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Database: UniProt
Entry: U3K2Z2_FICAL
LinkDB: U3K2Z2_FICAL
Original site: U3K2Z2_FICAL 
ID   U3K2Z2_FICAL            Unreviewed;       476 AA.
AC   U3K2Z2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN   Name=HYAL2 {ECO:0000313|Ensembl:ENSFALP00000009396.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000009396.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000009396.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000009396.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC       an intermediate-sized product which is further hydrolyzed by sperm
CC       hyaluronidase to give small oligosaccharides. Displays very low levels
CC       of activity. Associates with and negatively regulates MST1R.
CC       {ECO:0000256|ARBA:ARBA00037675}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
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_005052999.1; XM_005052942.1.
DR   AlphaFoldDB; U3K2Z2; -.
DR   STRING; 59894.ENSFALP00000009396; -.
DR   GlyCosmos; U3K2Z2; 1 site, No reported glycans.
DR   Ensembl; ENSFALT00000009436.2; ENSFALP00000009396.1; ENSFALG00000009008.2.
DR   GeneID; 101820358; -.
DR   KEGG; fab:101820358; -.
DR   eggNOG; ENOG502QUYI; Eukaryota.
DR   GeneTree; ENSGT01020000230364; -.
DR   HOGENOM; CLU_036366_0_0_1; -.
DR   OMA; TKNRESC; -.
DR   OrthoDB; 5344684at2759; -.
DR   Proteomes; UP000016665; Chromosome 12.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; IEA:Ensembl.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR   GO; GO:0001618; F:virus receptor activity; IEA:Ensembl.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; 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:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl.
DR   GO; GO:0042117; P:monocyte activation; IEA:Ensembl.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF6; HYALURONIDASE-2; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU610713};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..476
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004645206"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        49..342
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        213..229
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        367..378
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        372..431
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        433..442
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   476 AA;  54140 MW;  DE6980B56B75EFAC CRC64;
     MRGGCVAAVA VPWLALLALA RQPPEKPSAA PHLTRRPFLV AWNVPTQDCK PRFQVSFDFS
     IFDLYASPNE GFVGQNLTIF YKERLGLYPY YTHQGVAVNG GVPQNSSLSE HLARLQEGIN
     KYIRSPTKEG LAVIDWEEWR PVWARNWKPK DIYREASQEL VAQRQPAWPP EKVNKQAAFE
     FESAAQEFMV RTLRKAKSFR PKQLWGFYLF PDCYNHDYSK NKESYTGQCP DVEKSRNDQL
     KWLWNESMAL YPSIYLDPLL DSTPNSRKFV RARVMEAMRI SQKHHDDYSL PVFVYTRPTY
     IRKLNVLSQP DLISTIGESA ALGAAGAILW GDAVDTKNRE LCQLMKNYLE GDLGRYVVNV
     TTAAELCSTT LCQGRGRCLR QDSHADVFLH LNSTNFQLRR RDADHPERPL FWAEGQLSSA
     DILFLRTHFH CHCYQGWQGS GCQTHAGPRS AAPGPLAPLG LGVLLLLASW CYPPLD
//
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