PENK_HUMAN
ID PENK_HUMAN Reviewed; 267 AA.
AC P01210; B2RC23; Q6FHC6; Q6FHE6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Proenkephalin-A {ECO:0000305};
DE Contains:
DE RecName: Full=Synenkephalin {ECO:0000303|PubMed:9126357};
DE Contains:
DE RecName: Full=Met-enkephalin {ECO:0000303|PubMed:656131};
DE AltName: Full=Opioid growth factor;
DE Short=OGF;
DE Contains:
DE RecName: Full=PENK(114-133) {ECO:0000250|UniProtKB:P04094};
DE Contains:
DE RecName: Full=PENK(143-183) {ECO:0000250|UniProtKB:P04094};
DE Contains:
DE RecName: Full=Met-enkephalin-Arg-Gly-Leu {ECO:0000303|PubMed:2982830};
DE Contains:
DE RecName: Full=Leu-enkephalin {ECO:0000303|PubMed:656131};
DE Contains:
DE RecName: Full=PENK(237-258) {ECO:0000250|UniProtKB:P04094};
DE Contains:
DE RecName: Full=Met-enkephalin-Arg-Phe {ECO:0000250|UniProtKB:P22005};
DE Flags: Precursor;
GN Name=PENK {ECO:0000312|HGNC:HGNC:8831};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7057924; DOI=10.1038/295663a0;
RA Comb M., Seeburg P.H., Adelman J., Eiden L., Herbert E.;
RT "Primary structure of the human Met- and Leu-enkephalin precursor and its
RT mRNA.";
RL Nature 295:663-666(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6281660; DOI=10.1038/297431a0;
RA Noda M., Teranishi Y., Takahashi H., Toyosato M., Notake M., Nakanishi S.,
RA Numa S.;
RT "Isolation and structural organization of the human preproenkephalin
RT gene.";
RL Nature 297:431-434(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEOLYTIC CLEAVAGE (MET-ENKEPHALIN AND LEU-ENKEPHALIN).
RX PubMed=656131; DOI=10.1016/0006-2952(78)90542-7;
RA Erdoes E.G., Johnson A.R., Boyden N.T.;
RT "Hydrolysis of enkephalin by cultured human endothelial cells and by
RT purified peptidyl dipeptidase.";
RL Biochem. Pharmacol. 27:843-848(1978).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MET-ENKEPHALIN-ARG-GLY-LEU).
RX PubMed=2982830; DOI=10.1016/s0021-9258(18)89410-8;
RA Norman J.A., Chang J.Y.;
RT "Proteolytic conversion of [Met]enkephalin-Arg6-Gly7-Leu8 by brain synaptic
RT membranes. Characterization of formed peptides and mechanism of
RT proteolysis.";
RL J. Biol. Chem. 260:2653-2656(1985).
RN [9]
RP DISULFIDE BONDS.
RX PubMed=9126357; DOI=10.1006/bbrc.1997.6373;
RA Lecchi P., Loh Y.P., Snell C.R., Pannell L.K.;
RT "The structure of synenkephalin (pro-enkephalin 1-73) is dictated by three
RT disulfide bonds.";
RL Biochem. Biophys. Res. Commun. 232:800-805(1997).
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:0000269|PubMed:7057924}.
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:0000269|PubMed:7057924}.
CC -!- FUNCTION: [Met-enkephalin-Arg-Phe]: Met-enkephalin-Arg-Phe neuropeptide
CC acts as a strong ligand of Mu-type opioid receptor OPRM1. Met-
CC enkephalin-Arg-Phe-binding to OPRM1 in the nucleus accumbens of the
CC brain increases activation of OPRM1, leading to long-term synaptic
CC depression of glutamate release. {ECO:0000250|UniProtKB:P22005}.
CC -!- FUNCTION: [PENK(114-133)]: Increases glutamate release in the striatum
CC and decreases GABA concentration in the striatum.
CC {ECO:0000250|UniProtKB:P04094}.
CC -!- FUNCTION: [PENK(237-258)]: Increases glutamate release in the striatum.
CC {ECO:0000250|UniProtKB:P04094}.
CC -!- INTERACTION:
CC PRO_0000008243; P35372: OPRM1; NbExp=3; IntAct=EBI-6656055, EBI-2624570;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. Secreted
CC {ECO:0000250|UniProtKB:P01211}.
CC -!- PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
CC {ECO:0000250|UniProtKB:P01211}.
