HYAL5_MOUSE
ID HYAL5_MOUSE Reviewed; 526 AA.
AC Q812F3;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Hyaluronidase-5 {ECO:0000312|MGI:MGI:1921718};
DE Short=Hyal-5 {ECO:0000312|MGI:MGI:1921718};
DE EC=3.2.1.35 {ECO:0000255|RuleBase:RU610713, ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524, ECO:0000269|PubMed:19605784};
DE AltName: Full=Hyaluronoglucosaminidase-5 {ECO:0000303|PubMed:16330764, ECO:0000312|MGI:MGI:1921718};
DE Flags: Precursor;
GN Name=Hyal5 {ECO:0000312|MGI:MGI:1921718};
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 {ECO:0000312|EMBL:BAE21628.1};
RN [1] {ECO:0000312|EMBL:BAC55071.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:BAC55071.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC55071.1};
RX PubMed=16330764; DOI=10.1073/pnas.0506825102;
RA Kim E., Baba D., Kimura M., Yamashita M., Kashiwabara S., Baba T.;
RT "Identification of a hyaluronidase, Hyal5, involved in penetration of mouse
RT sperm through cumulus mass.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18028-18033(2005).
RN [2] {ECO:0000312|EMBL:BAE21628.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21628.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAE21628.1};
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 [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [4] {ECO:0000312|EMBL:EDL13813.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAI45993.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16925524; DOI=10.1042/bj20060598;
RA Reitinger S., Laschober G.T., Fehrer C., Greiderer B., Lepperdinger G.;
RT "Mouse testicular hyaluronidase-like proteins SPAM1 and HYAL5 but not
RT HYALP1 degrade hyaluronan.";
RL Biochem. J. 401:79-85(2007).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19605784; DOI=10.1095/biolreprod.109.078816;
RA Kimura M., Kim E., Kang W., Yamashita M., Saigo M., Yamazaki T.,
RA Nakanishi T., Kashiwabara S., Baba T.;
RT "Functional roles of mouse sperm hyaluronidases, HYAL5 and SPAM1, in
RT fertilization.";
RL Biol. Reprod. 81:939-947(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of hyaluronan into smaller
CC oligosaccharide fragments (PubMed:16330764, PubMed:16925524,
CC PubMed:19605784). Does not appear to be essential for fertilization
CC (PubMed:19605784). {ECO:0000269|PubMed:16330764,
CC ECO:0000269|PubMed:16925524, ECO:0000269|PubMed:19605784}.
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 Evidence={ECO:0000255|RuleBase:RU610713, ECO:0000269|PubMed:16330764,
CC ECO:0000269|PubMed:16925524, ECO:0000269|PubMed:19605784};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-7. {ECO:0000269|PubMed:16330764,
CC ECO:0000269|PubMed:16925524};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330764,
CC ECO:0000269|PubMed:16925524}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524}. Cytoplasmic
CC vesicle, secretory vesicle, acrosome membrane
CC {ECO:0000269|PubMed:16330764}. Secreted {ECO:0000269|PubMed:16330764}.
CC Note=Located on the plasma and acrosomal membranes of acrosome-intact
CC (AI) sperm and released during the acrosome reaction.
CC {ECO:0000269|PubMed:16330764}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, epididymal sperm and
CC epididymides (at protein level) (PubMed:16330764, PubMed:19605784).
CC Expressed at highest levels in testis with lesser amounts in epididymal
CC sperm (PubMed:16925524, PubMed:16330764, PubMed:19605784).
CC {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524,
CC ECO:0000269|PubMed:19605784}.
CC -!- DEVELOPMENTAL STAGE: Detected in the developing testis at postnatal day
CC 20, with increasing levels through development.
CC {ECO:0000269|PubMed:16330764}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Viable and fertile.
CC {ECO:0000269|PubMed:19605784}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AB085680; BAC55071.1; -; Genomic_DNA.
DR EMBL; AK133387; BAE21628.1; -; mRNA.
DR EMBL; AC127559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466533; EDL13813.1; -; Genomic_DNA.
DR EMBL; BC145992; AAI45993.1; -; mRNA.
DR EMBL; BC145994; AAI45995.1; -; mRNA.
DR CCDS; CCDS19948.1; -.
DR RefSeq; NP_083233.1; NM_028957.2.
DR RefSeq; XP_006505250.1; XM_006505187.1.
DR AlphaFoldDB; Q812F3; -.
DR SMR; Q812F3; -.
DR STRING; 10090.ENSMUSP00000031689; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q812F3; 2 sites.
DR PhosphoSitePlus; Q812F3; -.
DR PaxDb; Q812F3; -.
DR PRIDE; Q812F3; -.
DR ProteomicsDB; 267028; -.
DR DNASU; 74468; -.
DR Ensembl; ENSMUST00000031689; ENSMUSP00000031689; ENSMUSG00000029678.
DR Ensembl; ENSMUST00000200968; ENSMUSP00000144011; ENSMUSG00000029678.
DR GeneID; 74468; -.
DR KEGG; mmu:74468; -.
DR UCSC; uc009bcb.1; mouse.
DR CTD; 74468; -.
DR MGI; MGI:1921718; Hyal5.
DR VEuPathDB; HostDB:ENSMUSG00000029678; -.
DR eggNOG; ENOG502R6HD; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR InParanoid; Q812F3; -.
DR OMA; RAKIVFE; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; Q812F3; -.
DR TreeFam; TF321598; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 74468; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Hyal5; mouse.
DR PRO; PR:Q812F3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q812F3; protein.
DR Bgee; ENSMUSG00000029678; Expressed in spermatid and 14 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
DR GO; GO:0007341; P:penetration of zona pellucida; IDA:MGI.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR PANTHER; PTHR11769; PTHR11769; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..526
FT /note="Hyaluronidase-5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441636"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q08169"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..351
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 223..237
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 376..387
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 381..435
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 437..443
FT /evidence="ECO:0000250|UniProtKB:Q12794"
SQ SEQUENCE 526 AA; 60808 MW; 94DF140035DB52C9 CRC64;
MRVLYFKHSF FRSLLKSNGL PQTLLVFLLI PCYLTVDFRA PPLIPDVPFL WAWNAPTESC
FTRFNQPLDL GLFSLVGSPR KSATGQPVTI FYSDRLGLYP YIDDSQLIFN GGLPQLVSLK
SHLEVAKTDI LHYMPIDNVG LAVIDWEEWR PTWARNWKPK DIYRNKSIEL VQQQNILLNF
TEAVKWAKEE FEEAARHFME ETLRLGKSLR PNHLWGFYLF PDCYNNKFQV ADYKGECPDI
EKHRNDALFW IWEESTALYP SIYLKSSLKS SPQAALYVRN RVQEAIRVSK VKDPRNPLPI
FVYFRIVFTD LTYQYLYEDD LVNTIGETIA LGTSGMVMWG TLSLSQTMKS CLDLHDYLKT
ILNPYIINVT LAAKMCSQTL CQNQGVCSRK DWNSNDYLHL NPQNFQIHFV KHGKYEIRGN
PTLENLLYFS QKFRCSCFAH LNCQERADIE SVSTVSVCTL EDICINSLVI SDKSELPKDW
NRPYFVNSNQ SDITSSATVS PCVPRKDVSG YLVVLSLYSQ HLKYSL
