ID KLK8_MOUSE Reviewed; 260 AA. AC Q61955; Q8K5D7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Kallikrein-8; DE Short=mK8; DE EC=3.4.21.118; DE AltName: Full=Neuropsin; DE Short=NP; DE AltName: Full=Serine protease 19; DE Flags: Precursor; GN Name=Klk8; Synonyms=Nrpn, Prss19; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=BALB/cJ; TISSUE=Hippocampus; RX PubMed=7623137; DOI=10.1523/jneurosci.15-07-05088.1995; RA Chen Z.-L., Yoshida S., Kato K., Momota Y., Suzuki J., Tanaka T., Ito J., RA Nishino H., Aimoto S., Kiyama H., Shiosaka S.; RT "Expression and activity-dependent changes of a novel limbic-serine RT protease gene in the hippocampus."; RL J. Neurosci. 15:5088-5097(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10773678; DOI=10.1159/000015497; RA Yoshida S., Hirata A., Inoue N., Shiosaka S.; RT "Assignment of the neuropsin gene (Prss19) to mouse chromosome band 7B4 by RT in situ hybridization."; RL Cytogenet. Cell Genet. 88:97-98(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary gland; 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 [4] RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=9556608; DOI=10.1074/jbc.273.18.11189; RA Shimizu C., Yoshida S., Shibata M., Kato K., Momota Y., Matsumoto K., RA Shiosaka T., Midorikawa R., Kamachi T., Kawabe A., Shiosaka S.; RT "Characterization of recombinant and brain neuropsin, a plasticity-related RT serine protease."; RL J. Biol. Chem. 273:11189-11196(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-260, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=12354676; DOI=10.1016/s0303-7207(02)00184-3; RA Katsu Y., Takasu E., Iguchi T.; RT "Estrogen-independent expression of neuropsin, a serine protease in the RT vagina of mice exposed neonatally to diethylstilbestrol."; RL Mol. Cell. Endocrinol. 195:99-107(2002). RN [6] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=8602273; DOI=10.1016/0168-0102(95)00960-2; RA Suzuki J., Yoshida S., Chen Z.-L., Momota Y., Kato K., Hirata A., RA Shiosaka S.; RT "Ontogeny of neuropsin mRNA expression in the mouse brain."; RL Neurosci. Res. 23:345-351(1995). RN [7] RP INDUCTION. RX PubMed=8864305; DOI=10.1016/s0006-8993(96)00473-8; RA Okabe A., Momota Y., Yoshida S., Hirata A., Ito J., Nishino H., RA Shiosaka S.; RT "Kindling induces neuropsin mRNA in the mouse brain."; RL Brain Res. 728:116-120(1996). RN [8] RP INDUCTION. RX PubMed=9374276; DOI=10.1016/s0006-8993(97)00674-4; RA Akita H., Matsuyama T., Iso H., Sugita M., Yoshida S.; RT "Effects of oxidative stress on the expression of limbic-specific protease RT neuropsin and avoidance learning in mice."; RL Brain Res. 769:86-96(1997). RN [9] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=9749739; DOI=10.1046/j.1460-9568.1998.00068.x; RA Momota Y., Yoshida S., Ito J., Shibata M., Kato K., Sakurai K., RA Matsumoto K., Shiosaka S.; RT "Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy."; RL Eur. J. Neurosci. 10:760-764(1998). RN [10] RP TISSUE SPECIFICITY. RX PubMed=9620300; DOI=10.1046/j.1523-1747.1998.00212.x; RA Inoue N., Kuwae K., Ishida-Yamamoto A., Iizuka H., Shibata M., Yoshida S., RA Kato K., Shiosaka S.; RT "Expression of neuropsin in the keratinizing epithelial tissue RT - immunohistochemical analysis of wild-type and nude mice."; RL J. Invest. Dermatol. 110:923-931(1998). RN [11] RP INDUCTION. RX PubMed=10421059; DOI=10.1007/s004030050418; RA Kitayoshi H., Inoue N., Kuwae K., Chen Z.-L., Sato H., Ohta T., RA Hosokawa K., Itami S., Yoshikawa K., Yoshida S., Shiosaka S.; RT "Effect of 12-O-tetradecanoyl-phorbol ester and incisional wounding on RT neuropsin mRNA and its protein expression in murine skin."; RL Arch. Dermatol. Res. 291:333-338(1999). RN [12] RP INDUCTION. RX PubMed=10196465; DOI=10.1016/s0006-8993(99)01238-x; RA Tomizawa K., He X.-P., Yamanaka H., Shiosaka S., Yoshida S.; RT "Injury induces neuropsin mRNA in the central nervous system."; RL Brain Res. 824:308-311(1999). RN [13] RP FUNCTION. RX PubMed=10762375; DOI=10.1046/j.1460-9568.2000.00035.x; RA Komai S., Matsuyama T., Matsumoto K., Kato K., Kobayashi M., Imamura K., RA Yoshida S., Ugawa S., Shiosaka S.; RT "Neuropsin regulates an early phase of Schaffer-collateral long-term RT potentiation in the murine hippocampus."; RL Eur. J. Neurosci. 