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Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(114-133); PENK(143-183); Met-enkephalin-Arg-Gly-Leu; Leu-enkephalin; PENK(237-258); Met-enkephalin-Arg-Phe]

 PENK_HUMAN              Reviewed;         267 AA.
P01210; B2RC23; Q6FHC6; Q6FHE6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 161.
RecName: Full=Proenkephalin-A;
Contains:
RecName: Full=Synenkephalin;
Contains:
RecName: Full=Met-enkephalin;
AltName: Full=Opioid growth factor;
Short=OGF;
Contains:
RecName: Full=PENK(114-133);
Contains:
RecName: Full=PENK(143-183);
Contains:
RecName: Full=Met-enkephalin-Arg-Gly-Leu;
Contains:
RecName: Full=Leu-enkephalin;
Contains:
RecName: Full=PENK(237-258);
Contains:
RecName: Full=Met-enkephalin-Arg-Phe;
Flags: Precursor;
Name=PENK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7057924; DOI=10.1038/295663a0;
Comb M., Seeburg P.H., Adelman J., Eiden L., Herbert E.;
"Primary structure of the human Met- and Leu-enkephalin precursor and
its mRNA.";
Nature 295:663-666(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6281660; DOI=10.1038/297431a0;
Noda M., Teranishi Y., Takahashi H., Toyosato M., Notake M.,
Nakanishi S., Numa S.;
"Isolation and structural organization of the human preproenkephalin
gene.";
Nature 297:431-434(1982).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
DISULFIDE BONDS.
PubMed=9126357; DOI=10.1006/bbrc.1997.6373;
Lecchi P., Loh Y.P., Snell C.R., Pannell L.K.;
"The structure of synenkephalin (pro-enkephalin 1-73) is dictated by
three disulfide bonds.";
Biochem. Biophys. Res. Commun. 232:800-805(1997).
-!- FUNCTION: Met- and 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. PENK(114-133) and PENK(237-258) increase glutamate release
in the striatum. PENK(114-133) decreases GABA concentration in the
striatum.
-!- INTERACTION:
P35372:OPRM1; NbExp=3; IntAct=EBI-6656055, EBI-2624570;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: The N-terminal domain contains 6 conserved cysteines thought
to be involved in disulfide bonding and/or processing.
-!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
{ECO:0000305}.
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EMBL; V00509; CAA23767.1; -; Genomic_DNA.
EMBL; J00123; AAB59409.1; -; Genomic_DNA.
EMBL; J00122; AAB59409.1; JOINED; Genomic_DNA.
EMBL; AK314908; BAG37420.1; -; mRNA.
EMBL; CR541808; CAG46607.1; -; mRNA.
EMBL; CR541828; CAG46627.1; -; mRNA.
EMBL; CH471068; EAW86785.1; -; Genomic_DNA.
EMBL; BC032505; AAH32505.1; -; mRNA.
CCDS; CCDS6168.1; -.
PIR; A93278; EQHUA.
RefSeq; NP_001129162.1; NM_001135690.2.
UniGene; Hs.339831; -.
PDB; 1PLW; NMR; -; A=100-104.
PDB; 1PLX; NMR; -; A=100-104.
PDB; 2LWC; NMR; -; A=261-265.
PDB; 5E33; X-ray; 1.84 A; B=261-265.
PDB; 5E3A; X-ray; 2.05 A; B=230-234.
PDBsum; 1PLW; -.
PDBsum; 1PLX; -.
PDBsum; 2LWC; -.
PDBsum; 5E33; -.
PDBsum; 5E3A; -.
ProteinModelPortal; P01210; -.
SMR; P01210; -.
BioGrid; 111205; 8.
IntAct; P01210; 3.
STRING; 9606.ENSP00000324248; -.
TCDB; 1.C.89.1.2; the dynorphin channel-forming neuropeptide (dynorphin) family.
iPTMnet; P01210; -.
PhosphoSitePlus; P01210; -.
BioMuta; PENK; -.
DMDM; 129770; -.
PaxDb; P01210; -.
PeptideAtlas; P01210; -.
PRIDE; P01210; -.
ProteomicsDB; 51344; -.
DNASU; 5179; -.
Ensembl; ENST00000314922; ENSP00000324248; ENSG00000181195.
Ensembl; ENST00000451791; ENSP00000400894; ENSG00000181195.
GeneID; 5179; -.
KEGG; hsa:5179; -.
UCSC; uc003xsz.3; human.
CTD; 5179; -.
DisGeNET; 5179; -.
EuPathDB; HostDB:ENSG00000181195.10; -.
GeneCards; PENK; -.
HGNC; HGNC:8831; PENK.
HPA; CAB016390; -.
HPA; HPA013138; -.
MIM; 131330; gene.
neXtProt; NX_P01210; -.
