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Inactive heparanase-2 (Hpa2)

 HPSE2_HUMAN             Reviewed;         592 AA.
Q8WWQ2; Q5VUH4; Q5VUH5; Q5VUH6; Q8WWQ1; Q9HB37; Q9HB38; Q9HB39;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 3.
25-OCT-2017, entry version 120.
RecName: Full=Inactive heparanase-2;
Short=Hpa2;
Flags: Precursor;
Name=HPSE2; Synonyms=HPA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), VARIANT PHE-579, AND
TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=11027606; DOI=10.1006/bbrc.2000.3586;
McKenzie E., Tyson K., Stamps A., Smith P., Turner P., Barry R.,
Hircock M., Patel S., Barry E., Stubberfield C., Terrett J., Page M.;
"Cloning and expression profiling of Hpa2, a novel mammalian
heparanase family member.";
Biochem. Biophys. Res. Commun. 276:1170-1177(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT PHE-579.
TISSUE=Prostate;
Legoux P., Legoux R., O'Brien D., Salome M.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
INVOLVEMENT IN UFS1.
PubMed=20560209; DOI=10.1016/j.ajhg.2010.04.016;
Pang J., Zhang S., Yang P., Hawkins-Lee B., Zhong J., Zhang Y.,
Ochoa B., Agundez J.A., Voelckel M.A., Fisher R.B., Gu W., Xiong W.C.,
Mei L., She J.X., Wang C.Y.;
"Loss-of-function mutations in HPSE2 cause the autosomal recessive
urofacial syndrome.";
Am. J. Hum. Genet. 86:957-962(2010).
[5]
ERRATUM.
Pang J., Zhang S., Yang P., Hawkins-Lee B., Zhong J., Zhang Y.,
Ochoa B., Agundez J.A., Voelckel M.A., Fisher R.B., Gu W., Xiong W.C.,
Mei L., She J.X., Wang C.Y.;
Am. J. Hum. Genet. 87:161-161(2010).
[6]
INVOLVEMENT IN UFS1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20560210; DOI=10.1016/j.ajhg.2010.05.006;
Daly S.B., Urquhart J.E., Hilton E., McKenzie E.A., Kammerer R.A.,
Lewis M., Kerr B., Stuart H., Donnai D., Long D.A., Burgu B.,
Aydogdu O., Derbent M., Garcia-Minaur S., Reardon W., Gener B.,
Shalev S., Smith R., Woolf A.S., Black G.C., Newman W.G.;
"Mutations in HPSE2 cause urofacial syndrome.";
Am. J. Hum. Genet. 86:963-969(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HPSE, AND ABSENCE OF
HEPARANASE ACTIVITY.
PubMed=20576607; DOI=10.1074/jbc.M110.116384;
Levy-Adam F., Feld S., Cohen-Kaplan V., Shteingauz A., Gross M.,
Arvatz G., Naroditsky I., Ilan N., Doweck I., Vlodavsky I.;
"Heparanase 2 interacts with heparan sulfate with high affinity and
inhibits heparanase activity.";
J. Biol. Chem. 285:28010-28019(2010).
-!- FUNCTION: Binds heparin and heparan sulfate with high affinity,
but lacks heparanase activity. Inhibits HPSE, possibly by
competing for its substrates (in vitro).
{ECO:0000269|PubMed:20576607}.
-!- SUBUNIT: Interacts with HPSE. Interacts with SDC1 (via glycan
chains). {ECO:0000269|PubMed:20576607}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:20576607}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=HPA2c;
IsoId=Q8WWQ2-1; Sequence=Displayed;
Name=2;
IsoId=Q8WWQ2-2; Sequence=VSP_015852, VSP_015853;
Name=3; Synonyms=HPA2b;
IsoId=Q8WWQ2-3; Sequence=VSP_015851;
Name=4; Synonyms=HPA2a;
IsoId=Q8WWQ2-4; Sequence=VSP_015850;
-!- TISSUE SPECIFICITY: Widely expressed, with the highest expression
in brain, mammary gland, prostate, small intestine, testis and
uterus. In the central nervous system, expressed in the spinal
chord, caudate nucleus, thalamus, substantia nigra, medulla
oblongata, putamen and pons. In the urinary bladder, expressed in
longitudinal and circular layers of detrusor muscle. Found both in
normal and cancer tissues. {ECO:0000269|PubMed:11027606,
ECO:0000269|PubMed:20560210}.
-!- DEVELOPMENTAL STAGE: Expressed in the developing forebrain,
diencephalon, midbrain, hind brain and spinal cord at Carnagie
stage 16 (CS16, 6 weeks of gestation) and CS21 (8 weeks).
{ECO:0000269|PubMed:20560210}.
