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P01210

- PENK_HUMAN

UniProt

P01210 - PENK_HUMAN

Protein

Proenkephalin-A

Gene

PENK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. neuropeptide hormone activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. aggressive behavior Source: Ensembl
    2. behavioral fear response Source: Ensembl
    3. locomotory behavior Source: Ensembl
    4. neuropeptide signaling pathway Source: UniProtKB-KW
    5. sensory perception of pain Source: Ensembl
    6. signal transduction Source: ProtInc
    7. startle response Source: Ensembl

    Keywords - Molecular functioni

    Endorphin, Neuropeptide, Opioid peptide

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Protein family/group databases

    TCDBi1.C.89.1.2. the dynorphin channel-forming neuropeptide (dynorphin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proenkephalin-A
    Cleaved into the following 8 chains:
    Gene namesi
    Name:PENK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:8831. PENK.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33176.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Peptidei25 – 9773SynenkephalinPRO_0000008242Add
    BLAST
    Peptidei100 – 1045Met-enkephalinPRO_0000008243
    Peptidei107 – 1115Met-enkephalinPRO_0000008244
    Peptidei114 – 13320PENK(114-133)By similarityPRO_0000377691Add
    BLAST
    Peptidei136 – 1405Met-enkephalinPRO_0000008246
    Peptidei143 – 18341PENK(143-183)By similarityPRO_0000377692Add
    BLAST
    Peptidei186 – 1938Met-enkephalin-Arg-Gly-LeuPRO_0000008248
    Propeptidei196 – 20712PRO_0000008249Add
    BLAST
    Peptidei210 – 2145Met-enkephalinPRO_0000008250
    Propeptidei217 – 22711PRO_0000008251Add
    BLAST
    Peptidei230 – 2345Leu-enkephalinPRO_0000008252
    Peptidei237 – 25822PENK(237-258)By similarityPRO_0000377693Add
    BLAST
    Peptidei261 – 2677Met-enkephalin-Arg-PhePRO_0000008254

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 481 Publication
    Disulfide bondi30 ↔ 521 Publication
    Disulfide bondi33 ↔ 651 Publication

    Post-translational modificationi

    The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP01210.
    PRIDEiP01210.

    PTM databases

    PhosphoSiteiP01210.

    Miscellaneous databases

    PMAP-CutDBP01210.

    Expressioni

    Gene expression databases

    ArrayExpressiP01210.
    BgeeiP01210.
    CleanExiHS_PENK.
    GenevestigatoriP01210.

    Organism-specific databases

    HPAiCAB016390.
    HPA013138.

    Interactioni

    Protein-protein interaction databases

    BioGridi111205. 1 interaction.
    IntActiP01210. 1 interaction.
    STRINGi9606.ENSP00000324248.

    Structurei

    Secondary structure

    1
    267
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni262 – 2643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PLWNMR-A100-104[»]
    1PLXNMR-A100-104[»]
    2LWCNMR-A261-265[»]
    ProteinModelPortaliP01210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01210.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40630.
    HOGENOMiHOG000013003.
    HOVERGENiHBG000063.
    InParanoidiP01210.
    OMAiGGFMKKD.
    PhylomeDBiP01210.
    TreeFamiTF332620.

    Family and domain databases

    InterProiIPR006024. Opioid_neupept.
    IPR000703. Proenkphlin_A.
    [Graphical view]
    PANTHERiPTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF3. PTHR11438:SF3. 1 hit.
    PfamiPF01160. Opiods_neuropep. 1 hit.
    [Graphical view]
    PRINTSiPR01028. OPIOIDPRCRSR.
    PR01029. PENKAPRCRSR.
    PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01210-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARFLTLCTW LLLLGPGLLA TVRAECSQDC ATCSYRLVRP ADINFLACVM    50
    ECEGKLPSLK IWETCKELLQ LSKPELPQDG TSTLRENSKP EESHLLAKRY 100
    GGFMKRYGGF MKKMDELYPM EPEEEANGSE ILAKRYGGFM KKDAEEDDSL 150
    ANSSDLLKEL LETGDNRERS HHQDGSDNEE EVSKRYGGFM RGLKRSPQLE 200
    DEAKELQKRY GGFMRRVGRP EWWMDYQKRY GGFLKRFAEA LPSDEEGESY 250
    SKEVPEMEKR YGGFMRF 267
    Length:267
    Mass (Da):30,787
    Last modified:July 21, 1986 - v1
    Checksum:i4189BA600C3FC8EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191P → S in CAG46627. 1 PublicationCurated
    Sequence conflicti152 – 1521N → I in CAG46607. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831T → N.
    Corresponds to variant rs11998459 [ dbSNP | Ensembl ].
    VAR_048935
    Natural varianti247 – 2471G → D.
    Corresponds to variant rs1800567 [ dbSNP | Ensembl ].
    VAR_014584