12:1479-1486(2000). RN [14] RP DISRUPTION PHENOTYPE. RX PubMed=11549709; DOI=10.1523/jneurosci.21-18-06993.2001; RA Davies B., Kearns I.R., Ure J., Davies C.H., Lathe R.; RT "Loss of hippocampal serine protease BSP1/neuropsin predisposes to global RT seizure activity."; RL J. Neurosci. 21:6993-7000(2001). RN [15] RP DISRUPTION PHENOTYPE. RX PubMed=11273653; DOI=10.1006/mcne.2000.0945; RA Hirata A., Yoshida S., Inoue N., Matsumoto-Miyai K., Ninomiya A., RA Taniguchi M., Matsuyama T., Kato K., Iizasa H., Kataoka Y., Yoshida N., RA Shiosaka S.; RT "Abnormalities of synapses and neurons in the hippocampus of neuropsin- RT deficient mice."; RL Mol. Cell. Neurosci. 17:600-610(2001). RN [16] RP INDUCTION. RX PubMed=11274744; DOI=10.1016/s0168-0102(01)00200-0; RA He X.-P., Shiosaka S., Yoshida S.; RT "Expression of neuropsin in oligodendrocytes after injury to the CNS."; RL Neurosci. Res. 39:455-462(2001). RN [17] RP FUNCTION. RX PubMed=11880192; DOI=10.1016/s0304-3940(01)02470-3; RA Oka T., Akisada M., Okabe A., Sakurai K., Shiosaka S., Kato K.; RT "Extracellular serine protease neuropsin (KLK8) modulates neurite outgrowth RT and fasciculation of mouse hippocampal neurons in culture."; RL Neurosci. Lett. 321:141-144(2002). RN [18] RP INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=14616360; DOI=10.1046/j.1365-2133.2003.05484.x; RA Kirihara T., Matsumoto-Miyai K., Nakamura Y., Sadayama T., Yoshida S., RA Shiosaka S.; RT "Prolonged recovery of ultraviolet B-irradiated skin in neuropsin (KLK8)- RT deficient mice."; RL Br. J. Dermatol. 149:700-706(2003). RN [19] RP FUNCTION. RX PubMed=12944500; DOI=10.1523/jneurosci.23-21-07727.2003; RA Matsumoto-Miyai K., Ninomiya A., Yamasaki H., Tamura H., Nakamura Y., RA Shiosaka S.; RT "NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the RT hippocampus by neuropsin."; RL J. Neurosci. 23:7727-7736(2003). RN [20] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16537644; DOI=10.1242/jcs.02862; RA Nakamura Y., Tamura H., Horinouchi K., Shiosaka S.; RT "Role of neuropsin in formation and maturation of Schaffer-collateral RT L1cam-immunoreactive synaptic boutons."; RL J. Cell Sci. 119:1341-1349(2006). RN [21] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16308352; DOI=10.1113/jphysiol.2005.098715; RA Tamura H., Ishikawa Y., Hino N., Maeda M., Yoshida S., Kaku S., RA Shiosaka S.; RT "Neuropsin is essential for early processes of memory acquisition and RT Schaffer collateral long-term potentiation in adult mouse hippocampus in RT vivo."; RL J. Physiol. (Lond.) 570:541-551(2006). RN [22] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17761692; DOI=10.1093/jb/mvm156; RA Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.; RT "SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes."; RL J. Biochem. 142:435-442(2007). RN [23] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17182622; DOI=10.1074/jbc.m607998200; RA Kishibe M., Bando Y., Terayama R., Namikawa K., Takahashi H., Hashimoto Y., RA Ishida-Yamamoto A., Jiang Y.-P., Mitrovic B., Perez D., Iizuka H., RA Yoshida S.; RT "Kallikrein 8 is involved in skin desquamation in cooperation with other RT kallikreins."; RL J. Biol. Chem. 282:5834-5841(2007). RN [24] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17629414; DOI=10.1016/j.neuroscience.2007.05.037; RA Terayama R., Bando Y., Murakami K., Kato K., Kishibe M., Yoshida S.; RT "Neuropsin promotes oligodendrocyte death, demyelination and axonal RT degeneration after spinal cord injury."; RL Neuroscience 148:175-187(2007). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-257. RC TISSUE=Hippocampus; RX PubMed=9933620; DOI=10.1074/jbc.274.7.4220; RA Kishi T., Kato M., Shimizu T., Kato K., Matsumoto K., Yoshida S., RA Shiosaka S., Hakoshima T.; RT "Crystal structure of neuropsin, a hippocampal protease involved in RT kindling epileptogenesis."; RL J. Biol. Chem. 274:4220-4224(1999). CC -!