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Database: UniProt
Entry: F7CYI5_MONDO
LinkDB: F7CYI5_MONDO
Original site: F7CYI5_MONDO 
ID   F7CYI5_MONDO            Unreviewed;       418 AA.
AC   F7CYI5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN   Name=HYAL3 {ECO:0000313|Ensembl:ENSMODP00000015236.2};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000015236.2, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000015236.2, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000015236.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000251,
CC         ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC       ECO:0000256|RuleBase:RU610713}.
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DR   RefSeq; XP_007499960.1; XM_007499898.2.
DR   RefSeq; XP_007499961.1; XM_007499899.2.
DR   AlphaFoldDB; F7CYI5; -.
DR   STRING; 13616.ENSMODP00000015236; -.
DR   GlyCosmos; F7CYI5; 1 site, No reported glycans.
DR   Ensembl; ENSMODT00000015520.3; ENSMODP00000015236.2; ENSMODG00000012164.3.
DR   GeneID; 100028570; -.
DR   KEGG; mdo:100028570; -.
DR   CTD; 8372; -.
DR   eggNOG; ENOG502QTXP; Eukaryota.
DR   GeneTree; ENSGT01020000230364; -.
DR   HOGENOM; CLU_036366_0_0_1; -.
DR   InParanoid; F7CYI5; -.
DR   OMA; GWATSWH; -.
DR   OrthoDB; 5344684at2759; -.
DR   TreeFam; TF321598; -.
DR   Proteomes; UP000002280; Chromosome 6.
DR   Bgee; ENSMODG00000012164; Expressed in hindlimb bud and 14 other cell types or tissues.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR   GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; IEA:Ensembl.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0071493; P:cellular response to UV-B; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:2000355; P:negative regulation of ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0001552; P:ovarian follicle atresia; IEA:Ensembl.
DR   GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
DR   GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF19; HYALURONIDASE-3; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..418
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003355768"
FT   DOMAIN          399..410
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS00022,
FT                   ECO:0000259|PROSITE:PS01186"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        40..328
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        203..217
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        353..364
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        358..399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        401..410
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   418 AA;  47683 MW;  7996996CFDB82061 CRC64;
     MNGGCYLVAW ATLCLVGGWA TSWHLGRPFT AVWNVPTARC QTHFGQPLPL DPFDIVHNWA
     QRFRGQNITI FYKNQFGLYP YLGPRGIVHH GGIPQAVSLH RHLALVANQI SGLMHKGFRG
     LAVLDWEEWH PLWNRNWGLR QVYRKAAWAW AQQQWPDLPP KQQHLKARTT FEQAARALME
     STLQLGQALR PRGLWGFYRF PLCRSPWQGR HNYTGKCRKT DKVYNDQLYW LWKASSALFP
     SIYLPPDLPQ VYRKSYTRHR LEEAFRVAQF GHPRPLPVLA YARLTHPGSG QFLSQNDLIQ
     TIGVSVALGV EGVVLWGDLS FSSSEEQCKH LQSYLSTILG PYLSNVTQAA QACSQQLCHG
     NGRCARWEPS NDEVFLHLEP RRAQGTLMEG TAKWAHFRCL CYPGWEGTTC KVPVAGTE
//
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