HYAL2_HUMAN
ID HYAL2_HUMAN Reviewed; 473 AA.
AC Q12891; B3KRZ2; O15177; Q9BW29;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Hyaluronidase-2;
DE Short=Hyal-2;
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase-2;
DE AltName: Full=Lung carcinoma protein 2;
DE Short=LuCa-2;
DE Flags: Precursor;
GN Name=HYAL2; Synonyms=LUCA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP ALA-18.
RX PubMed=9712871; DOI=10.1074/jbc.273.35.22466;
RA Lepperdinger G., Strobl B., Kreil G.;
RT "HYAL2, a human gene expressed in many cells, encodes a lysosomal
RT hyaluronidase with a novel type of specificity.";
RL J. Biol. Chem. 273:22466-22470(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Chen J., Bader S., Latif F., Duh F.-M., Lerman M.I., Minna J.D.;
RT "LUCA2 (HYAL2, lysosomal hyaluronidase) a novel human cDNA with homology to
RT human PH-20 gene is homozygously deleted in small cell lung cancer and
RT located in 3p21.3.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-18.
RC TISSUE=Placenta, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-18.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-18.
RC TISSUE=Kidney;
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 [LARGE SCALE MRNA] OF 15-473, AND VARIANT ALA-18.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP REVIEW.
RX PubMed=11731268; DOI=10.1016/s0945-053x(01)00170-6;
RA Lepperdinger G., Mullegger J., Kreil G.;
RT "Hyal2 -- less active, but more versatile?";
RL Matrix Biol. 20:509-514(2001).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11296287; DOI=10.1073/pnas.071572898;
RA Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A., Lerman M.I.,
RA Miller A.D.;
RT "Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-
RT anchored cell-surface receptor for jaagsiekte sheep retrovirus, the
RT envelope protein of which mediates oncogenic transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH MST1R.
RX PubMed=12676986; DOI=10.1073/pnas.0837136100;
RA Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., Liu S.-L.,
RA Miller A.D., Lerman M.I.;
RT "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and
RT mediates transformation of epithelial cells by jaagsiekte sheep
RT retrovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003).
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:0000269|PubMed:11296287, ECO:0000269|PubMed:12676986,
CC ECO:0000269|PubMed:9712871}.
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 -!- SUBUNIT: Interacts with MST1R. {ECO:0000269|PubMed:12676986}.
CC -!- INTERACTION:
CC Q12891; P05067-2: APP; NbExp=3; IntAct=EBI-2806068, EBI-17264467;
CC Q12891; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-2806068, EBI-702390;
CC Q12891; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2806068, EBI-3867333;
CC Q12891; Q13643: FHL3; NbExp=3; IntAct=EBI-2806068, EBI-741101;
CC Q12891; P14136: GFAP; NbExp=3; IntAct=EBI-2806068, EBI-744302;
CC Q12891; P42858: HTT; NbExp=9; IntAct=EBI-2806068, EBI-466029;
CC Q12891; Q15323: KRT31; NbExp=3; IntAct=EBI-2806068, EBI-948001;
CC Q12891; O76011: KRT34; NbExp=3; IntAct=EBI-2806068, EBI-1047093;
CC Q12891; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-2806068, EBI-11959885;
CC Q12891; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-2806068, EBI-751260;
CC Q12891; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2806068, EBI-11962084;
CC Q12891; P29474: NOS3; NbExp=3; IntAct=EBI-2806068, EBI-1391623;
CC Q12891; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-2806068, EBI-448407;
CC Q12891; P49768-2: PSEN1; NbExp=3; IntAct=EBI-2806068, EBI-11047108;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11296287};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11296287}.
CC -!- TISSUE SPECIFICITY: Widely expressed. No expression detected in adult
CC brain. {ECO:0000269|PubMed:9712871}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be lysosomal. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28656.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HYAL2ID40904ch3p21.html";
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DR EMBL; AJ000099; CAA03924.1; -; mRNA.
DR EMBL; U09577; AAC62823.1; -; mRNA.
DR EMBL; AK092449; BAG52554.1; -; mRNA.
DR EMBL; AK127945; BAG54602.1; -; mRNA.
DR EMBL; AC002455; AAB67045.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65092.1; -; Genomic_DNA.
DR EMBL; BC000692; AAH00692.1; -; mRNA.
DR EMBL; AF070608; AAC28656.1; ALT_INIT; mRNA.
DR CCDS; CCDS2818.1; -.
DR RefSeq; NP_003764.3; NM_003773.4.
DR RefSeq; NP_149348.2; NM_033158.4.
DR RefSeq; XP_005265581.1; XM_005265524.2.
DR RefSeq; XP_005265582.1; XM_005265525.2.
DR AlphaFoldDB; Q12891; -.
DR SMR; Q12891; -.
DR BioGRID; 114239; 162.
DR IntAct; Q12891; 31.
