KIL1_DICDI
ID KIL1_DICDI Reviewed; 471 AA.
AC Q55GK8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Membrane-associated sulfotransferase kil1;
DE EC=2.8.2.-;
GN Name=kil1; ORFNames=DDB_G0267630;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION.
RX PubMed=16367873; DOI=10.1111/j.1462-5822.2005.00607.x;
RA Benghezal M., Fauvarque M.O., Tournebize R., Froquet R., Marchetti A.,
RA Bergeret E., Lardy B., Klein G., Sansonetti P., Charette S.J., Cosson P.;
RT "Specific host genes required for the killing of Klebsiella bacteria by
RT phagocytes.";
RL Cell. Microbiol. 8:139-148(2006).
CC -!- FUNCTION: Sulfotransferase involved in intracellular killing of
CC bacteria. {ECO:0000269|PubMed:16367873}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73268.1; -; Genomic_DNA.
DR RefSeq; XP_647176.1; XM_642084.1.
DR AlphaFoldDB; Q55GK8; -.
DR SMR; Q55GK8; -.
DR STRING; 44689.DDB0233104; -.
DR PaxDb; Q55GK8; -.
DR ABCD; Q55GK8; 12 sequenced antibodies.
DR EnsemblProtists; EAL73268; EAL73268; DDB_G0267630.
DR GeneID; 8615979; -.
DR KEGG; ddi:DDB_G0267630; -.
DR dictyBase; DDB_G0267630; kil1.
DR eggNOG; KOG3704; Eukaryota.
DR HOGENOM; CLU_580655_0_0_1; -.
DR InParanoid; Q55GK8; -.
DR OMA; LYYEQID; -.
DR PhylomeDB; Q55GK8; -.
DR Reactome; R-DDI-2022928; HS-GAG biosynthesis.
DR PRO; PR:Q55GK8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:dictyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:dictyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR GO; GO:0006477; P:protein sulfation; IMP:dictyBase.
DR GO; GO:0140460; P:response to Gram-negative bacterium; HDA:dictyBase.
DR GO; GO:0001878; P:response to yeast; IMP:dictyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605; PTHR10605; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..471
FT /note="Membrane-associated sulfotransferase kil1"
FT /id="PRO_0000327865"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 89..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..172
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 55568 MW; 51A1F6200B7D415E CRC64;
MSTTSMILTK KNIIILSIII ITIIAYQFYI TSPQSFPSSN TITNTINTSG KGLDYTELLN
LQKDLKAQQT EIRKQLEQLK YSINDINQNQ NENQNQINNE YNNNKLNDEQ ENNNNNNYNN
NNNNNNNELI NYKERIKKKS KEQPNTCIPV EGKLLCLPNF IVIGTMKSGT TFLDYYLQKH
PQIAHHSKKE IWYFNSYYAN GIEWYAKHFE QYTSLENQKL IGEATPFYIN NPNTAPRLFT
TLKNAKLILL LRDPVERSLS QYHFSIQWLK RNKSPPLEYS FEHLIHEEAD VIETCIRGHE
RYKEAFKQRK EIEKNGGGGL LNDNTSGEEF NLVDPFYTLH SEKNWTFYKD CIRCDKCFQI
GSILHTSGHP TFGMLAKSLY FEQLDYWLNF FPLEQIHIIR YEDISSQPES VLSELEDFLD
INHIDYGEFK PRNVVQHDPM NQEIKSYLIN YFKQSNEKLY NLLNRDFKWQ N
