PIGV_RAT
ID PIGV_RAT Reviewed; 492 AA.
AC Q5KR61;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class V protein;
DE Short=PIG-V;
GN Name=Pigv;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15623507; DOI=10.1074/jbc.m413867200;
RA Kang J.Y., Hong Y., Ashida H., Shishioh N., Murakami Y., Morita Y.S.,
RA Maeda Y., Kinoshita T.;
RT "PIG-V involved in transferring the second mannose in
RT glycosylphosphatidylinositol.";
RL J. Biol. Chem. 280:9489-9497(2005).
CC -!- FUNCTION: Alpha-1,6-mannosyltransferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second
CC mannose to the glycosylphosphatidylinositol during GPI precursor
CC 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 -!- PTM: Not N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
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DR EMBL; AB196341; BAD88519.1; -; mRNA.
DR RefSeq; NP_001010966.1; NM_001010966.1.
DR RefSeq; XP_006239117.1; XM_006239055.3.
DR RefSeq; XP_008762381.1; XM_008764159.2.
DR RefSeq; XP_017449031.1; XM_017593542.1.
DR RefSeq; XP_017449032.1; XM_017593543.1.
DR RefSeq; XP_017449033.1; XM_017593544.1.
DR RefSeq; XP_017449034.1; XM_017593545.1.
DR AlphaFoldDB; Q5KR61; -.
DR STRING; 10116.ENSRNOP00000000133; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR PaxDb; Q5KR61; -.
DR Ensembl; ENSRNOT00000000133; ENSRNOP00000000133; ENSRNOG00000000121.
DR GeneID; 366478; -.
DR KEGG; rno:366478; -.
DR UCSC; RGD:1309526; rat.
DR CTD; 55650; -.
DR RGD; 1309526; Pigv.
DR eggNOG; KOG2647; Eukaryota.
DR GeneTree; ENSGT00390000013174; -.
DR InParanoid; Q5KR61; -.
DR OMA; EYFLHIA; -.
DR OrthoDB; 960696at2759; -.
DR PhylomeDB; Q5KR61; -.
DR TreeFam; TF314515; -.
DR Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5KR61; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000000121; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5KR61; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; ISO:RGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:RGD.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 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..492
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246236"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..77
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..136
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..468
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 54701 MW; 3C865F63B5280620 CRC64;
MGLLDPSQKE VLKFAVSCRI LTLVLQALFN IIIPDHHADA FSPPRLAPSG SVDQLVEALL
GGLSRWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLMGTE LLRPLQGLLS ERSCLLVSVA
LLNSLFSVLA AVALHDLGCL VLHCPRQAFC AALLFCLSPA NVFLAAGYSE ALFAFLTFSA
MGQLERGRGW ASGLLFALAA GVRSNGLVSV GFLLHSQCRG FCSSLVVLDP LKGLVKLMAS
LCLSVLTVSL PFALFQYYAY TQFCFPGSAH AIPEPLLRLA SDRGYRLAGD YEPPWCSRAP
PLIYSYIQDV YWNVGLLRYY ELRQVPNFLL ATPVTVLVVW ATWTYVTAHP WLCLTLGLQR
TKDRESLEKP HPGFLSAKVF VYLVHAAALL AFGGLCMHVQ VLTRLLGSST PITYWFPAYL
LQDREPLLRC VDTAPQKLLE NSPPGQKAPR NCVMKLLYNW KTCSPVTKCI LVYFLTYWLL
GLIMHCNFLP WT