DR STRING; 9606.ENSP00000401853; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q12891; 3 sites.
DR iPTMnet; Q12891; -.
DR PhosphoSitePlus; Q12891; -.
DR BioMuta; HYAL2; -.
DR DMDM; 311033483; -.
DR EPD; Q12891; -.
DR jPOST; Q12891; -.
DR MassIVE; Q12891; -.
DR MaxQB; Q12891; -.
DR PaxDb; Q12891; -.
DR PeptideAtlas; Q12891; -.
DR PRIDE; Q12891; -.
DR ProteomicsDB; 59006; -.
DR Antibodypedia; 30889; 281 antibodies from 32 providers.
DR DNASU; 8692; -.
DR Ensembl; ENST00000357750.9; ENSP00000350387.4; ENSG00000068001.14.
DR Ensembl; ENST00000395139.7; ENSP00000378571.3; ENSG00000068001.14.
DR Ensembl; ENST00000442581.1; ENSP00000406657.1; ENSG00000068001.14.
DR Ensembl; ENST00000447092.5; ENSP00000401853.1; ENSG00000068001.14.
DR GeneID; 8692; -.
DR KEGG; hsa:8692; -.
DR MANE-Select; ENST00000357750.9; ENSP00000350387.4; NM_003773.5; NP_003764.3.
DR UCSC; uc003czv.4; human.
DR CTD; 8692; -.
DR DisGeNET; 8692; -.
DR GeneCards; HYAL2; -.
DR HGNC; HGNC:5321; HYAL2.
DR HPA; ENSG00000068001; Tissue enhanced (lymphoid).
DR MalaCards; HYAL2; -.
DR MIM; 603551; gene.
DR neXtProt; NX_Q12891; -.
DR OpenTargets; ENSG00000068001; -.
DR Orphanet; 508476; Cleft lip and palate-craniofacial dysmorphism-congenital heart defect-hearing loss syndrome.
DR PharmGKB; PA29572; -.
DR VEuPathDB; HostDB:ENSG00000068001; -.
DR eggNOG; ENOG502QUYI; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; Q12891; -.
DR OMA; FHCHCYQ; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; Q12891; -.
DR TreeFam; TF321598; -.
DR BioCyc; MetaCyc:HS00926-MON; -.
DR BRENDA; 3.2.1.35; 2681.
DR BRENDA; 4.2.2.1; 2681.
DR PathwayCommons; Q12891; -.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR SignaLink; Q12891; -.
DR BioGRID-ORCS; 8692; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; HYAL2; human.
DR GeneWiki; HYAL2; -.
DR GenomeRNAi; 8692; -.
DR Pharos; Q12891; Tbio.
DR PRO; PR:Q12891; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q12891; protein.
DR Bgee; ENSG00000068001; Expressed in right lung and 186 other tissues.
DR ExpressionAtlas; Q12891; baseline and differential.
DR Genevisible; Q12891; HS.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0033906; F:hyaluronoglucuronidase activity; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
DR GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; IEP:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:UniProtKB.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0042117; P:monocyte activation; IDA:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0070295; P:renal water absorption; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEP:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; ISS: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 Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Receptor; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..448
FT /note="Hyaluronidase-2"
FT /id="PRO_0000012099"
FT PROPEP 449..473
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012100"
FT DOMAIN 361..439
FT /note="EGF-like"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 448
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..340
FT /evidence="ECO:0000250"
FT DISULFID 211..227
FT /evidence="ECO:0000250"
FT DISULFID 365..376
FT /evidence="ECO:0000250"
FT DISULFID 370..427
FT /evidence="ECO:0000250"
FT DISULFID 429..438
FT /evidence="ECO:0000250"
FT VARIANT 18
FT /note="S -> A (in dbSNP:rs709210)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9712871,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT /id="VAR_028170"
FT VARIANT 418
FT /note="I -> L (in dbSNP:rs35455589)"
FT /id="VAR_061193"
FT CONFLICT 261..262
FT /note="SR -> AL (in Ref. 1; CAA03924)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="RL -> C (in Ref. 1; CAA03924)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="Missing (in Ref. 1; CAA03924)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..379
FT /note="RR -> PG (in Ref. 1; CAA03924)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="S -> N (in Ref. 1; CAA03924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53860 MW; A8302738478BFE61 CRC64;
MRAGPGPTVT LALVLAVSWA MELKPTAPPI FTGRPFVVAW DVPTQDCGPR LKVPLDLNAF
DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV PQNVSLWAHR KMLQKRVEHY
IRTQESAGLA VIDWEDWRPV WVRNWQDKDV YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE
FAAQQFMLET LRYVKAVRPR HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW
LWAESTALFP SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR
RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL LVPYVVNVSW
ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH APGEPQLRPV GELSWADIDH
LQTHFRCQCY LGWSGEQCQW DHRQAAGGAS EAWAGSHLTS LLALAALAFT WTL