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00509 Genomic DNA. Translation: CAA23767.1.
    J00123, J00122 Genomic DNA. Translation: AAB59409.1.
    AK314908 mRNA. Translation: BAG37420.1.
    CR541808 mRNA. Translation: CAG46607.1.
    CR541828 mRNA. Translation: CAG46627.1.
    CH471068 Genomic DNA. Translation: EAW86785.1.
    BC032505 mRNA. Translation: AAH32505.1.
    CCDSiCCDS6168.1.
    PIRiA93278. EQHUA.
    RefSeqiNP_001129162.1. NM_001135690.1.
    NP_006202.1. NM_006211.3.
    UniGeneiHs.339831.

    Genome annotation databases

    EnsembliENST00000314922; ENSP00000324248; ENSG00000181195.
    ENST00000451791; ENSP00000400894; ENSG00000181195.
    GeneIDi5179.
    KEGGihsa:5179.
    UCSCiuc003xsz.2. human.

    Polymorphism databases

    DMDMi129770.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00509 Genomic DNA. Translation: CAA23767.1 .
    J00123 , J00122 Genomic DNA. Translation: AAB59409.1 .
    AK314908 mRNA. Translation: BAG37420.1 .
    CR541808 mRNA. Translation: CAG46607.1 .
    CR541828 mRNA. Translation: CAG46627.1 .
    CH471068 Genomic DNA. Translation: EAW86785.1 .
    BC032505 mRNA. Translation: AAH32505.1 .
    CCDSi CCDS6168.1.
    PIRi A93278. EQHUA.
    RefSeqi NP_001129162.1. NM_001135690.1.
    NP_006202.1. NM_006211.3.
    UniGenei Hs.339831.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PLW NMR - A 100-104 [» ]
    1PLX NMR - A 100-104 [» ]
    2LWC NMR - A 261-265 [» ]
    ProteinModelPortali P01210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111205. 1 interaction.
    IntActi P01210. 1 interaction.
    STRINGi 9606.ENSP00000324248.

    Protein family/group databases

    TCDBi 1.C.89.1.2. the dynorphin channel-forming neuropeptide (dynorphin) family.

    PTM databases

    PhosphoSitei P01210.

    Polymorphism databases

    DMDMi 129770.

    Proteomic databases

    PaxDbi P01210.
    PRIDEi P01210.

    Protocols and materials databases

    DNASUi 5179.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314922 ; ENSP00000324248 ; ENSG00000181195 .
    ENST00000451791 ; ENSP00000400894 ; ENSG00000181195 .
    GeneIDi 5179.
    KEGGi hsa:5179.
    UCSCi uc003xsz.2. human.

    Organism-specific databases

    CTDi 5179.
    GeneCardsi GC08M057349.
    HGNCi HGNC:8831. PENK.
    HPAi CAB016390.
    HPA013138.
    MIMi 131330. gene.
    neXtProti NX_P01210.
    PharmGKBi PA33176.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40630.
    HOGENOMi HOG000013003.
    HOVERGENi HBG000063.
    InParanoidi P01210.
    OMAi GGFMKKD.
    PhylomeDBi P01210.
    TreeFami TF332620.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P01210.
    GenomeRNAii 5179.
    NextBioi 20046.
    PMAP-CutDB P01210.
    PROi P01210.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01210.
    Bgeei P01210.
    CleanExi HS_PENK.
    Genevestigatori P01210.

    Family and domain databases

    InterProi IPR006024. Opioid_neupept.
    IPR000703. Proenkphlin_A.
    [Graphical view ]
    PANTHERi PTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF3. PTHR11438:SF3. 1 hit.
    Pfami PF01160. Opiods_neuropep. 1 hit.
    [Graphical view ]
    PRINTSi PR01028. OPIOIDPRCRSR.
    PR01029. PENKAPRCRSR.
    PROSITEi PS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the human Met- and Leu-enkephalin precursor and its mRNA."
      Comb M., Seeburg P.H., Adelman J., Eiden L., Herbert E.
      Nature 295:663-666(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation and structural organization of the human preproenkephalin gene."
      Noda M., Teranishi Y., Takahashi H., Toyosato M., Notake M., Nakanishi S., Numa S.
      Nature 297:431-434(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      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.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain.
    7. "The structure of synenkephalin (pro-enkephalin 1-73) is dictated by three disulfide bonds."
      Lecchi P., Loh Y.P., Snell C.R., Pannell L.K.
      Biochem. Biophys. Res. Commun. 232:800-805(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.

    Entry informationi

    Entry nameiPENK_HUMAN
    AccessioniPrimary (citable) accession number: P01210
    Secondary accession number(s): B2RC23, Q6FHC6, Q6FHE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 132 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3