	Mass (Da)
	P01213-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 783E7D6AC068CE68	FASTA	254	28,385
	10 20 30 40 50 60 MAWQGLVLAA CLLMFPSTTA DCLSRCSLCA VKTQDGPKPI NPLICSLQCQ AALLPSEEWE 70 80 90 100 110 120 RCQSFLSFFT PSTLGLNDKE DLGSKSVGEG PYSELAKLSG SFLKELEKSK FLPSISTKEN 130 140 150 160 170 180 TLSKSLEEKL RGLSDGFREG AESELMRDAQ LNDGAMETGT LYLAEEDPKE QVKRYGGFLR 190 200 210 220 230 240 KYPKRSSEVA GEGDGDSMGH EDLYKRYGGF LRRIRPKLKW DNQKRYGGFL RRQFKVVTRS 250 QEDPNAYSGE LFDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and structural organization of the human preproenkephalin B gene." Horikawa S., Takai T., Toyosato M., Takahashi H., Noda M., Kakidani H., Kubo T., Hirose T., Inayama S., Hayashida H., Miyata T., Numa S. Nature 306:611-614(1983) [PubMed: 6316163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles." Tessmer M.R., Kallick D.A. Biochemistry 36:1971-1981(1997) [PubMed: 9047294] [Abstract] Cited for: STRUCTURE BY NMR OF DYNORPHIN A(1-17).
[5]	"Dynorphin peptides differentially regulate the human kappa opioid receptor." Chen Y., Chen C., Liu-Chen L.-Y. Life Sci. 80:1439-1448(2007) [PubMed: 17316701] [Abstract] Cited for: FUNCTION.
[6]	"Big dynorphin as a putative endogenous ligand for the kappa-opioid receptor." Merg F., Filliol D., Usynin I., Bazov I., Bark N., Hurd Y.L., Yakovleva T., Kieffer B.L., Bakalkin G. J. Neurochem. 97:292-301(2006) [PubMed: 16515546] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X02536 Genomic DNA. No translation available. K02267 Genomic DNA. No translation available. K02268 Genomic DNA. Translation: AAA58456.2. X00176 Genomic DNA. Translation: CAA24999.1. AL034562 Genomic DNA. Translation: CAB38875.1. BC026334 mRNA. Translation: AAH26334.1.
IPI	IPI00000832.
PIR	DFHU. A01478.
RefSeq	NP_077722.1.
UniGene	Hs.22584
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	1.C.89.1.1. dynorphin channel-forming neuropeptide (Dynorphin) family.
Proteomic databases
PeptideAtlas	P01213.
PRIDE	P01213.
Genome annotation databases
Ensembl	ENSG00000101327. Homo sapiens. [Contig view]
GeneID	5173.
KEGG	hsa:5173.
Organism-specific databases
GeneCards	GC20M001907.
H-InvDB	HIX0015573.
HGNC	HGNC:8820. PDYN.
MIM	131340. gene.
PharmGKB	PA33163.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P01213.
HOVERGEN	P01213.
OMA	P01213. QEDPNAY.
Enzyme and pathway databases
Reactome	REACT_14797. Signaling by GPCR.
Gene expression databases
ArrayExpress	P01213.
Bgee	P01213.
CleanEx	HS_PDYN.
GermOnline	ENSG00000101327. Homo sapiens.
Family and domain databases
InterPro	IPR006024. Opioid_neupept. IPR000750. Proenkphlin_B. [Graphical view]
PANTHER	PTHR11438. Opioid_neupept. 1 hit. PTHR11438:SF4. Proenkphlin_B. 1 hit.
Pfam	PF01160. Opiods_neuropep. 1 hit. [Graphical view]
PRINTS	PR01028. OPIOIDPRCRSR. PR01030. PENKBPRCRSR.
PROSITE	PS01252. OPIOIDS_PRECURSOR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	20018.
PMAP-CutDB	P01213.
SOURCE	Search...

Entry information

Entry name

PDYN_HUMAN

Accession

Primary (citable) accession number: P01213

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)