UniProt: A0A1S3GFT9

Database: UniProt
Entry: A0A1S3GFT9_DIPOR

LinkDB:  A0A1S3GFT9_DIPOR 
Original site:  A0A1S3GFT9_DIPOR

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Ontology (21)   
   GO (21)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
All databases (27)   

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ID   A0A1S3GFT9_DIPOR        Unreviewed;       552 AA.
AC   A0A1S3GFT9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Hyaluronan synthase 2 {ECO:0000256|ARBA:ARBA00022262};
DE            EC=2.4.1.212 {ECO:0000256|ARBA:ARBA00012207};
DE   AltName: Full=Hyaluronate synthase 2 {ECO:0000256|ARBA:ARBA00030887};
DE   AltName: Full=Hyaluronic acid synthase 2 {ECO:0000256|ARBA:ARBA00031214};
GN   Name=Has2 {ECO:0000313|RefSeq:XP_012887681.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012887681.1};
RN   [1] {ECO:0000313|RefSeq:XP_012887681.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012887681.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-
CC         alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP;
CC         Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC         Evidence={ECO:0000256|ARBA:ARBA00033617};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529;
CC         Evidence={ECO:0000256|ARBA:ARBA00033617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-
CC         acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP;
CC         Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC         Evidence={ECO:0000256|ARBA:ARBA00033606};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466;
CC         Evidence={ECO:0000256|ARBA:ARBA00033606};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004698}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the NodC/HAS family.
CC       {ECO:0000256|ARBA:ARBA00006782}.
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DR   RefSeq; XP_012887681.1; XM_013032227.1.
DR   AlphaFoldDB; A0A1S3GFT9; -.
DR   STRING; 10020.ENSDORP00000005671; -.
DR   GeneID; 105997712; -.
DR   KEGG; dord:105997712; -.
DR   CTD; 3037; -.
DR   InParanoid; A0A1S3GFT9; -.
DR   OMA; KSATYVW; -.
DR   OrthoDB; 1361850at2759; -.
DR   UniPathway; UPA00341; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1903561; C:extracellular vesicle; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR   GO; GO:0050501; F:hyaluronan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0036302; P:atrioventricular canal development; IEA:Ensembl.
DR   GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0090500; P:endocardial cushion to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030213; P:hyaluronan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:1900625; P:positive regulation of monocyte aggregation; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd06434; GT2_HAS; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22913; HYALURONAN SYNTHASE; 1.
DR   PANTHER; PTHR22913:SF7; HYALURONAN SYNTHASE 2; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        475..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   552 AA;  63481 MW;  EA91837AC29DE04B CRC64;
     MHCERFLCIL RIIGTTLFGV SLLLGITAAY IVGYQFIQTD NYYFSFGLYG AFLASHLIIQ
     SLFAFLEHRK MKKSLETPIK LNKKVALCIA AYQEDPDYLR KCLQSVKRLT YPGIKVVMVI
     DGNSDDDCYM MDIFSEVMGR DKSATYIWKN NFHEKGPGET DKSHKESSQH VTQLVLSNKS
     ICIMQKWGGK REVMYTAFRA LGRSVDYVQV CDSDTMLDPA SSVEMVKVLE EDPMVGGVGG
     DVQILNKYDS WISFLSSVRY WMAFNIERAC QSYFGCVQCI SGPLGMYRNS LLHEFVEDWY
     NQEFMGNQCS FGDDRHLTNR VLSLGYATKY TARSKCLTET PIEYLRWLNQ QTRWSKSYFR
     EWLYNAMWFH KHHLWMTYEA VITGFFPFFL IATVIQLFYR GKIWNILLFL LTVQLVGLIK
     SSFASCLRGN IVMVFMSLYS VLYMSSLLPA KMFAIATINK AGWGTSGRKT IVVNFIGLIP
     VSIWFTILLG GVIFTIYKES KKPFSESKQT VLIVGSLVYA CYWVMLLTLY VVLINKCGRR
     KKGQPYDMVL DV
//

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