-!- DISEASE: Urofacial syndrome 1 (UFS1) [MIM:236730]: A rare
autosomal recessive disorder characterized by facial grimacing
when attempting to smile and failure of the urinary bladder to
void completely despite a lack of anatomical bladder outflow
obstruction or overt neurological damage. Affected individuals
often have reflux of infected urine from the bladder to the upper
renal tract, with a risk of kidney damage and renal failure.
{ECO:0000269|PubMed:20560209, ECO:0000269|PubMed:20560210}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF282885; AAG23421.1; -; mRNA.
EMBL; AF282886; AAG23422.1; -; mRNA.
EMBL; AF282887; AAG23423.1; -; mRNA.
EMBL; AJ299719; CAC82491.1; -; mRNA.
EMBL; AJ299720; CAC82492.1; -; mRNA.
EMBL; AL590036; CAH73137.1; -; Genomic_DNA.
EMBL; AL139243; CAH73137.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH73137.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH73137.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH73137.1; JOINED; Genomic_DNA.
EMBL; AL139243; CAI14146.1; -; Genomic_DNA.
EMBL; AL356220; CAI14146.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI14146.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI14146.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI14146.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH70448.1; -; Genomic_DNA.
EMBL; AL139243; CAH70448.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH70448.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH70448.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAH70448.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI16472.1; -; Genomic_DNA.
EMBL; AL139243; CAI16472.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI16472.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI16472.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI16472.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI17160.1; -; Genomic_DNA.
EMBL; AL139243; CAI17160.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI17160.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI17160.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI17160.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAH73139.1; -; Genomic_DNA.
EMBL; AL139243; CAH73139.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH73139.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH73139.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH73139.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI17162.1; -; Genomic_DNA.
EMBL; AL356268; CAI17162.1; JOINED; Genomic_DNA.
EMBL; AL139243; CAI17162.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI17162.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI17162.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH70450.1; -; Genomic_DNA.
EMBL; AL139243; CAH70450.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH70450.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH70450.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAH70450.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI16474.1; -; Genomic_DNA.
EMBL; AL139243; CAI16474.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI16474.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI16474.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI16474.1; JOINED; Genomic_DNA.
EMBL; AL139243; CAI14148.1; -; Genomic_DNA.
EMBL; AL356220; CAI14148.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI14148.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI14148.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI14148.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAH73138.1; -; Genomic_DNA.
EMBL; AL139243; CAH73138.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH73138.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH73138.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH73138.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI17161.1; -; Genomic_DNA.
EMBL; AL139243; CAI17161.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI17161.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI17161.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI17161.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAH70449.1; -; Genomic_DNA.
EMBL; AL139243; CAH70449.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAH70449.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAH70449.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAH70449.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI16473.1; -; Genomic_DNA.
EMBL; AL139243; CAI16473.1; JOINED; Genomic_DNA.
EMBL; AL356220; CAI16473.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI16473.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI16473.1; JOINED; Genomic_DNA.
EMBL; AL139243; CAI14147.1; -; Genomic_DNA.
EMBL; AL356220; CAI14147.1; JOINED; Genomic_DNA.
EMBL; AL356268; CAI14147.1; JOINED; Genomic_DNA.
EMBL; AL445251; CAI14147.1; JOINED; Genomic_DNA.
EMBL; AL590036; CAI14147.1; JOINED; Genomic_DNA.
CCDS; CCDS53566.1; -. [Q8WWQ2-4]
CCDS; CCDS53567.1; -. [Q8WWQ2-3]
CCDS; CCDS53568.1; -. [Q8WWQ2-2]
CCDS; CCDS7477.1; -. [Q8WWQ2-1]
PIR; JC7506; JC7506.
RefSeq; NP_001159716.1; NM_001166244.1. [Q8WWQ2-3]
RefSeq; NP_001159717.1; NM_001166245.1. [Q8WWQ2-4]
RefSeq; NP_001159718.1; NM_001166246.1. [Q8WWQ2-2]
RefSeq; NP_068600.4; NM_021828.4. [Q8WWQ2-1]
UniGene; Hs.500750; -.
UniGene; Hs.676960; -.
UniGene; Hs.689544; -.
ProteinModelPortal; Q8WWQ2; -.
SMR; Q8WWQ2; -.
BioGrid; 121926; 22.
STRING; 9606.ENSP00000359583; -.
iPTMnet; Q8WWQ2; -.
PhosphoSitePlus; Q8WWQ2; -.
BioMuta; HPSE2; -.
DMDM; 125987832; -.
PaxDb; Q8WWQ2; -.
PRIDE; Q8WWQ2; -.
DNASU; 60495; -.
