ID G1P4V4_MYOLU Unreviewed; 484 AA.
AC G1P4V4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN Name=CHST3 {ECO:0000313|Ensembl:ENSMLUP00000005003.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005003.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005003.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005003.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-
CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00036278};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+);
CC Xref=Rhea:RHEA:11108, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:62065; EC=2.8.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00036249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC Evidence={ECO:0000256|ARBA:ARBA00036249};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000256|ARBA:ARBA00005530}.
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DR EMBL; AAPE02020633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P4V4; -.
DR STRING; 59463.ENSMLUP00000005003; -.
DR Ensembl; ENSMLUT00000005483.2; ENSMLUP00000005003.2; ENSMLUG00000005485.2.
DR eggNOG; ENOG502QWEX; Eukaryota.
DR GeneTree; ENSGT00940000161045; -.
DR HOGENOM; CLU_028381_3_2_1; -.
DR InParanoid; G1P4V4; -.
DR OMA; KWRFGMP; -.
DR TreeFam; TF342871; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; IEA:Ensembl.
DR GO; GO:0050698; F:proteoglycan sulfotransferase activity; IEA:Ensembl.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10704; CARBOHYDRATE SULFOTRANSFERASE; 1.
DR PANTHER; PTHR10704:SF60; CARBOHYDRATE SULFOTRANSFERASE 3; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|RuleBase:RU361155};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 139..456
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT REGION 104..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 55625 MW; D8E57E3CFF4A9027 CRC64;
MEKGLALPQD CRDFLHSLRM RSKYALFLAF VVVVFVFIEK ENKIISRVSD KLKQIPQSLA
DANSTDPALV LAENASLLSL SELDSAFTQL QSRLRNFSLQ LGLQPAEEEE EETKREEEEA
AEEEQGEQPP DPAEARRRRH VLLMATTRTG SSFVGEFFNQ QGNIFYLFEP LWHIERTVSF
EPGGASAAGS ALVYRDVLKQ LFLCDLYVLE HFISPLPEDH LTHGMFRRGS SRSLCEDPVC
TPFVKKVFEK YHCKNRRCGP LNVTLAAEAC RRKEHMALKA VRIRQLEFLQ PLAEDPRLDL
RVIQLVRDPR AVLASRMVAF AGKYETWKKW LAEGQDRLRE EEVQRLRGNC ESIRVSAELG
LRQPAWLRGR YMLVRYEDVA RRPLQKARDM YRFAGIPLTP QVEDWIQKNT QAPRDGSGIY
STQKNSSEQF EKWRFSMPFK LAQVVQDACG PAMRLFGYKL ARDAASLTNR SVSLLEERGT
FWVT
//