CC -!- PTM: [Met-enkephalin]: Processed and degraded by ACE.
CC {ECO:0000269|PubMed:656131}.
CC -!- PTM: [Leu-enkephalin]: Processed and degraded by ACE.
CC {ECO:0000269|PubMed:656131}.
CC -!- PTM: [Met-enkephalin-Arg-Gly-Leu]: Probably cleaved by ACE.
CC {ECO:0000305|PubMed:2982830}.
CC -!- PTM: [Met-enkephalin-Arg-Phe]: Processed by ACE to generate Met-
CC enkephalin in the nucleus accumbens of the brain.
CC {ECO:0000250|UniProtKB:P04094}.
CC -!- PTM: The N-terminal domain contains 6 conserved cysteines thought to be
CC involved in disulfide bonding and/or processing.
CC {ECO:0000269|PubMed:9126357}.
CC -!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
CC {ECO:0000305}.
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DR EMBL; V00509; CAA23767.1; -; Genomic_DNA.
DR EMBL; J00123; AAB59409.1; -; Genomic_DNA.
DR EMBL; J00122; AAB59409.1; JOINED; Genomic_DNA.
DR EMBL; AK314908; BAG37420.1; -; mRNA.
DR EMBL; CR541808; CAG46607.1; -; mRNA.
DR EMBL; CR541828; CAG46627.1; -; mRNA.
DR EMBL; CH471068; EAW86785.1; -; Genomic_DNA.
DR EMBL; BC032505; AAH32505.1; -; mRNA.
DR CCDS; CCDS6168.1; -.
DR PIR; A93278; EQHUA.
DR RefSeq; NP_001129162.1; NM_001135690.2.
DR PDB; 1PLW; NMR; -; A=100-104.
DR PDB; 1PLX; NMR; -; A=100-104.
DR PDB; 2LWC; NMR; -; A=261-265.
DR PDB; 5E33; X-ray; 1.84 A; B=261-265.
DR PDB; 5E3A; X-ray; 2.05 A; B=230-234.
DR PDBsum; 1PLW; -.
DR PDBsum; 1PLX; -.
DR PDBsum; 2LWC; -.
DR PDBsum; 5E33; -.
DR PDBsum; 5E3A; -.
DR AlphaFoldDB; P01210; -.
DR SMR; P01210; -.
DR BioGRID; 111205; 9.
DR IntAct; P01210; 9.
DR STRING; 9606.ENSP00000324248; -.
DR TCDB; 1.C.89.1.2; the dynorphin channel-forming neuropeptide (dynorphin) family.
DR iPTMnet; P01210; -.
DR PhosphoSitePlus; P01210; -.
DR BioMuta; PENK; -.
DR DMDM; 129770; -.
DR jPOST; P01210; -.
DR MassIVE; P01210; -.
DR PaxDb; P01210; -.
DR PeptideAtlas; P01210; -.
DR PRIDE; P01210; -.
DR ProteomicsDB; 51344; -.
DR Antibodypedia; 2211; 395 antibodies from 36 providers.
DR DNASU; 5179; -.
DR Ensembl; ENST00000314922.3; ENSP00000324248.3; ENSG00000181195.11.
DR Ensembl; ENST00000451791.7; ENSP00000400894.2; ENSG00000181195.11.
DR GeneID; 5179; -.
DR KEGG; hsa:5179; -.
DR MANE-Select; ENST00000451791.7; ENSP00000400894.2; NM_001135690.3; NP_001129162.1.
DR UCSC; uc003xsz.3; human.
DR CTD; 5179; -.
DR DisGeNET; 5179; -.
DR GeneCards; PENK; -.
DR HGNC; HGNC:8831; PENK.
DR HPA; ENSG00000181195; Group enriched (adrenal gland, brain, testis).
DR MIM; 131330; gene.
DR neXtProt; NX_P01210; -.
DR OpenTargets; ENSG00000181195; -.
DR PharmGKB; PA33176; -.
DR VEuPathDB; HostDB:ENSG00000181195; -.
DR eggNOG; ENOG502QWWK; Eukaryota.
DR GeneTree; ENSGT00950000183149; -.
DR HOGENOM; CLU_070973_0_0_1; -.
DR InParanoid; P01210; -.
DR OMA; CAACAYR; -.
DR OrthoDB; 1149395at2759; -.
DR PhylomeDB; P01210; -.
DR TreeFam; TF332620; -.
DR PathwayCommons; P01210; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P01210; -.
