KLK8_MOUSE
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 03-AUG-2022, entry version 168.
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}.
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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 GlyGen; Q61955; 1 site.
DR iPTMnet; Q61955; -.
DR PhosphoSitePlus; Q61955; -.
DR EPD; Q61955; -.
DR PaxDb; Q61955; -.
DR PRIDE; Q61955; -.
DR ProteomicsDB; 263661; -.
DR Antibodypedia; 32417; 1304 antibodies from 32 providers.
DR DNASU; 259277; -.
DR Ensembl; ENSMUST00000085461; ENSMUSP00000082588; ENSMUSG00000064023.
DR GeneID; 259277; -.
DR KEGG; mmu:259277; -.
DR UCSC; uc009gns.1; mouse.
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; GQECKPH; -.
DR OrthoDB; 1314811at2759; -.
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 74 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 173 other tissues.
DR ExpressionAtlas; Q61955; baseline and differential.
DR Genevisible; Q61955; MM.
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:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; 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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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
