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PIGV_DROPS
ID   PIGV_DROPS              Reviewed;         452 AA.
AC   Q290J8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=GPI mannosyltransferase 2;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase II;
DE            Short=GPI-MT-II;
GN   ORFNames=GA19757;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the second mannose to the
CC       glycosylphosphatidylinositol during GPI precursor assembly. Required
CC       for the GPI-mediated endoplasmic reticulum exit and proper targeting to
CC       the cell surface of chp. Required for GPI-mediated membrane attachment
CC       of chp, qsm and Cont. Essential for microvillar stability in the
CC       rhabdomere (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
CC   -!- CAUTION: Was originally named veg by similarity to the D.melanogaster
CC       ortholog. However, it was later shown that the veg phenotype does not
CC       map to this protein. It is still not known which gene corresponds to
CC       the veg phenotype. {ECO:0000305}.
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DR   EMBL; CM000071; EAL25364.1; -; Genomic_DNA.
DR   RefSeq; XP_001360789.1; XM_001360752.3.
DR   AlphaFoldDB; Q290J8; -.
DR   STRING; 7237.FBpp0277779; -.
DR   CAZy; GT76; Glycosyltransferase Family 76.
DR   EnsemblMetazoa; FBtr0279341; FBpp0277779; FBgn0079753.
DR   GeneID; 4804187; -.
DR   KEGG; dpo:Dpse_GA19757; -.
DR   eggNOG; KOG2647; Eukaryota.
DR   HOGENOM; CLU_029048_3_2_1; -.
DR   InParanoid; Q290J8; -.
DR   OMA; EYFLHIA; -.
DR   PhylomeDB; Q290J8; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0079753; Expressed in female reproductive system and 3 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045052; P:protein insertion into ER membrane by GPI attachment sequence; IEA:EnsemblMetazoa.
DR   GO; GO:0045313; P:rhabdomere membrane biogenesis; IEA:EnsemblMetazoa.
DR   InterPro; IPR007315; PIG-V/Gpi18.
DR   PANTHER; PTHR12468; PTHR12468; 1.
DR   Pfam; PF04188; Mannosyl_trans2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..452
FT                   /note="GPI mannosyltransferase 2"
FT                   /id="PRO_0000246238"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..113
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..209
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..284
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..370
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..426
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  52131 MW;  5639FB37520C552E CRC64;
     MMEKVTKLAL TSRVMVLVVQ LLANFATPDH KPDVFRMPQS EGPKKNGPFP WLDELVLQSL
     SGLRHWDGEY FLHIASNLYT YENTLAFYPL YPVVVRHVAQ ACQHLGIPLS RDALILLVAV
     ALNVLIFCKT ANVLYKLTQR MFNDHNKSWN AALIFCFNPA SIFFSAAYSE TFFAFASFSL
     MLECMRSEKD FRTFRLGAAL TGCFVCRSNG LLTLGFPLYF LARHILLSTG SVQRCWQLFK
     MGLAMLVALG ILHTYYFYIY RLYCLPDVKV QHAQHVVDYA KERSFLISGQ ASVGSPWCGY
     TLPFPYTYVQ SHYWDVGFLR YYKWKQLPNF LLALPMLLFM HWHCYDYIRK LVANTWSKIS
     PSEYQGILKE HISFPFVLHA AVLTLVCTLY VHIQVSTRLL ASATPVFYWF AADYMPNTFQ
     LSFRSKAGVL FIWCLTYSLV GTVLFSNNYP WT
 
 
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