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HYAL2_SHEEP
ID   HYAL2_SHEEP             Reviewed;         476 AA.
AC   Q8SQG7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Hyaluronidase-2;
DE            Short=Hyal-2;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase-2;
DE   Flags: Precursor;
GN   Name=HYAL2;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11836391; DOI=10.1128/jvi.76.5.2141-2149.2002;
RA   Dirks C., Duh F.-M., Rai S.K., Lerman M.I., Miller A.D.;
RT   "Mechanism of cell entry and transformation by enzootic nasal tumor
RT   virus.";
RL   J. Virol. 76:2141-2149(2002).
RN   [2]
RP   INTERACTION WITH JSRV ENVELOPE PROTEINS.
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).
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 (By
CC       similarity). {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   -!- SUBUNIT: Interacts with MST1R (By similarity). Interacts with
CC       Jaagsiekte sheep retrovirus (JSRV) envelope proteins. {ECO:0000250,
CC       ECO:0000269|PubMed:11296287}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- MISCELLANEOUS: Acts as a receptor for the Jaagsiekte sheep retrovirus
CC       (JSRV), which induces ovine pulmonary adenocarcinoma. A possible
CC       mechanism is that binding to JSRV envelope proteins may liberate the
CC       oncogenic factor MST1R that is normally negatively regulated by HYAL2,
CC       leading to oncogenic transformation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; AF411974; AAL78386.1; -; mRNA.
DR   RefSeq; NP_001009754.1; NM_001009754.1.
DR   RefSeq; XP_011954627.1; XM_012099237.2.
DR   RefSeq; XP_011954628.1; XM_012099238.2.
DR   RefSeq; XP_011954629.1; XM_012099239.2.
DR   AlphaFoldDB; Q8SQG7; -.
DR   SMR; Q8SQG7; -.
DR   STRING; 9940.ENSOARP00000010309; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   Ensembl; ENSOART00000010462; ENSOARP00000010309; ENSOARG00000009614.
DR   Ensembl; ENSOART00020021134; ENSOARP00020017491; ENSOARG00020013831.
DR   GeneID; 443154; -.
DR   KEGG; oas:443154; -.
DR   CTD; 8692; -.
DR   eggNOG; ENOG502QUYI; Eukaryota.
DR   HOGENOM; CLU_036366_0_0_1; -.
DR   OMA; FHCHCYQ; -.
DR   OrthoDB; 1096692at2759; -.
DR   Proteomes; UP000002356; Chromosome 19.
DR   Bgee; ENSOARG00000009614; Expressed in prescapular lymph node and 52 other tissues.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; ISS:UniProtKB.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; ISS:UniProtKB.
DR   GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS: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; ISS:UniProtKB.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; ISS:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
DR   GO; GO:0042117; P:monocyte activation; ISS: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; ISS:UniProtKB.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; ISS:UniProtKB.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
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: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; IEA:Ensembl.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; ISS: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; Host-virus interaction; Hydrolase; Lipoprotein; Membrane;
KW   Receptor; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..451
FT                   /note="Hyaluronidase-2"
FT                   /id="PRO_0000239065"
FT   PROPEP          452..476
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000239066"
FT   DOMAIN          364..442
FT                   /note="EGF-like"
FT   ACT_SITE        138
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           451
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..343
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..230
FT                   /evidence="ECO:0000250"
FT   DISULFID        368..379
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..430
FT                   /evidence="ECO:0000250"
FT   DISULFID        432..441
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  54229 MW;  427C9277ACF7AAAA CRC64;
     MWTGLGPAVT LALVLVVAWA TELKPTAPPI FTGRPFVVAW DVPTQDCGPR HKMPLDPKDM
     KAFDVQASPN EGFVNQNITI FYRDRLGMYP HFNSVGRSVH GGVPQNGSLW VHLEMLKGHV
     EHYIRTQEPA GLAVIDWEDW RPVWVRNWQD KDVYRRLSRQ LVASHHPDWP PERIVKEAQY
     EFEFAARQFM LETLRFVKAF RPRHLWGFYL FPDCYNHDYV QNWETYTGRC PDVEVSRNDQ
     LSWLWAESTA LFPSVYLEET LASSTHGRNF VSFRVQEALR VADVHHANHA LPVYVFTRPT
     YSRGLTGLSE MDLISTIGES AALGAAGVIL WGDAGFTTSN ETCRRLKDYL TRSLVPYVVN
     VSWAAQYCSW AQCHGHGRCV RRDPNAHTFL HLSASSFRLV PSHAPDEPRL RPEGELSWAD
     RNHLQTHFRC QCYLGWGGEQ CQWDRRRAAG GASGAWAGSH LTGLLAVAVL AFTWTS
 
 
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