HYAL1_MOUSE
ID HYAL1_MOUSE Reviewed; 462 AA.
AC Q91ZJ9; B1AV90; O70229; Q8CE62; Q8QZX3; Q8VBW7; Q8VDK0;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Hyaluronidase-1;
DE Short=Hyal-1;
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase-1;
DE Flags: Precursor;
GN Name=Hyal1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9503017; DOI=10.1006/geno.1997.5158;
RA Csoka A.B., Frost G.I., Heng H.H.Q., Scherer S.W., Mohapatra G., Stern R.;
RT "The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and
RT 9F1-F2 in mouse, a conserved candidate tumor suppressor locus.";
RL Genomics 48:63-70(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=C3H/HeJ;
RX PubMed=11960552; DOI=10.1186/1471-2121-3-8;
RA Chang N.-S.;
RT "Transforming growth factor-beta1 blocks the enhancement of tumor necrosis
RT factor cytotoxicity by hyaluronidase Hyal-2 in L929 fibroblasts.";
RL BMC Cell Biol. 3:8-8(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Csoka A.B.;
RT "Genomic sequence of the mouse Hyal1 locus encoding the mouse Hyal1, Fus2,
RT and Hyal3 genes.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 331-462, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
RX PubMed=11929860; DOI=10.1074/jbc.m108991200;
RA Shuttleworth T.L., Wilson M.D., Wicklow B.A., Wilkins J.A.,
RA Triggs-Raine B.L.;
RT "Characterization of the murine hyaluronidase gene region reveals complex
RT organization and cotranscription of Hyal1 with downstream genes, Fus2 and
RT Hyal3.";
RL J. Biol. Chem. 277:23008-23018(2002).
CC -!- FUNCTION: May have a role in promoting tumor progression. May block the
CC TGFB1-enhanced cell growth. {ECO:0000269|PubMed:11960552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5-4.0. {ECO:0000269|PubMed:9503017};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZJ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZJ9-2; Sequence=VSP_015923;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney, lung and skin.
CC {ECO:0000269|PubMed:11929860, ECO:0000269|PubMed:9503017}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos of all developmental stages,
CC with high level at the 7 day stage. {ECO:0000269|PubMed:11929860}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AF011567; AAC15949.1; -; mRNA.
DR EMBL; AF422176; AAL17822.1; -; mRNA.
DR EMBL; AF069741; AAL54881.1; -; Genomic_DNA.
DR EMBL; AF338323; AAL57173.1; -; Genomic_DNA.
DR EMBL; AK028942; BAC26206.1; -; mRNA.
DR EMBL; AL672219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021636; AAH21636.1; -; mRNA.
DR EMBL; AF417496; AAM14428.1; -; mRNA.
DR EMBL; AF417497; AAM14430.1; -; mRNA.
DR EMBL; AF417498; AAM14432.1; -; mRNA.
DR RefSeq; NP_001318090.1; NM_001331161.1.
DR RefSeq; NP_032343.2; NM_008317.5.
DR AlphaFoldDB; Q91ZJ9; -.
DR SMR; Q91ZJ9; -.
DR STRING; 10090.ENSMUSP00000010195; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q91ZJ9; 5 sites.
DR PhosphoSitePlus; Q91ZJ9; -.
DR MaxQB; Q91ZJ9; -.
DR PaxDb; Q91ZJ9; -.
DR PRIDE; Q91ZJ9; -.
DR ProteomicsDB; 273061; -. [Q91ZJ9-1]
DR ProteomicsDB; 273062; -. [Q91ZJ9-2]
DR Antibodypedia; 1046; 291 antibodies from 30 providers.
DR DNASU; 15586; -.
DR Ensembl; ENSMUST00000010195; ENSMUSP00000010195; ENSMUSG00000010051. [Q91ZJ9-1]
DR Ensembl; ENSMUST00000112387; ENSMUSP00000108006; ENSMUSG00000010051. [Q91ZJ9-2]
DR GeneID; 15586; -.
DR KEGG; mmu:15586; -.
DR UCSC; uc009rlv.1; mouse. [Q91ZJ9-1]
DR UCSC; uc009rlw.1; mouse. [Q91ZJ9-2]
DR CTD; 3373; -.
DR MGI; MGI:96298; Hyal1.
DR VEuPathDB; HostDB:ENSMUSG00000010051; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; Q91ZJ9; -.
DR OMA; GQCPLGI; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; Q91ZJ9; -.
DR TreeFam; TF321598; -.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR BioGRID-ORCS; 15586; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Hyal1; mouse.
DR PRO; PR:Q91ZJ9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91ZJ9; protein.
DR Bgee; ENSMUSG00000010051; Expressed in hepatobiliary system and 61 other tissues.
DR ExpressionAtlas; Q91ZJ9; baseline and differential.
DR Genevisible; Q91ZJ9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0036117; C:hyaluranon cable; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IMP:MGI.
DR GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:MGI.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; IMP:MGI.
DR GO; GO:0030212; P:hyaluronan metabolic process; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
DR GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; PTHR11769; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Glycosidase; Hydrolase; Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..462
FT /note="Hyaluronidase-1"
FT /id="PRO_0000042624"
FT DOMAIN 446..457
FT /note="EGF-like"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
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 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..361
FT /evidence="ECO:0000250"
FT DISULFID 235..249
FT /evidence="ECO:0000250"
FT DISULFID 386..397
FT /evidence="ECO:0000250"
FT DISULFID 391..446
FT /evidence="ECO:0000250"
FT DISULFID 448..457
FT /evidence="ECO:0000250"
FT VAR_SEQ 455..462
FT /note="KWCDKRGM -> GSST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015923"
FT CONFLICT 16
FT /note="P -> S (in Ref. 1; AAC15949 and 2; AAL17822)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="G -> R (in Ref. 1; AAC15949)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="E -> G (in Ref. 2; AAL17822 and 3; AAL54881/
FT AAL57173)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="R -> C (in Ref. 2; AAL17822 and 3; AAL54881/
FT AAL57173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52109 MW; DCE7339D7E0BCB9D CRC64;
MLGLTQHAQK VWRMKPFSPE VSPGSSPATA GHLLRISTLF LTLLELAQVC RGSVVSNRPF
ITVWNGDTHW CLTEYGVDVD VSVFDVVANK EQSFQGSNMT IFYREELGTY PYYTPTGEPV
FGGLPQNASL VTHLAHTFQD IKAAMPEPDF SGLAVIDWEA WRPRWAFNWD SKDIYRQRSM
ELVQAEHPDW PETLVEAAAK NQFQEAAEAW MAGTLQLGQV LRPRGLWGYY GFPDCYNNDF
LSLNYTGQCP VFVRDQNDQL GWLWNQSYAL YPSIYLPAAL MGTEKSQMYV RHRVQEALRV
AIVSRDPHVP VMPYVQIFYE MTDYLLPLEE LEHSLGESAA QGVAGAVLWL SSDKTSTKES
CQAIKAYMDS TLGPFIVNVT SAALLCSEAL CSGHGRCVRH PSYPEALLTL NPASFSIELT
HDGRPPSLKG TLSLKDRAQM AMKFRCRCYR GWRGKWCDKR GM
