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PIGM_BOVIN
ID   PIGM_BOVIN              Reviewed;         423 AA.
AC   Q5EA10;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=GPI mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase I;
DE            Short=GPI-MT-I;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class M protein;
DE            Short=PIG-M;
GN   Name=PIGM;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly (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 PIGM family. {ECO:0000305}.
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DR   EMBL; BT020759; AAX08776.1; -; mRNA.
DR   RefSeq; NP_001015563.1; NM_001015563.1.
DR   AlphaFoldDB; Q5EA10; -.
DR   STRING; 9913.ENSBTAP00000003140; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   PaxDb; Q5EA10; -.
DR   PRIDE; Q5EA10; -.
DR   GeneID; 509680; -.
DR   KEGG; bta:509680; -.
DR   CTD; 93183; -.
DR   eggNOG; KOG3893; Eukaryota.
DR   InParanoid; Q5EA10; -.
DR   OrthoDB; 1003258at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..423
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246212"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..287
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..357
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..423
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  49553 MW;  875B1D67174DB788 CRC64;
     MSPTTHWGDK FLNLRVPPAG VFVVAFFARV ALIFYGVFQD RTLLVRYTDI DYQVFTDAAR
     FVTEGHSPYL RATYRYTPLL AWLLTPNIYL NELFGKFLFI SFDLFTAFLL YRLLLLKGLG
     RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLMTLYL IEKRLVACAA VSYGFAVHLK
     MYPVTYILPI ALHLLPERDS DEGLRQSRYS FQVRLYEFLK RLCHRAVLLF VAVAGLTFFA
     LSFGFYYRYG WEFLEHAYLY HLTRRDIRHN FSPYFYMLYL TAESKWSFSL GIAAFLPQFI
     LLSAVSFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RIPWRRAVVL
     LMLWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEEPLTDRT
     KYD
 
 
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