- FUNCTION: Serine protease which is capable of degrading a number of CC proteins such as casein, fibrinogen, kininogen, fibronectin and CC collagen type IV. Also cleaves L1CAM in response to increased neural CC activity. Induces neurite outgrowth and fasciculation of cultured CC hippocampal neurons. Plays a role in the formation and maturation of CC orphan and small synaptic boutons in the Schaffer-collateral pathway, CC regulates Schaffer-collateral long-term potentiation in the hippocampus CC and is required for memory acquisition and synaptic plasticity. CC Involved in skin desquamation and keratinocyte proliferation. Plays a CC role in the secondary phase of pathogenesis following spinal cord CC injury. {ECO:0000269|PubMed:10762375, ECO:0000269|PubMed:11880192, CC ECO:0000269|PubMed:12944500, ECO:0000269|PubMed:16308352, CC ECO:0000269|PubMed:16537644, ECO:0000269|PubMed:17182622, CC ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:9556608}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of amide substrates following the basic amino acids CC Arg or Lys at the P1 position, with a preference for Arg over Lys.; CC EC=3.4.21.118; CC -!- ACTIVITY REGULATION: Strongly inhibited by diisopropyl fluorophosphate, CC leupeptin and (4-amidinophenyl)methanesulfonyl 1-fluoride. CC {ECO:0000269|PubMed:9556608}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=300 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:9556608}; CC KM=540 uM for Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:9556608}; CC KM=280 uM for D-Val-Leu-Arg-MCA {ECO:0000269|PubMed:9556608}; CC -!- SUBUNIT: Interacts with SPINK9. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Shows a cytoplasmic CC distribution in the keratinocytes. CC -!- TISSUE SPECIFICITY: Expressed in the limbic system of mouse brain and CC is localized at highest concentration in pyramidal neurons of the CC hippocampal CA1-3 subfields. Also detected in spinal cord gray matter CC and in keratinized stratified epithelia of epidermis, hair, tongue, CC palate, nasal cavity, pharynges, esophagus and forestomach. In skin and CC mucus membranes, expressed in stratum spinosum and stratum granulosum. CC Expressed during estrus in vaginal epithelial cells but not stromal CC cells. Within the vaginal epithelium, expressed in prickle cells, CC granular cells and parakeratotic cells but not in basal cells. Not CC expressed in uterus. Expressed in the keratinocytes. CC {ECO:0000269|PubMed:12354676, ECO:0000269|PubMed:17629414, CC ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:7623137, CC ECO:0000269|PubMed:8602273, ECO:0000269|PubMed:9620300, CC ECO:0000269|PubMed:9749739}. CC -!- DEVELOPMENTAL STAGE: Expression is detected in the brain from embryonic CC day 12 and continues into adulthood. {ECO:0000269|PubMed:8602273}. CC -!- INDUCTION: By chemical/incision-induced brain injury which leads to CC increased expression in axon fiber bundles of the peri-lesioned region, CC by electrically-induced seizure (kindling) in brain, by UV irradiation CC in skin and by incisional and chemically-induced skin wounding which CC causes epidermal proliferation and hyperkeratosis. Induced by CC chemically-induced oxidative stress which leads to increased expression CC in the hippocampal pyramidal neurons 2 hours after treatment. Levels CC then decrease, drop to 60% of pretreated control levels at day 7 when CC avoidance learning is impaired and return to control levels at day 30. CC Also induced by spinal crush injury which leads to increased expression CC in spinal cord white matter adjacent to the lesion. Expression CC increases between days 1-14 post-injury with a peak at day 4. CC {ECO:0000269|PubMed:10196465, ECO:0000269|PubMed:10421059, CC ECO:0000269|PubMed:11274744, ECO:0000269|PubMed:14616360, CC ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:8864305, CC ECO:0000269|PubMed:9374276, ECO:0000269|PubMed:9749739}. CC -!- MASS SPECTROMETRY: Mass=26229; Method=MALDI; CC Evidence={ECO:0000269|PubMed:9556608}; CC -!