DR SIGNOR; P01210; -.
DR BioGRID-ORCS; 5179; 6 hits in 1062 CRISPR screens.
DR ChiTaRS; PENK; human.
DR EvolutionaryTrace; P01210; -.
DR GenomeRNAi; 5179; -.
DR Pharos; P01210; Tbio.
DR PRO; PR:P01210; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P01210; protein.
DR Bgee; ENSG00000181195; Expressed in nucleus accumbens and 164 other tissues.
DR ExpressionAtlas; P01210; baseline and differential.
DR Genevisible; P01210; HS.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0070852; C:cell body fiber; IEA:Ensembl.
DR GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0099013; C:neuronal dense core vesicle lumen; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032280; C:symmetric synapse; IEA:Ensembl.
DR GO; GO:0034592; C:synaptic vesicle lumen; IEA:Ensembl.
DR GO; GO:0005184; F:neuropeptide hormone activity; TAS:ProtInc.
DR GO; GO:0001515; F:opioid peptide activity; ISS:UniProtKB.
DR GO; GO:0031628; F:opioid receptor binding; ISS:UniProtKB.
DR GO; GO:0002118; P:aggressive behavior; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0051867; P:general adaptation syndrome, behavioral process; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IEA:Ensembl.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0007600; P:sensory perception; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0001964; P:startle response; IEA:Ensembl.
DR GO; GO:0099538; P:synaptic signaling via neuropeptide; IEA:Ensembl.
DR InterPro; IPR006024; Opioid_neupept.
DR InterPro; IPR000703; Proenkphlin_A.
DR PANTHER; PTHR11438; PTHR11438; 1.
DR PANTHER; PTHR11438:SF3; PTHR11438:SF3; 1.
DR Pfam; PF01160; Opiods_neuropep; 1.
DR PRINTS; PR01028; OPIOIDPRCRSR.
DR PRINTS; PR01029; PENKAPRCRSR.
DR PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Disulfide bond; Endorphin; Neuropeptide; Opioid peptide; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PEPTIDE 25..97
FT /note="Synenkephalin"
FT /id="PRO_0000008242"
FT PEPTIDE 100..104
FT /note="Met-enkephalin"
FT /evidence="ECO:0000269|PubMed:656131"
FT /id="PRO_0000008243"
FT PEPTIDE 107..111
FT /note="Met-enkephalin"
FT /evidence="ECO:0000269|PubMed:656131"
FT /id="PRO_0000008244"
FT PEPTIDE 114..133
FT /note="PENK(114-133)"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT /id="PRO_0000377691"
FT PEPTIDE 136..140
FT /note="Met-enkephalin"
FT /id="PRO_0000008246"
FT PEPTIDE 143..183
FT /note="PENK(143-183)"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT /id="PRO_0000377692"
FT PEPTIDE 186..193
FT /note="Met-enkephalin-Arg-Gly-Leu"
FT /evidence="ECO:0000269|PubMed:2982830"
FT /id="PRO_0000008248"
FT PROPEP 196..207
FT /id="PRO_0000008249"
FT PEPTIDE 210..214
FT /note="Met-enkephalin"
FT /id="PRO_0000008250"
FT PROPEP 217..227
FT /id="PRO_0000008251"
FT PEPTIDE 230..234
FT /note="Leu-enkephalin"
FT /id="PRO_0000008252"
FT PEPTIDE 237..258
FT /note="PENK(237-258)"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT /id="PRO_0000377693"
FT PEPTIDE 261..267
FT /note="Met-enkephalin-Arg-Phe"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT /id="PRO_0000008254"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 111..112
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 112..113
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 133..134
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 214..215
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 215..216
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT SITE 218..219
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P01211"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04094"
FT DISULFID 26..48
FT /evidence="ECO:0000269|PubMed:9126357"
FT DISULFID 30..52
FT /evidence="ECO:0000269|PubMed:9126357"
FT DISULFID 33..65
FT /evidence="ECO:0000269|PubMed:9126357"
FT VARIANT 83
FT /note="T -> N (in dbSNP:rs11998459)"
FT /id="VAR_048935"
FT VARIANT 247
FT /note="G -> D (in dbSNP:rs1800567)"
FT /id="VAR_014584"
FT CONFLICT 119
FT /note="P -> S (in Ref. 4; CAG46627)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="N -> I (in Ref. 4; CAG46607)"
FT /evidence="ECO:0000305"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2LWC"
SQ 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
