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Database: UniProt
Entry: A0A452HSW0_9SAUR
LinkDB: A0A452HSW0_9SAUR
Original site: A0A452HSW0_9SAUR 
ID   A0A452HSW0_9SAUR        Unreviewed;       508 AA.
AC   A0A452HSW0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000018152.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000018152.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|RuleBase:RU610713}.
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DR   AlphaFoldDB; A0A452HSW0; -.
DR   STRING; 38772.ENSGAGP00000018152; -.
DR   Ensembl; ENSGAGT00000020690.1; ENSGAGP00000018152.1; ENSGAGG00000013446.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF19; HYALURONIDASE-3; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000291020};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ   SEQUENCE   508 AA;  57981 MW;  A5B072CCA6965736 CRC64;
     MLGRGVHSGR KQEGVWTGRS CRTSTMTLGL TVWPWVLFCL GAILPSSSRG RSWESASASP
     LLQHEPFVVV WNLPTARCHQ RFGVALPLED YAIVENQGNA FQGQNMTIFY KNKFGLYPYI
     SPEGKYYNGG IPQKVRLKQH LERATAEITQ LLQPDFHGLA VVDWEEWRPL WRRNWGPKAV
     YKEASEQWVW ERFPDMRAKK RVYLAEVEFE GAAQELMERT LELGKELRPW GLWGFYKFPD
     CFNDNWMKGG NYSGECNAME VLRNNRLMWL WEASTALYPS IYLPPKLPPA KRQSYVHHRL
     QEAFRVARFG LEQPLSVIAY SRVSYRHSTR YLSEADLVHT IGESAALGAT GLALWGDNSY
     SRSAESCRSL RHYITHTLGP YVVNVTSAAQ LCSRQLCHGH GRCVRQRPDE LGAFLHLSLQ
     QWGADPVLTN YVGMDEPGQR AWGQFCCRCY RGWTGASCEK PGWTEPIRSP DCIARAHHPD
     ICVAVRDRNT AGSQICPKSA YEGKTELR
//
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