HPSE_MOUSE
ID HPSE_MOUSE Reviewed; 535 AA.
AC Q6YGZ1; B2RS99; Q8K3K3;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Heparanase;
DE EC=3.2.1.166;
DE AltName: Full=Endo-glucoronidase;
DE Contains:
DE RecName: Full=Heparanase 8 kDa subunit;
DE Contains:
DE RecName: Full=Heparanase 50 kDa subunit;
DE Flags: Precursor;
GN Name=Hpse; Synonyms=Hpa;
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].
RC STRAIN=SJL/J; TISSUE=Spleen;
RX PubMed=10395326; DOI=10.1038/10525;
RA Hulett M.D., Freeman C., Hamdorf B.J., Baker R.T., Harris M.J.,
RA Parish C.R.;
RT "Cloning of mammalian heparanase, an important enzyme in tumor invasion and
RT metastasis.";
RL Nat. Med. 5:803-809(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-57 AND 150-179,
RP GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBUNIT.
RC STRAIN=FVB/NJ; TISSUE=Embryo;
RX PubMed=12460766; DOI=10.1016/s1046-5928(02)00558-2;
RA Miao H.-Q., Navarro E., Patel S., Sargent D., Koo H., Wan H., Plata A.,
RA Zhou Q., Ludwig D., Bohlen P., Kussie P.;
RT "Cloning, expression, and purification of mouse heparanase.";
RL Protein Expr. Purif. 26:425-431(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACTIVITY REGULATION.
RX PubMed=12837765; DOI=10.1074/jbc.m300925200;
RA Gong F., Jemth P., Galvis M.L.E., Vlodavsky I., Horner A., Lindahl U.,
RA Li J.-P.;
RT "Processing of macromolecular heparin by heparanase.";
RL J. Biol. Chem. 278:35152-35158(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15793281; DOI=10.1016/s0002-9440(10)62321-8;
RA Zcharia E., Philp D., Edovitsky E., Aingorn H., Metzger S., Kleinman H.K.,
RA Vlodavsky I., Elkin M.;
RT "Heparanase regulates murine hair growth.";
RL Am. J. Pathol. 166:999-1008(2005).
RN [7]
RP FUNCTION, ENZYMATIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15677344; DOI=10.1096/fj.04-1970com;
RA Zcharia E., Zilka R., Yaar A., Yacoby-Zeevi O., Zetser A., Metzger S.,
RA Sarid R., Naggi A., Casu B., Ilan N., Vlodavsky I., Abramovitch R.;
RT "Heparanase accelerates wound angiogenesis and wound healing in mouse and
RT rat models.";
RL FASEB J. 19:211-221(2005).
RN [8]
RP FUNCTION.
RX PubMed=17689495; DOI=10.1016/j.bbrc.2007.06.188;
RA Ben-Zaken O., Gingis-Velitski S., Vlodavsky I., Ilan N.;
RT "Heparanase induces Akt phosphorylation via a lipid raft receptor.";
RL Biochem. Biophys. Res. Commun. 361:829-834(2007).
RN [9]
RP FUNCTION, ENZYMATIC ACTIVITY, PROTEOLYTIC PROCESSING, AND TISSUE
RP SPECIFICITY.
RX PubMed=18589009; DOI=10.1016/j.bone.2008.05.022;
RA Brown A.J., Alicknavitch M., D'Souza S.S., Daikoku T., Kirn-Safran C.B.,
RA Marchetti D., Carson D.D., Farach-Carson M.C.;
RT "Heparanase expression and activity influences chondrogenic and osteogenic
RT processes during endochondral bone formation.";
RL Bone 43:689-699(2008).
CC -!- FUNCTION: Endoglycosidase that cleaves heparan sulfate proteoglycans
CC (HSPGs) into heparan sulfate side chains and core proteoglycans.
CC Participates in extracellular matrix (ECM) degradation and remodeling.
CC Selectively cleaves the linkage between a glucuronic acid unit and an
CC N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo
CC group. Can also cleave the linkage between a glucuronic acid unit and
CC an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not
CC linkages between a glucuronic acid unit and a 2-O-sulfated iduronic
CC acid moiety. It is essentially inactive at neutral pH but becomes
CC active under acidic conditions such as during tumor invasion and in
CC inflammatory processes. Facilitates cell migration associated with
CC metastasis, wound healing and inflammation. Enhances shedding of
CC syndecans, and increases endothelial invasion and angiogenesis in
CC myelomas. Acts as procoagulant by increasing the generation of
CC activation factor X in the presence of tissue factor and activation
CC factor VII. Increases cell adhesion to the extracellular matrix (ECM),
CC independent of its enzymatic activity. Induces AKT1/PKB phosphorylation
CC via lipid rafts increasing cell mobility and invasion. Heparin
CC increases this AKT1/PKB activation. Regulates osteogenesis. Enhances
CC angiogenesis through up-regulation of SRC-mediated activation of VEGF.
