HST2_CAEEL
ID HST2_CAEEL Reviewed; 324 AA.
AC O17645;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Heparan sulfate 2-O-sulfotransferase hst-2;
DE Short=Heparan sulfotransferase 2;
DE EC=2.8.2.-;
DE AltName: Full=HS2ST1 homolog;
GN Name=hst-2; ORFNames=C34F6.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15003172; DOI=10.1016/s0896-6273(04)00084-4;
RA Buelow H.E., Hobert O.;
RT "Differential sulfations and epimerization define heparan sulfate
RT specificity in nervous system development.";
RL Neuron 41:723-736(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15671174; DOI=10.1073/pnas.0401591102;
RA Kinnunen T., Huang Z., Townsend J., Gatdula M.M., Brown J.R., Esko J.D.,
RA Turnbull J.E.;
RT "Heparan 2-O-sulfotransferase, hst-2, is essential for normal cell
RT migration in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1507-1512(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION.
RX PubMed=12653634; DOI=10.1042/bst0310343;
RA Turnbull J., Drummond K., Huang Z., Kinnunen T., Ford-Perriss M.,
RA Murphy M., Guimond S.;
RT "Heparan sulphate sulphotransferase expression in mice and Caenorhabditis
RT elegans.";
RL Biochem. Soc. Trans. 31:343-348(2003).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to the C2-position of
CC selected hexuronic acid residues within the maturing heparan sulfate
CC (HS). Involved in cell adhesion and guidance by specifically modifying
CC proteoglycans in the extracellular matrix and on the cell surface that
CC are essential for axon migrations. {ECO:0000269|PubMed:12653634,
CC ECO:0000269|PubMed:15003172, ECO:0000269|PubMed:15671174}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in the hypodermis, muscle, distal tip cells
CC (DTCs) and in neurons (at protein level).
CC {ECO:0000269|PubMed:15671174}.
CC -!- DISRUPTION PHENOTYPE: Worms are viable but display axonal and cellular
CC guidance defects in specific neuron classes.
CC {ECO:0000269|PubMed:15671174}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY552606; AAS89253.1; -; mRNA.
DR EMBL; Z81479; CAB03945.2; -; Genomic_DNA.
DR PIR; T19735; T19735.
DR RefSeq; NP_509871.2; NM_077470.3.
DR AlphaFoldDB; O17645; -.
DR SMR; O17645; -.
DR BioGRID; 46219; 1.
DR DIP; DIP-25527N; -.
DR STRING; 6239.C34F6.4; -.
DR EPD; O17645; -.
DR PaxDb; O17645; -.
DR PeptideAtlas; O17645; -.
DR PRIDE; O17645; -.
DR EnsemblMetazoa; C34F6.4.1; C34F6.4.1; WBGene00002029.
DR GeneID; 181309; -.
DR KEGG; cel:CELE_C34F6.4; -.
DR UCSC; C34F6.4; c. elegans.
DR CTD; 181309; -.
DR WormBase; C34F6.4; CE34159; WBGene00002029; hst-2.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR HOGENOM; CLU_045310_1_2_1; -.
DR InParanoid; O17645; -.
DR OMA; KWHEMKP; -.
DR OrthoDB; 877221at2759; -.
DR PhylomeDB; O17645; -.
DR Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR PRO; PR:O17645; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002029; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; ISS:WormBase.
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:0004394; F:heparan sulfate 2-O-sulfotransferase activity; IDA:WormBase.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IDA:WormBase.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..324
FT /note="Heparan sulfate 2-O-sulfotransferase hst-2"
FT /id="PRO_0000207679"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..175
FT /evidence="ECO:0000250"
FT DISULFID 188..194
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 37925 MW; 2BB8153FE8501C6E CRC64;
MLWKKRKVLY FAGISVFILI LLLLKLNSKP KANVWPTSSK IVIYNRIPKT GSTTFTNAIA
YDLYKENGFS VLHVNMTKNR QVMSLPDQYT FVNNITTWTE RLPAFYHGHV AFIDFQRFGI
ANPIYINIIR EPLERLLSHY YFLRYGDNYR IGLKRSRAGN NETFDECYSR GGKDCDMKQM
WIQIPYFCGH YHFCTEVGNP EALRVAKQNV LEKYLLVGTT SRMRDMIALL EVTVPDFFKG
ALGHFDSLDA NRAHLRYTKK KIPPNDQTLS MIRRDEVYKM EREFYDFINN LFDAVFKKAT
NGISKADDLV KLPLQYHFEK IKPS
