HYAS3_CHICK
ID HYAS3_CHICK Reviewed; 574 AA.
AC O57425; F1NU27;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Hyaluronan synthase 3;
DE EC=2.4.1.212 {ECO:0000250|UniProtKB:O08650};
DE AltName: Full=Hyaluronate synthase 3;
DE AltName: Full=Hyaluronic acid synthase 3;
DE Short=CHAS3;
DE Short=HA synthase 3;
GN Name=HAS3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-485.
RC STRAIN=White leghorn;
RX PubMed=9442026; DOI=10.1074/jbc.273.4.1923;
RA Spicer A.P., McDonald J.A.;
RT "Characterization and molecular evolution of a vertebrate hyaluronan
RT synthase gene family.";
RL J. Biol. Chem. 273:1923-1932(1998).
CC -!- FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to
CC the nascent hyaluronan polymer. Therefore, it is essential to
CC hyaluronan synthesis a major component of most extracellular matrices
CC that has a structural role in tissues architectures and regulates cell
CC adhesion, migration and differentiation (By similarity). This is one of
CC three isoenzymes responsible for cellular hyaluronan synthesis.
CC {ECO:0000250|UniProtKB:O08650}.
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:0000250|UniProtKB:O08650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466;
CC Evidence={ECO:0000250|UniProtKB:O08650};
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:0000250|UniProtKB:O08650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529;
CC Evidence={ECO:0000250|UniProtKB:O08650};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC {ECO:0000250|UniProtKB:O08650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08650};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O08650}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:O08650}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:O08650}. Note=Travels through endoplasmic
CC reticulum (ER), Golgi, plasma membrane, and endocytic vesicles (By
CC similarity). Actives only when present in plasma membrane (By
CC similarity). O-GlcNAcylation controls its membrane localization. A
CC rapid recycling of HAS3 between plasma membrane and endosomes is
CC controlled by the cytosolic levels of UDP-GlcUA and UDP-GlcNAc (By
CC similarity). {ECO:0000250|UniProtKB:O00219,
CC ECO:0000250|UniProtKB:O08650}.
CC -!- PTM: O-GlcNAcylation increases the hyaluronan synthase activity, HAS3
CC stability and its plasma membrane residence. The concentration of UDP-
CC GlcNAc controls the level of O-GlcNAc modification.
CC {ECO:0000250|UniProtKB:O00219}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
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DR EMBL; AADN05000558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF015777; AAB94538.1; -; Genomic_DNA.
DR AlphaFoldDB; O57425; -.
DR STRING; 9031.ENSGALP00000000894; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; O57425; -.
DR Ensembl; ENSGALT00000000896; ENSGALP00000000894; ENSGALG00000000630.
DR VEuPathDB; HostDB:geneid_427564; -.
DR eggNOG; KOG2571; Eukaryota.
DR GeneTree; ENSGT00390000010337; -.
DR HOGENOM; CLU_029695_3_0_1; -.
DR InParanoid; O57425; -.
DR OMA; DVIVPCF; -.
DR OrthoDB; 332363at2759; -.
DR PhylomeDB; O57425; -.
DR TreeFam; TF332506; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000000630; Expressed in granulocyte and 1 other tissue.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasmic vesicle; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..574
FT /note="Hyaluronan synthase 3"
FT /id="PRO_0000197180"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..44
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 399..419
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..429
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..450
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 457..477
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..494
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..515
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 531..551
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..574
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> T (in Ref. 2; AAB94538)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> P (in Ref. 2; AAB94538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 64653 MW; 58A850B3BB11883E CRC64;
MPVSLSTALR VVGTSLFALA VLGGILAAYV TGYQFIHTEK HYLSFGLYGA ILGLHLFIQS
LFAFLEHRRM RAERQPVRLG RSVALCIAAY QEDPDYLKKC LLSVKRIAFP DLKVVMVVDG
NGPDDTYMLD IFHDVMGSER AGSYVWRSNF HARGEGETEA GLQEGLAHVQ ALVRSTTYSC
ILQKWGGKRE VMYTAFRALG DSVDYIQVCD SDTVLDPACT AEMLRILEAD PRVGGVGGDV
QVWRRGGDGT HGGTALALVA LTPSPPQILN KYDSWISFLS SVRYWMAFNV ERACQSYFGC
VQCISGPLGM YRNALLQQFL EDWYHQTFLG TKCSFGDDRH LTNRVLSLGY QTKYTARSRC
LTETPTRYLR WLNQQTRWSK SYFREWLYNA LWFHKHHLWM TYESVVTGFF PFFLIATVIQ
LFYRGRIWNI LLFLLTVQLV GIIKATYACF LRGSAEMIFV SLYALLYMSS LLPAKMFAIA
TINKSGWGTS GRRTIVVNFV GLLPVSVWAA VLLGGLAYTA YSQDLLSDTE VAFLISGAVL
YACYWVALLT LYLAMVARRC GKRKEQCGLV FAEV
