HYAL4_MOUSE
ID HYAL4_MOUSE Reviewed; 481 AA.
AC Q05A56; Q9D660;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hyaluronidase-4;
DE Short=Hyal-4;
DE EC=3.2.1.35;
DE AltName: Full=Chondroitin sulfate endo-beta-N-acetylgalactosaminidase;
DE AltName: Full=Chondroitin sulfate hydrolase;
DE Short=CSHY;
DE AltName: Full=Hyaluronoglucosaminidase-4;
GN Name=Hyal4;
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 [LARGE SCALE MRNA].
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 [2]
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).
CC -!- FUNCTION: Endo-hyaluronidase that degrades hyaluronan to smaller
CC oligosaccharide fragments. Has also chondroitin sulfate hydrolase
CC activity, The best substrate being the galactosaminidic linkage in the
CC sequence of a trisulfated tetrasaccharide (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AK014599; BAB29454.1; -; mRNA.
DR EMBL; BC125402; AAI25403.1; -; mRNA.
DR EMBL; BC132096; AAI32097.1; -; mRNA.
DR CCDS; CCDS39441.1; -.
DR RefSeq; NP_084124.1; NM_029848.1.
DR AlphaFoldDB; Q05A56; -.
DR SMR; Q05A56; -.
DR STRING; 10090.ENSMUSP00000031691; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q05A56; 4 sites.
DR iPTMnet; Q05A56; -.
DR PhosphoSitePlus; Q05A56; -.
DR PaxDb; Q05A56; -.
DR PRIDE; Q05A56; -.
DR ProteomicsDB; 273290; -.
DR Antibodypedia; 31779; 86 antibodies from 18 providers.
DR Ensembl; ENSMUST00000031691; ENSMUSP00000031691; ENSMUSG00000029680.
DR GeneID; 77042; -.
DR KEGG; mmu:77042; -.
DR UCSC; uc009bbx.1; mouse.
DR CTD; 23553; -.
DR MGI; MGI:1924292; Hyal4.
DR VEuPathDB; HostDB:ENSMUSG00000029680; -.
DR eggNOG; ENOG502QPZH; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; Q05A56; -.
DR OMA; CVVQPIH; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; Q05A56; -.
DR TreeFam; TF321598; -.
DR BioGRID-ORCS; 77042; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q05A56; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q05A56; protein.
DR Bgee; ENSMUSG00000029680; Expressed in interventricular septum and 24 other tissues.
DR ExpressionAtlas; Q05A56; baseline and differential.
DR Genevisible; Q05A56; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030207; P:chondroitin sulfate catabolic process; IDA:MGI.
DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; Hydrolase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Hyaluronidase-4"
FT /id="PRO_0000302000"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..351
FT /evidence="ECO:0000250"
FT DISULFID 223..237
FT /evidence="ECO:0000250"
FT DISULFID 376..387
FT /evidence="ECO:0000250"
FT DISULFID 381..435
FT /evidence="ECO:0000250"
FT DISULFID 437..446
FT /evidence="ECO:0000250"
FT CONFLICT 124..126
FT /note="KAA -> GAG (in Ref. 1; BAB29454)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..317
FT /note="LS -> PF (in Ref. 1; BAB29454)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="C -> S (in Ref. 1; BAB29454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 54385 MW; 388B46DDD9EFDB40 CRC64;
MQLLPEGQLR LCVFQPVHLT SGLLILFILK SISSLKPARL PVYQRKPFIA AWNAPTDLCL
IKYNLTLNLK VFQMVGSPRL KDRGQNVVIF YANRLGYYPW YTSEGVPING GLPQNTSLQV
HLKKAAQDIN YYIPSENFSG LAVIDWEYWR PQWARNWNTK DIYRQKSRTL ISDMKENISA
ADIEYSAKAT FEKSAKAFME ETIKLGSKSR PKGLWGYYLY PDCHNYNVYA TNYTGSCPEE
EVLRNNDLSW LWNSSTALYP AVSIRKSFAD SENTLHFSRF RVRESLRIST MTSQDYALPV
FVYTQLGYKE EPLLFLSKQD LISTIGESAA LGAAGIVVWG DMNLTSSEEN CTKVNRFVNS
DFGSYIINVT RAAEVCSRHL CKNNGRCVRK TWKAAHYLHL NPASYHIEAS EDGEFIVRGR
ASDTDLAVMA ENFLCHCYEG YEGADCREMT EASGPSGLSL SSSSVITLCL LVLAGYQSIQ
L
