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Database: UniProt
Entry: L5LJL5_MYODS
LinkDB: L5LJL5_MYODS
Original site: L5LJL5_MYODS 
ID   L5LJL5_MYODS            Unreviewed;       473 AA.
AC   L5LJL5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   10-APR-2019, entry version 23.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000256|RuleBase:RU610713};
GN   ORFNames=MDA_GLEAN10002487 {ECO:0000313|EMBL:ELK26392.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26392.1};
RN   [1] {ECO:0000313|EMBL:ELK26392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:ELK26392.1};
RA   Zhang G., Cowled C., Wang L.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 0:0-0(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35; Evidence={ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713}.
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DR   EMBL; KB111145; ELK26392.1; -; Genomic_DNA.
DR   STRING; 225400.XP_006768878.1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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; 2.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 2.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      9     30       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    445    462       Helical. {ECO:0000256|SAM:Phobius}.
FT   ACT_SITE    147    147       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   CARBOHYD    338    338       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     60    321       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    223    237       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    346    357       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    351    405       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    407    413       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   473 AA;  54740 MW;  48D6969636FAF883 CRC64;
     MGVLRFKYIF FRSFVGSGGA FQVVFIFLLI PCCFTKDYRA TPMLPNVSYL WAWNAPTEPC
     PKKFHVSIDL SLFSLIGNPQ KDAVGQPVIL FYVDRLGHYP HIDKNGKKEH GGIPQLGDTQ
     SHLAKAEKDI EFYIPKDQLG LAIIDWEEWR PIWARNWKPK DIYKNESILL VQRQHPAFTL
     EEATDKAKEE FERDGRKFMV ETLKLGKKLR PKYLWGFYLF PDCYNHQYTK PNYTGVCFDI
     EKKRNNELNW LWNESTALFP SIYLNTHLMN SPKAAPFVRN RVKEAIRVSV VLNEKSPLPV
     YIYTRPVFTD DSSKYLSQDT CKKLHDYMIT TMNPYIINIT LAALMCSQVF CQEQGMCTRK
     DADSSAYLHL NSKNFVIGSF GNGTFRILGT PTMEDLKQFA EHFQCSCYSN TDCEKEVNFT
     QTIAIDVCMI EDVCIKAIVK SKNEIFHSSA SLVLFLLFLI VLENEYFGMQ TRL
//
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