PENK_FELCA
ID PENK_FELCA Reviewed; 187 AA.
AC Q28409;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Proenkephalin-A;
DE Contains:
DE RecName: Full=Synenkephalin;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Contains:
DE RecName: Full=Leu-enkephalin;
DE Flags: Precursor; Fragment;
GN Name=PENK;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=8719703; DOI=10.1016/0197-0186(95)00079-8;
RA Chaminade M., Chelot E., de Carvalho L., Bochet P., Rossier J.;
RT "Cat proenkephalin-A does not contain the opioid octapeptide.";
RL Neurochem. Int. 28:155-160(1996).
CC -!- FUNCTION: [Met-enkephalin]: Neuropeptide that competes with and mimic
CC the effects of opiate drugs. They play a role in a number of
CC physiologic functions, including pain perception and responses to
CC stress. {ECO:0000250|UniProtKB:P01210}.
CC -!- FUNCTION: [Leu-enkephalin]: Neuropeptide that competes with and mimic
CC the effects of opiate drugs. They play a role in a number of
CC physiologic functions, including pain perception and responses to
CC stress. {ECO:0000250|UniProtKB:P01210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. Secreted
CC {ECO:0000250|UniProtKB:P01211}.
CC -!- PTM: [Met-enkephalin]: Processed and degraded by ACE.
CC {ECO:0000250|UniProtKB:P01210}.
CC -!- PTM: [Leu-enkephalin]: Processed and degraded by ACE.
CC {ECO:0000250|UniProtKB:P01210}.
CC -!- PTM: The N-terminal domain contains 6 conserved cysteines thought to be
CC involved in disulfide bonding and/or processing.
CC {ECO:0000250|UniProtKB:P01210}.
CC -!- PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
CC {ECO:0000250|UniProtKB:P01211}.
CC -!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
CC {ECO:0000305}.
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DR EMBL; U24247; AAC48512.1; -; mRNA.
DR AlphaFoldDB; Q28409; -.
DR SMR; Q28409; -.
DR STRING; 9685.ENSFCAP00000016633; -.
DR eggNOG; ENOG502QWWK; Eukaryota.
DR InParanoid; Q28409; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
DR GO; GO:0031628; F:opioid receptor binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007600; P:sensory perception; IBA:GO_Central.
DR InterPro; IPR006024; Opioid_neupept.
DR InterPro; IPR000703; Proenkphlin_A.
DR PANTHER; PTHR11438; PTHR11438; 1.
DR PANTHER; PTHR11438:SF3; PTHR11438:SF3; 1.
DR PRINTS; PR01029; PENKAPRCRSR.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle; Disulfide bond;
KW Endorphin; Neuropeptide; Opioid peptide; Phosphoprotein;
KW Reference proteome; Secreted.
FT PEPTIDE <1..34
FT /note="Synenkephalin"
FT /id="PRO_0000008232"
FT PEPTIDE 38..42
FT /note="Met-enkephalin"
FT /id="PRO_0000008233"
FT PEPTIDE 45..49
FT /note="Met-enkephalin"
FT /id="PRO_0000008234"
FT PROPEP 52..70
FT /id="PRO_0000008235"
FT PEPTIDE 73..77
FT /note="Met-enkephalin"
FT /id="PRO_0000008236"
FT PROPEP 80..143
FT /id="PRO_0000008237"
FT PEPTIDE 146..150
FT /note="Met-enkephalin"
FT /id="PRO_0000008238"
FT PROPEP 153..163
FT /id="PRO_0000008239"
FT PEPTIDE 166..170
FT /note="Leu-enkephalin"
FT /id="PRO_0000008240"
FT PROPEP 173..>187
FT /id="PRO_0000008241"
FT REGION 81..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 49..50
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 50..51
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 70..71
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 150..151
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 151..152
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 154..155
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT NON_TER 1
FT NON_TER 187
SQ SEQUENCE 187 AA; 21267 MW; 0D1837460773E433 CRC64;
WETCKEFLKL SQLEIPQDGT SALRESSPEE SHALRKKYGG FMKRYGGFMK KMDELYPQEP
EEEAPAEILA KRYGGFMKKD AEEEEDALAS SSDLLKELLG PGETETAAAP RGRDDEDVSK
SHGGFMRALK GSPQLAQEAK MLQKRYGGFM RRVGRPEWWM DYQKRYGGFL KRFADSLPSD
EEGESYS