CC Implicated in hair follicle inner root sheath differentiation and hair
CC homeostasis. {ECO:0000269|PubMed:15677344, ECO:0000269|PubMed:15793281,
CC ECO:0000269|PubMed:17689495, ECO:0000269|PubMed:18589009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan
CC sulfate chains in heparan sulfate proteoglycan.; EC=3.2.1.166;
CC Evidence={ECO:0000269|PubMed:15677344, ECO:0000269|PubMed:18589009};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and activated by calcium and
CC magnesium (By similarity). Inhibited by laminarin sulfate and, to a
CC lower extent, by heparin and sulfamin. {ECO:0000250,
CC ECO:0000269|PubMed:12460766, ECO:0000269|PubMed:12837765}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:12460766};
CC -!- SUBUNIT: Heterodimer; heterodimer formation between the 8 kDa and the
CC 50 kDa subunits is required for enzyme activity. Interacts with TF; the
CC interaction, inhibited by heparin, enhances the generation of activated
CC factor X and activates coagulation. Interacts with HRG; the interaction
CC is enhanced at acidic pH, partially inhibits binding of HPSE to cell
CC surface receptors and modulates its enzymatic activity. Interacts with
CC SDC1; the interaction enhances the shedding of SDC1 (By similarity).
CC Interacts with HPSE2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:15793281}.
CC Nucleus {ECO:0000269|PubMed:15793281}. Note=Proheparanase is secreted
CC via vesicles of the Golgi. Interacts with cell membrane heparan sulfate
CC proteoglycans (HSPGs). Endocytosed and accumulates in endosomes.
CC Transferred to lysosomes where it is proteolytically cleaved to produce
CC the active enzyme. Under certain stimuli, transferred to the cell
CC surface. Colocalizes with SDC1 in endosomal/lysosomal vesicles.
CC Accumulates in perinuclear lysosomal vesicles. Heparin retains
CC proheparanase in the extracellular medium (By similarity). Associates
CC with lipid rafts. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in skin, mainly in the stratum granulosum
CC and the first layer of the stratum corneum in the upper part of the
CC epidermis. Also detected in hair follicles and in sebaceous glands.
CC {ECO:0000269|PubMed:15793281, ECO:0000269|PubMed:18589009}.
CC -!- DEVELOPMENTAL STAGE: In 18.5 day embryos, expressed in the peri-
CC chondrium, periosteum and at the chondro-osseus junction of developing
CC bone. {ECO:0000269|PubMed:15677344}.
CC -!- PTM: Proteolytically processed. The cleavage of the 65 kDa form leads
CC to the generation of a linker peptide, and the 8 kDa and 50 kDa
CC products. The active form, the 8/50 kDa heterodimer, is resistant to
CC degradation. Complete removal of the linker peptide appears to be a
CC prerequisite to the complete activation of the enzyme (By similarity).
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. Glycosylation of the 50 kDa subunit appears to be
CC essential for its solubility. {ECO:0000269|PubMed:12460766}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
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DR EMBL; AF359507; AAQ15188.1; -; mRNA.
DR EMBL; AY077467; AAL76083.1; -; mRNA.
DR EMBL; AY151051; AAN41636.1; -; mRNA.
DR EMBL; AK040471; BAC30600.1; -; mRNA.
DR EMBL; AK154628; BAE32725.1; -; mRNA.
DR EMBL; BC138782; AAI38783.1; -; mRNA.
DR EMBL; BC138784; AAI38785.1; -; mRNA.
DR CCDS; CCDS19466.1; -.
DR RefSeq; NP_690016.1; NM_152803.5.
DR AlphaFoldDB; Q6YGZ1; -.
DR SMR; Q6YGZ1; -.
DR ComplexPortal; CPX-363; Heparanase complex.
DR STRING; 10090.ENSMUSP00000044072; -.
DR BindingDB; Q6YGZ1; -.
DR ChEMBL; CHEMBL4295872; -.
DR CAZy; GH79; Glycoside Hydrolase Family 79.
DR GlyGen; Q6YGZ1; 3 sites.
DR iPTMnet; Q6YGZ1; -.
DR PhosphoSitePlus; Q6YGZ1; -.
DR EPD; Q6YGZ1; -.
DR MaxQB; Q6YGZ1; -.
DR PaxDb; Q6YGZ1; -.
