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PIGM_CHICK
ID   PIGM_CHICK              Reviewed;         418 AA.
AC   Q5F380;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 83.
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; ORFNames=RCJMB04_29i7;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH65404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ851770; CAH65404.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001026693.2; NM_001031522.2.
DR   AlphaFoldDB; Q5F380; -.
DR   STRING; 9031.ENSGALP00000037081; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   PaxDb; Q5F380; -.
DR   GeneID; 428583; -.
DR   KEGG; gga:428583; -.
DR   CTD; 93183; -.
DR   VEuPathDB; HostDB:geneid_428583; -.
DR   eggNOG; KOG3893; Eukaryota.
DR   InParanoid; Q5F380; -.
DR   OrthoDB; 1003258at2759; -.
DR   PhylomeDB; Q5F380; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q5F380; -.
DR   Proteomes; UP000000539; 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..418
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246218"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..79
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..220
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..323
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..378
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..418
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46577 MW;  08A704FB8CEF2C6F CRC64;
     MAGGRPGLRA ALGAGLLARL SLVLYGLYQD AVMRVRYTDV DYRVFTDAAR LVTQGRSPYR
     RATFRYTPLL AWLLTPNVHL GELFGKLLFV AGDLAAAGVA YRALRRRGAS PGRACGCCAA
     AWLLNPLPMA VSSRGNAEAL VAVLVLAALH LVEAGSVGRA ALCYGLAVHL KIYPLTYALP
     IALRLQGSGE GAAGAGRDGT AEFTLVGGIW RRVVRVLNRN VLLFGAVAGS VLAALTVLFY
     HLYGWEFLEH AYLYHLTRRD IRHNFSPYFY MLYLTAESKW SFALGLAAFL PQLLLLLVVS
     VAFYKDLFFC CFLHTAIFVS FNKVCTSQYF IWYLCLLPII IPNIKMSWRR GVLLLFLWFA
     GQGLWLAPAY LLEFKGYNTF VFIWSAGLLF LFINSFILVQ IISHYQQETQ VARKVKEQ
 
 
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