Ensembl; ENST00000370546; ENSP00000359577; ENSG00000172987. [Q8WWQ2-2]
Ensembl; ENST00000370549; ENSP00000359580; ENSG00000172987. [Q8WWQ2-3]
Ensembl; ENST00000370552; ENSP00000359583; ENSG00000172987. [Q8WWQ2-1]
Ensembl; ENST00000628193; ENSP00000485916; ENSG00000172987. [Q8WWQ2-4]
GeneID; 60495; -.
KEGG; hsa:60495; -.
UCSC; uc001kpn.3; human. [Q8WWQ2-1]
CTD; 60495; -.
DisGeNET; 60495; -.
EuPathDB; HostDB:ENSG00000172987.12; -.
GeneCards; HPSE2; -.
GeneReviews; HPSE2; -.
HGNC; HGNC:18374; HPSE2.
HPA; HPA044603; -.
MalaCards; HPSE2; -.
MIM; 236730; phenotype.
MIM; 613469; gene.
neXtProt; NX_Q8WWQ2; -.
OpenTargets; ENSG00000172987; -.
Orphanet; 2704; Ochoa syndrome.
PharmGKB; PA38533; -.
eggNOG; ENOG410IHNV; Eukaryota.
eggNOG; ENOG410YDJW; LUCA.
GeneTree; ENSGT00390000004874; -.
HOVERGEN; HBG081606; -.
InParanoid; Q8WWQ2; -.
KO; K07965; -.
OMA; RTIAMPP; -.
OrthoDB; EOG091G05QD; -.
PhylomeDB; Q8WWQ2; -.
TreeFam; TF328999; -.
Reactome; R-HSA-2024096; HS-GAG degradation.
SIGNOR; Q8WWQ2; -.
GeneWiki; HPSE2; -.
GenomeRNAi; 60495; -.
PRO; PR:Q8WWQ2; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000172987; -.
CleanEx; HS_HPSE2; -.
ExpressionAtlas; Q8WWQ2; baseline and differential.
Genevisible; Q8WWQ2; HS.
GO; GO:0005622; C:intracellular; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
GO; GO:0030305; F:heparanase activity; TAS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
InterPro; IPR005199; Glyco_hydro_79.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR14363; PTHR14363; 1.
Pfam; PF03662; Glyco_hydro_79n; 1.
SUPFAM; SSF51445; SSF51445; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Extracellular matrix;
Glycoprotein; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 592 Inactive heparanase-2.
/FTId=PRO_0000068140.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 150 261 Missing (in isoform 4).
{ECO:0000303|PubMed:11027606}.
/FTId=VSP_015850.
VAR_SEQ 204 261 Missing (in isoform 3).
{ECO:0000303|PubMed:11027606}.
/FTId=VSP_015851.
VAR_SEQ 539 548 SVQLNGQPLV -> TQRCQYCGII (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_015852.
VAR_SEQ 549 592 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_015853.
VARIANT 315 315 A -> T (in dbSNP:rs17110744).
/FTId=VAR_030472.
VARIANT 579 579 Y -> F (in dbSNP:rs10883100).
{ECO:0000269|PubMed:11027606,
ECO:0000269|Ref.2}.
/FTId=VAR_023601.
CONFLICT 12 12 P -> L (in Ref. 2; CAC82492).
{ECO:0000305}.
CONFLICT 213 213 F -> S (in Ref. 2; CAC82491/CAC82492).
{ECO:0000305}.
SEQUENCE 592 AA; 66596 MW; 95C384AD9A6C868E CRC64;
MRVLCAFPEA MPSSNSRPPA CLAPGALYLA LLLHLSLSSQ AGDRRPLPVD RAAGLKEKTL
ILLDVSTKNP VRTVNENFLS LQLDPSIIHD GWLDFLSSKR LVTLARGLSP AFLRFGGKRT
DFLQFQNLRN PAKSRGGPGP DYYLKNYEDD IVRSDVALDK QKGCKIAQHP DVMLELQREK
AAQMHLVLLK EQFSNTYSNL ILTARSLDKL YNFADCSGLH LIFALNALRR NPNNSWNSSS
ALSLLKYSAS KKYNISWELG NEPNNYRTMH GRAVNGSQLG KDYIQLKSLL QPIRIYSRAS
LYGPNIGRPR KNVIALLDGF MKVAGSTVDA VTWQHCYIDG RVVKVMDFLK TRLLDTLSDQ
IRKIQKVVNT YTPGKKIWLE GVVTTSAGGT NNLSDSYAAG FLWLNTLGML ANQGIDVVIR
HSFFDHGYNH LVDQNFNPLP DYWLSLLYKR LIGPKVLAVH VAGLQRKPRP GRVIRDKLRI
YAHCTNHHNH NYVRGSITLF IINLHRSRKK IKLAGTLRDK LVHQYLLQPY GQEGLKSKSV
QLNGQPLVMV DDGTLPELKP RPLRAGRTLV IPPVTMGFYV VKNVNALACR YR


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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