ID   CHSTA_CHICK             Reviewed;         358 AA.
AC   Q5ZIE4; Q8AYG8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Carbohydrate sulfotransferase 10;
DE            EC=2.8.2.-;
DE   AltName: Full=HNK-1 sulfotransferase;
DE            Short=HNK-1ST;
DE            Short=HNK1ST;
GN   Name=CHST10; ORFNames=RCJMB04_27h10;
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 [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 132-305, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain, and Cartilage;
RX   PubMed=12508223; DOI=10.1002/dvdy.10214;
RA   Domowicz M.S., Mueller M.M., Novak T.E., Schwartz L.E., Schwartz N.B.;
RT   "Developmental expression of the HNK-1 carbohydrate epitope on aggrecan
RT   during chondrogenesis.";
RL   Dev. Dyn. 226:42-50(2003).
CC   -!- FUNCTION: Catalyzes the transfer of sulfate to position 3 of terminal
CC       glucuronic acid of both protein- and lipid-linked oligosaccharides.
CC       Participates in biosynthesis of HNK-1 carbohydrate structure, a
CC       sulfated glucuronyl-lactosaminyl residue carried by many neural
CC       recognition molecules, which is involved in cell interactions during
CC       ontogenetic development and in synaptic plasticity in the adult (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in hypertrophic,
CC       prehypertrophic and proliferative chondrocytes at E12 but is down-
CC       regulated in epiphyseal chondrocytes. {ECO:0000269|PubMed:12508223}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR   EMBL; AJ720840; CAG32499.1; -; mRNA.
DR   EMBL; AF468194; AAN60757.1; -; mRNA.
DR   RefSeq; NP_001025514.1; NM_001030343.1.
DR   AlphaFoldDB; Q5ZIE4; -.
DR   STRING; 9031.ENSGALP00000040860; -.
DR   PaxDb; Q5ZIE4; -.
DR   GeneID; 395206; -.
DR   KEGG; gga:395206; -.
DR   CTD; 9486; -.
DR   VEuPathDB; HostDB:geneid_395206; -.
DR   eggNOG; KOG4651; Eukaryota.
DR   HOGENOM; CLU_043398_2_0_1; -.
DR   InParanoid; Q5ZIE4; -.
DR   PhylomeDB; Q5ZIE4; -.
DR   TreeFam; TF325581; -.
DR   PRO; PR:Q5ZIE4; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR018011; Carb_sulfotrans_8-10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12137; PTHR12137; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..358
FT                   /note="Carbohydrate sulfotransferase 10"
FT                   /id="PRO_0000189661"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..358
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         129..135
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..199
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        298
FT                   /note="A -> E (in Ref. 2; AAN60757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="R -> H (in Ref. 2; AAN60757)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  42148 MW;  6B879BEB2DE2277B CRC64;
     MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDGYGAKQE PLILTAVTKV EEARVPEEKH
     WTKEFQPTGK AFTGNLLHHP LVHMERLELL RNVCRDTALR NLSHTAVSKF VLDRIFVCDK
     HKILFCQTPK VGNTQWKKVL IVLNGAYSSI DEIPESIVHD HEKNGLPRLS SFSDSEIKKR
     LNLYFKFFIV RDPFERLISA FKDKFVHNPR FEPWYRHEIA PSIIRKYRRN RMETKGLQFE
     DFVRYLGDPN HRWLDVQFGD HIIHWVTYVE LCAPCEITYS VIGHHETLED DAPYILKAAG
     IDRLVSYPTI PPGITVYNKT KVERYFSGIS KRDIRRLYAR FEGDFKLFGY RVPDFLLN