OpenTargets; ENSG00000181195; -.
PharmGKB; PA33176; -.
eggNOG; ENOG410IJUY; Eukaryota.
eggNOG; ENOG4110ZYD; LUCA.
GeneTree; ENSGT00530000063761; -.
HOGENOM; HOG000013003; -.
HOVERGEN; HBG000063; -.
InParanoid; P01210; -.
KO; K18832; -.
OMA; GFMKKMD; -.
OrthoDB; EOG091G0HV8; -.
PhylomeDB; P01210; -.
TreeFam; TF332620; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P01210; -.
EvolutionaryTrace; P01210; -.
GenomeRNAi; 5179; -.
PMAP-CutDB; P01210; -.
PRO; PR:P01210; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000181195; -.
CleanEx; HS_PENK; -.
ExpressionAtlas; P01210; baseline and differential.
Genevisible; P01210; HS.
GO; GO:0043679; C:axon terminus; IBA:GO_Central.
GO; GO:0070852; C:cell body fiber; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032280; C:symmetric synapse; IEA:Ensembl.
GO; GO:0005184; F:neuropeptide hormone activity; TAS:ProtInc.
GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
GO; GO:0031628; F:opioid receptor binding; IBA:GO_Central.
GO; GO:0002118; P:aggressive behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0051867; P:general adaptation syndrome, behavioral process; IEA:Ensembl.
GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:2000987; P:positive regulation of behavioral fear response; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0007600; P:sensory perception; IBA:GO_Central.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001964; P:startle response; IEA:Ensembl.
InterPro; IPR006024; Opioid_neupept.
InterPro; IPR000703; Proenkphlin_A.
PANTHER; PTHR11438; PTHR11438; 1.
PANTHER; PTHR11438:SF3; PTHR11438:SF3; 1.
Pfam; PF01160; Opiods_neuropep; 1.
PRINTS; PR01028; OPIOIDPRCRSR.
PRINTS; PR01029; PENKAPRCRSR.
PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Endorphin; Neuropeptide; Opioid peptide;
Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000255}.
PEPTIDE 25 97 Synenkephalin.
/FTId=PRO_0000008242.
PEPTIDE 100 104 Met-enkephalin.
/FTId=PRO_0000008243.
PEPTIDE 107 111 Met-enkephalin.
/FTId=PRO_0000008244.
PEPTIDE 114 133 PENK(114-133). {ECO:0000250}.
/FTId=PRO_0000377691.
PEPTIDE 136 140 Met-enkephalin.
/FTId=PRO_0000008246.
PEPTIDE 143 183 PENK(143-183). {ECO:0000250}.
/FTId=PRO_0000377692.
PEPTIDE 186 193 Met-enkephalin-Arg-Gly-Leu.
/FTId=PRO_0000008248.
PROPEP 196 207
/FTId=PRO_0000008249.
PEPTIDE 210 214 Met-enkephalin.
/FTId=PRO_0000008250.
PROPEP 217 227
/FTId=PRO_0000008251.
PEPTIDE 230 234 Leu-enkephalin.
/FTId=PRO_0000008252.
PEPTIDE 237 258 PENK(237-258). {ECO:0000250}.
/FTId=PRO_0000377693.
PEPTIDE 261 267 Met-enkephalin-Arg-Phe.
/FTId=PRO_0000008254.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:P04094}.
DISULFID 26 48 {ECO:0000269|PubMed:9126357}.
DISULFID 30 52 {ECO:0000269|PubMed:9126357}.
DISULFID 33 65 {ECO:0000269|PubMed:9126357}.
VARIANT 83 83 T -> N (in dbSNP:rs11998459).
/FTId=VAR_048935.
VARIANT 247 247 G -> D (in dbSNP:rs1800567).
/FTId=VAR_014584.
CONFLICT 119 119 P -> S (in Ref. 4; CAG46627).
{ECO:0000305}.
CONFLICT 152 152 N -> I (in Ref. 4; CAG46607).
{ECO:0000305}.
TURN 262 264 {ECO:0000244|PDB:2LWC}.
SEQUENCE 267 AA; 30787 MW; 4189BA600C3FC8EE CRC64;
MARFLTLCTW LLLLGPGLLA TVRAECSQDC ATCSYRLVRP ADINFLACVM ECEGKLPSLK
IWETCKELLQ LSKPELPQDG TSTLRENSKP EESHLLAKRY GGFMKRYGGF MKKMDELYPM
EPEEEANGSE ILAKRYGGFM KKDAEEDDSL ANSSDLLKEL LETGDNRERS HHQDGSDNEE
EVSKRYGGFM RGLKRSPQLE DEAKELQKRY GGFMRRVGRP EWWMDYQKRY GGFLKRFAEA
LPSDEEGESY SKEVPEMEKR YGGFMRF


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