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GNT15_DICDI
ID   GNT15_DICDI             Reviewed;         516 AA.
AC   Q555X4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Glycosyltransferase-like protein gnt15;
GN   Name=gnt15; ORFNames=DDB_G0274741;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
RP   DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17588537; DOI=10.1016/j.bbrc.2007.06.016;
RA   Pang T.L., Wu C.J., Chen P.A., Weng Y.L., Chen M.Y.;
RT   "Dictyostelium gnt15 encodes a protein with similarity to LARGE and plays
RT   an essential role in development.";
RL   Biochem. Biophys. Res. Commun. 360:83-89(2007).
CC   -!- FUNCTION: May have a role in modulating cell adhesion and
CC       glycosylation. Essential for development.
CC       {ECO:0000269|PubMed:17588537}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression at vegetative and pre-
CC       aggregation stages. {ECO:0000269|PubMed:17588537}.
CC   -!- DISRUPTION PHENOTYPE: Slow growth, aberrant morphology and development.
CC       Produces a severe defect in spore formation. Cells are more adhesive.
CC       Alterations in glycosylation on membrane proteins and decreased gp130
CC       and gp150 levels are observed. {ECO:0000269|PubMed:17588537}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Highly
CC       divergent. {ECO:0000305}.
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DR   EMBL; AAFI02000012; EAL70263.1; -; Genomic_DNA.
DR   RefSeq; XP_643936.1; XM_638844.1.
DR   AlphaFoldDB; Q555X4; -.
DR   PaxDb; Q555X4; -.
DR   EnsemblProtists; EAL70263; EAL70263; DDB_G0274741.
DR   GeneID; 8619363; -.
DR   KEGG; ddi:DDB_G0274741; -.
DR   dictyBase; DDB_G0274741; gnt15.
DR   eggNOG; KOG3765; Eukaryota.
DR   HOGENOM; CLU_528327_0_0_1; -.
DR   InParanoid; Q555X4; -.
DR   PhylomeDB; Q555X4; -.
DR   PRO; PR:Q555X4; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042285; F:xylosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IMP:dictyBase.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..516
FT                   /note="Glycosyltransferase-like protein gnt15"
FT                   /id="PRO_0000393410"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..516
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          199..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   516 AA;  59898 MW;  491B655C3D1BB935 CRC64;
     MSNFYNNNPR RNTFRLTERI KKKPYQTLIV FILIFLFLYV FGPFGEKKSN NNNNNHPVSK
     TSSFTESLYT KFQTETFAYR ANGDLKKYDI SIITQFTVDR FDRIAMMADK WRAPISAAVY
     ITSFKDIDEV FKLVRNSFAV TEFVDLHFLF ANKTRYPVNN LRNLALRNAR TEWCLLLDVD
     FISPLGMYDY LHSTLEKLDT SNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNENNDNDNG
     NNNNNNDNEK NFKKKQEDLK IDPNDFEGDL KAIEKLKRNG EKLYVKNLKK VLDGSENNLG
     KNINFNNNNN DNNNKDDGGG GGYYLNSDNS NINNNNKIAF VIPSFSSSIS RFDFPDNKKD
     LLDFIKQDLI KEINSGVCPK CHGPTNYSRW YLSSEPYLVQ YKWIYEPFLL YNRSQIHDYD
     ERLKGYGFDK NSHTFGMAAA GFDFVVLPDA WIIHMNHVSK PWEGADTFNE QMFDCLSIVC
     ESILPDAKSK NGYDPNAKLF NEPLKNNDNC LTREHW
 
 
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