HPSE_CHICK
ID HPSE_CHICK Reviewed; 523 AA.
AC Q90YK5;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Heparanase;
DE EC=3.2.1.166;
DE Flags: Precursor;
GN Name=HPSE; Synonyms=HPA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, ENZYME ACTIVITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11387326; DOI=10.1074/jbc.m102462200;
RA Goldshmidt O., Zcharia E., Aingorn H., Guatta-Rangini Z., Atzmon R.,
RA Michal I., Pecker I., Mitrani E., Vlodavsky I.;
RT "Expression pattern and secretion of human and chicken heparanase are
RT determined by their signal peptide sequence.";
RL J. Biol. Chem. 276:29178-29187(2001).
RN [2]
RP FUNCTION.
RX PubMed=12773484; DOI=10.1096/fj.02-0773com;
RA Goldshmidt O., Zcharia E., Cohen M., Aingorn H., Cohen I., Nadav L.,
RA Katz B.Z., Geiger B., Vlodavsky I.;
RT "Heparanase mediates cell adhesion independent of its enzymatic activity.";
RL FASEB J. 17:1015-1025(2003).
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 (By similarity). Increases cell adhesion to the
CC extracellular matrix (ECM), independent of its enzymatic activity.
CC {ECO:0000250, ECO:0000269|PubMed:12773484}.
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:11387326};
CC -!- SUBUNIT: Heterodimer; the active enzyme is a heterodimer of the 60 kDa
CC and 45 kDa proteolytic products. {ECO:0000269|PubMed:11387326}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11387326}.
CC Note=Localized close to cell surface.
CC -!- DEVELOPMENTAL STAGE: Expressed, as early as 12 hours post
CC fertilization, in cells migrating from the epiblast and forming the
CC hypoblast layer. Later on at 72 h, preferentially expressed in cells of
CC the developing vascular and nervous systems.
CC {ECO:0000269|PubMed:11387326}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved to produce a 60 kDa and a 45 kDa product.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
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; AY037007; AAK82648.1; -; mRNA.
DR RefSeq; NP_989498.1; NM_204167.1.
DR AlphaFoldDB; Q90YK5; -.
DR SMR; Q90YK5; -.
DR STRING; 9031.ENSGALP00000018245; -.
DR CAZy; GH79; Glycoside Hydrolase Family 79.
DR PaxDb; Q90YK5; -.
DR GeneID; 373981; -.
DR KEGG; gga:373981; -.
DR CTD; 10855; -.
DR VEuPathDB; HostDB:geneid_373981; -.
DR eggNOG; ENOG502QQST; Eukaryota.
DR InParanoid; Q90YK5; -.
DR OrthoDB; 1132327at2759; -.
DR PhylomeDB; Q90YK5; -.
DR PRO; PR:Q90YK5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030305; F:heparanase activity; ISS:UniProtKB.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; ISS: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 Cell adhesion; Disulfide bond; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..523
FT /note="Heparanase"
FT /id="PRO_0000042259"
FT REGION 268..397
FT /note="Required for heterodimerization with the heparanase
FT 8 kDa subunit"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT REGION 507..523
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 204
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 42..44
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 77
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 137..141
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 250..260
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 276
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 283
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 328..330
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT BINDING 369..371
FT /ligand="heparan sulfate group"
FT /ligand_id="ChEBI:CHEBI:157750"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
FT DISULFID 417..522
FT /evidence="ECO:0000250|UniProtKB:Q9Y251"
SQ SEQUENCE 523 AA; 58386 MW; 8EB0B7B18C9BF881 CRC64;
MLVLLLLVLL LAVPPRRTAE LQLGLREPIG AVSPAFLSLT LDASLARDPR FVALLRHPKL
HTLASGLSPG FLRFGGTSTD FLIFNPNKDS TWEEKVLSEF QAKDVCEAWP SFAVVPKLLL
TQWPLQEKLL LAEHSWKKHK NTTITRSTLD ILHTFASSSG FRLVFGLNAL LRRAGLQWDS
SNAKQLLGYC AQRSYNISWE LGNEPNSFRK KSGICIDGFQ LGRDFVHLRQ LLSQHPLYRH
AELYGLDVGQ PRKHTQHLLR SFMKSGGKAI DSVTWHHYYV NGRSATREDF LSPEVLDSFA
TAIHDVLGIV EATVPGKKVW LGETGSAYGG GAPQLSNTYV AGFMWLDKLG LAARRGIDVV
MRQVSFGAGS YHLVDAGFKP LPDYWLSLLY KRLVGTRVLQ ASVEQADARR PRVYLHCTNP
RHPKYREGDV TLFALNLSNV TQSLQLPKQL WSKSVDQYLL LPHGKDSILS REVQLNGRLL
QMVDDETLPA LHEMALAPGS TLGLPAFSYG FYVIRNAKAI ACI