DR PRIDE; Q6YGZ1; -.
DR ProteomicsDB; 267016; -.
DR ABCD; Q6YGZ1; 8 sequenced antibodies.
DR Antibodypedia; 4072; 562 antibodies from 34 providers.
DR DNASU; 15442; -.
DR Ensembl; ENSMUST00000045617; ENSMUSP00000044072; ENSMUSG00000035273.
DR GeneID; 15442; -.
DR KEGG; mmu:15442; -.
DR UCSC; uc008yhw.1; mouse.
DR CTD; 10855; -.
DR MGI; MGI:1343124; Hpse.
DR VEuPathDB; HostDB:ENSMUSG00000035273; -.
DR eggNOG; ENOG502QQST; Eukaryota.
DR GeneTree; ENSGT00390000004874; -.
DR HOGENOM; CLU_021823_0_1_1; -.
DR InParanoid; Q6YGZ1; -.
DR OMA; SGFMWLD; -.
DR OrthoDB; 1132327at2759; -.
DR PhylomeDB; Q6YGZ1; -.
DR TreeFam; TF328999; -.
DR BRENDA; 3.2.1.166; 3474.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 15442; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Hpse; mouse.
DR PRO; PR:Q6YGZ1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6YGZ1; protein.
DR Bgee; ENSMUSG00000035273; Expressed in iris and 152 other tissues.
DR ExpressionAtlas; Q6YGZ1; baseline and differential.
DR Genevisible; Q6YGZ1; MM.
DR GO; GO:0005776; C:autophagosome; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1904974; C:heparanase complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030305; F:heparanase activity; IDA:MGI.
DR GO; GO:0045545; F:syndecan binding; ISO:MGI.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IDA:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; IDA:MGI.
DR GO; GO:0002542; P:Factor XII activation; ISO:MGI.
DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; ISS:UniProtKB.
DR GO; GO:0030202; P:heparin metabolic process; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IC:ComplexPortal.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IDA:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:0071806; P:protein transmembrane transport; IMP:MGI.
DR GO; GO:0051797; P:regulation of hair follicle development; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0061042; P:vascular wound healing; IDA:UniProtKB.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR InterPro; IPR005199; Glyco_hydro_79.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF03662; Glyco_hydro_79n; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Magnesium; Membrane; Nucleus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..101
FT /note="Heparanase 8 kDa subunit"
FT /id="PRO_0000042263"
FT PROPEP 102..149
FT /note="Linker peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042264"
FT CHAIN 150..535
FT /note="Heparanase 50 kDa subunit"
FT /id="PRO_0000042265"
FT REGION 280..409
FT /note="Required for heterodimerization with the heparanase
FT 8 kDa subunit"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT REGION 519..535
FT /note="Required for transferring proheparanase to the Golgi
FT apparatus, secretion and subsequent enzyme activity and for
FT enhancement of PKB/AKT1 phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 54..56
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 89
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 150..154
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 262..272
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 288
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 295
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 340..342
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 381..383
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT DISULFID 119..171
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT DISULFID 429..534
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CONFLICT 206
FT /note="K -> R (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="W -> S (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..232
FT /note="DGL -> NGS (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="E -> K (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="G -> A (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="H -> Y (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="I -> V (in Ref. 3; AAN41636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 60066 MW; 6E73A8302FB8A0DF CRC64;
MLRLLLLWLW GPLGALAQGA PAGTAPTDDV VDLEFYTKRP LRSVSPSFLS ITIDASLATD
PRFLTFLGSP RLRALARGLS PAYLRFGGTK TDFLIFDPDK EPTSEERSYW KSQVNHDICR
SEPVSAAVLR KLQVEWPFQE LLLLREQYQK EFKNSTYSRS SVDMLYSFAK CSGLDLIFGL
NALLRTPDLR WNSSNAQLLL DYCSSKGYNI SWELGNEPNS FWKKAHILID GLQLGEDFVE
LHKLLQRSAF QNAKLYGPDI GQPRGKTVKL LRSFLKAGGE VIDSLTWHHY YLNGRIATKE
DFLSSDVLDT FILSVQKILK VTKEITPGKK VWLGETSSAY GGGAPLLSNT FAAGFMWLDK
LGLSAQMGIE VVMRQVFFGA GNYHLVDENF EPLPDYWLSL LFKKLVGPRV LLSRVKGPDR
SKLRVYLHCT NVYHPRYQEG DLTLYVLNLH NVTKHLKVPP PLFRKPVDTY LLKPSGPDGL
LSKSVQLNGQ ILKMVDEQTL PALTEKPLPA GSALSLPAFS YGFFVIRNAK IAACI