- DISRUPTION PHENOTYPE: Mice display marked abnormalities of synapses and CC neurons in the CA1 subfield of the hippocampus with enlarged and CC elongated pyramidal cell soma and reduced asymmetrical synapse numbers. CC Mutants also display impaired spatial memory acquisition, increased CC hippocampal susceptibility to hyperexcitability in response to CC repetitive afferent stimulation and prolonged recovery of UV-irradiated CC skin. Following spinal cord injury, mutants display reduced CC demyelination, oligodendrocyte death and axonal degeneration, and CC inproved hind limb recovery, suggesting that attenuation of neuropsin CC activity may be beneficial in the treatment of spinal cord injury. CC Blocking of Klk8 activity by intraventricular injection with monoclonal CC antibodies reduces or eliminates epileptic seizures in kindled mice. CC {ECO:0000269|PubMed:11273653, ECO:0000269|PubMed:11549709, CC ECO:0000269|PubMed:14616360, ECO:0000269|PubMed:16308352, CC ECO:0000269|PubMed:16537644, ECO:0000269|PubMed:17182622, CC ECO:0000269|PubMed:17629414}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D30785; BAA06451.1; -; mRNA. DR EMBL; AB032202; BAA92435.1; -; Genomic_DNA. DR EMBL; BC055895; AAH55895.1; -; mRNA. DR EMBL; AB074296; BAB92021.1; -; mRNA. DR CCDS; CCDS21182.1; -. DR PIR; I56559; I56559. DR RefSeq; NP_001311327.1; NM_001324398.1. DR RefSeq; NP_032966.1; NM_008940.3. DR PDB; 1NPM; X-ray; 2.10 A; A/B=33-257. DR PDBsum; 1NPM; -. DR AlphaFoldDB; Q61955; -. DR SMR; Q61955; -. DR BioGRID; 234416; 2. DR STRING; 10090.ENSMUSP00000082588; -. DR MEROPS; S01.244; -. DR GlyCosmos; Q61955; 1 site, No reported glycans. DR GlyGen; Q61955; 1 site. DR iPTMnet; Q61955; -. DR PhosphoSitePlus; Q61955; -. DR EPD; Q61955; -. DR PaxDb; 10090-ENSMUSP00000082588; -. DR ProteomicsDB; 263661; -. DR Antibodypedia; 32417; 1500 antibodies from 32 providers. DR DNASU; 259277; -. DR Ensembl; ENSMUST00000085461.4; ENSMUSP00000082588.3; ENSMUSG00000064023.5. DR GeneID; 259277; -. DR KEGG; mmu:259277; -. DR UCSC; uc009gns.1; mouse. DR AGR; MGI:1343327; -. DR CTD; 11202; -. DR MGI; MGI:1343327; Klk8. DR VEuPathDB; HostDB:ENSMUSG00000064023; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01020000230389; -. DR HOGENOM; CLU_006842_1_1_1; -. DR InParanoid; Q61955; -. DR OMA; GMTCYSG; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q61955; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.118; 3474. DR Reactome; R-MMU-6809371; Formation of the cornified envelope. DR BioGRID-ORCS; 259277; 3 hits in 79 CRISPR screens. DR ChiTaRS; Klk1b8; mouse. DR EvolutionaryTrace; Q61955; -. DR PRO; PR:Q61955; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q61955; Protein. DR Bgee; ENSMUSG00000064023; Expressed in lip and 175 other cell types or tissues. DR ExpressionAtlas; Q61955; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0097180; C:serine protease inhibitor complex; ISO:MGI. DR GO; GO:0008233; F:peptidase activity; IDA:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0043616; P:keratinocyte proliferation; IMP:UniProtKB. DR GO; GO:0007613; P:memory; IMP:UniProtKB. DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0050807; P:regulation of synapse organization; IMP:UniProtKB. DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB. DR GO; GO:0050808; P:synapse organization; IMP:MGI. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24271:SF62; KALLIKREIN-8; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; Q61955; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT PROPEP 29..32 FT /evidence="ECO:0000269|PubMed:9556608" FT /id="PRO_0000027948" FT CHAIN 33..260 FT /note="Kallikrein-8" FT /id="PRO_0000027949" FT DOMAIN 33..257 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 73 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 120 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 212 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 39..173 FT DISULFID 58..74 FT DISULFID 145..246 FT DISULFID 152..218 FT DISULFID 184..198 FT DISULFID 208..233 FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 55..64 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:1NPM" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 122..128 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:1NPM" FT HELIX 181..187 FT /evidence="ECO:0007829|PDB:1NPM" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 221..228 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1NPM" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1NPM" FT HELIX 245..256 FT /evidence="ECO:0007829|PDB:1NPM" SQ SEQUENCE 260 AA; 28524 MW; BE5F6F6BE37CD60E CRC64; MGRPPPCAIQ PWILLLLFMG AWAGLTRAQG SKILEGRECI PHSQPWQAAL FQGERLICGG VLVGDRWVLT AAHCKKQKYS VRLGDHSLQS RDQPEQEIQV AQSIQHPCYN NSNPEDHSHD IMLIRLQNSA NLGDKVKPVQ LANLCPKVGQ KCIISGWGTV TSPQENFPNT LNCAEVKIYS QNKCERAYPG KITEGMVCAG SSNGADTCQG DSGGPLVCDG MLQGITSWGS DPCGKPEKPG VYTKICRYTT WIKKTMDNRD //