ID   HPSE3_ARATH             Reviewed;         536 AA.
AC   Q9FZP1; O82604; O82605; Q0WP10;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Heparanase-like protein 3;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g34940; ORFNames=MGG23.2, T2L5.6, T2L5.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoglycosidase which is a cell surface and extracellular
CC       matrix-degrading enzyme. Cleaves heparan sulfate proteoglycans (HSPGs)
CC       into heparan sulfate side chains and core proteoglycans (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FZP1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FZP1-2; Sequence=VSP_018141, VSP_018142;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62790.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAC62794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB10787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF096371; AAC62790.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF096371; AAC62794.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB028613; BAB10787.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED93923.1; -; Genomic_DNA.
DR   EMBL; AK229275; BAF01139.1; -; mRNA.
DR   PIR; T01953; T01953.
DR   PIR; T01954; T01954.
DR   RefSeq; NP_851093.1; NM_180762.3. [Q9FZP1-1]
DR   AlphaFoldDB; Q9FZP1; -.
DR   SMR; Q9FZP1; -.
DR   BioGRID; 18694; 1.
DR   STRING; 3702.AT5G34940.2; -.
DR   CAZy; GH79; Glycoside Hydrolase Family 79.
DR   iPTMnet; Q9FZP1; -.
DR   PaxDb; Q9FZP1; -.
DR   PRIDE; Q9FZP1; -.
DR   ProteomicsDB; 232174; -. [Q9FZP1-1]
DR   EnsemblPlants; AT5G34940.2; AT5G34940.2; AT5G34940. [Q9FZP1-1]
DR   GeneID; 833437; -.
DR   Gramene; AT5G34940.2; AT5G34940.2; AT5G34940. [Q9FZP1-1]
DR   KEGG; ath:AT5G34940; -.
DR   Araport; AT5G34940; -.
DR   TAIR; locus:2183542; AT5G34940.
DR   eggNOG; ENOG502QQST; Eukaryota.
DR   InParanoid; Q9FZP1; -.
DR   OrthoDB; 1132327at2759; -.
DR   PhylomeDB; Q9FZP1; -.
DR   BioCyc; ARA:AT5G34940-MON; -.
DR   PRO; PR:Q9FZP1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FZP1; baseline and differential.
DR   Genevisible; Q9FZP1; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004566; F:beta-glucuronidase activity; ISS:TAIR.
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   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Lysosome; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..536
FT                   /note="Heparanase-like protein 3"
FT                   /id="PRO_0000042271"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         382
FT                   /note="S -> R (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018141"
FT   VAR_SEQ         383..536
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018142"
SQ   SEQUENCE   536 AA;  59709 MW;  BBD6C47CA17DF1C7 CRC64;
     MAYRQILAIV LFLCVFQFLD CTVSSAVEEN GTVFVYGRAA VGTIDEDFIC ATLDWWPPEK
     CDYGSCSWDH ASILNLDLNN VILQNAIKAF APLKIRIGGT LQDIVIYETP DSKQPCLPFT
     KNSSILFGYT QGCLPMRRWD ELNAFFRKTG TKVIFGLNAL SGRSIKSNGE AIGAWNYTNA
     ESFIRFTAEN NYTIDGWELG NELCGSGVGA RVGANQYAID TINLRNIVNR VYKNVSPMPL
     VIGPGGFFEV DWFTEYLNKA ENSLNATTRH IYDLGPGVDE HLIEKILNPS YLDQEAKSFR
     SLKNIIKNSS TKAVAWVGES GGAYNSGRNL VSNAFVYSFW YLDQLGMASL YDTKTYCRQS
     LIGGNYGLLN TTNFTPNPDY YSALIWRQLM GRKALFTTFS GTKKIRSYTH CARQSKGITV
     LLMNLDNTTT VVAKVELNNS FSLRHTKHMK SYKRASSQLF GGPNGVIQRE EYHLTAKDGN
     LHSQTMLLNG NALQVNSMGD LPPIEPIHIN STEPITIAPY SIVFVHMRNV VVPACA