PIGV_MOUSE
ID PIGV_MOUSE Reviewed; 493 AA.
AC Q7TPN3; Q8BGL2; Q8BJR5; Q8BWH9; Q8BXF5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Adrenal gland, Cerebellum, Corpora quadrigemina, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TPN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPN3-2; Sequence=VSP_019840;
CC -!- PTM: Not N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK046527; BAC32773.1; -; mRNA.
DR EMBL; AK047322; BAC33023.1; ALT_INIT; mRNA.
DR EMBL; AK052446; BAC34995.1; -; mRNA.
DR EMBL; AK080590; BAC37950.1; -; mRNA.
DR EMBL; AK080858; BAC38047.1; -; mRNA.
DR EMBL; AK148285; BAE28458.1; -; mRNA.
DR EMBL; BC055060; AAH55060.1; -; mRNA.
DR CCDS; CCDS18755.1; -. [Q7TPN3-1]
DR CCDS; CCDS51322.1; -. [Q7TPN3-2]
DR RefSeq; NP_001139427.1; NM_001145955.1.
DR RefSeq; NP_001139428.1; NM_001145956.1. [Q7TPN3-2]
DR RefSeq; NP_848813.3; NM_178698.5. [Q7TPN3-1]
DR RefSeq; XP_006538810.1; XM_006538747.3.
DR AlphaFoldDB; Q7TPN3; -.
DR STRING; 10090.ENSMUSP00000050647; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR PhosphoSitePlus; Q7TPN3; -.
DR EPD; Q7TPN3; -.
DR PaxDb; Q7TPN3; -.
DR PRIDE; Q7TPN3; -.
DR ProteomicsDB; 288160; -. [Q7TPN3-1]
DR ProteomicsDB; 288161; -. [Q7TPN3-2]
DR Antibodypedia; 30687; 106 antibodies from 17 providers.
DR Ensembl; ENSMUST00000062118; ENSMUSP00000050647; ENSMUSG00000043257. [Q7TPN3-1]
DR Ensembl; ENSMUST00000067902; ENSMUSP00000065601; ENSMUSG00000043257. [Q7TPN3-2]
DR GeneID; 230801; -.
DR KEGG; mmu:230801; -.
DR UCSC; uc008vdf.2; mouse. [Q7TPN3-1]
DR UCSC; uc008vdg.2; mouse. [Q7TPN3-2]
DR CTD; 55650; -.
DR MGI; MGI:2442480; Pigv.
DR VEuPathDB; HostDB:ENSMUSG00000043257; -.
DR eggNOG; KOG2647; Eukaryota.
DR GeneTree; ENSGT00390000013174; -.
DR HOGENOM; CLU_029048_3_2_1; -.
DR InParanoid; Q7TPN3; -.
DR OMA; EYFLHIA; -.
DR OrthoDB; 960696at2759; -.
DR PhylomeDB; Q7TPN3; -.
DR TreeFam; TF314515; -.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 230801; 11 hits in 71 CRISPR screens.
DR ChiTaRS; Pigv; mouse.
DR PRO; PR:Q7TPN3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TPN3; protein.
DR Bgee; ENSMUSG00000043257; Expressed in ear vesicle and 197 other tissues.
DR Genevisible; Q7TPN3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..493
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246235"
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..469
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 27..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019840"
FT CONFLICT 218
FT /note="C -> F (in Ref. 1; BAC34995)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="D -> N (in Ref. 2; AAH55060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55026 MW; 8A176D43F3CB7F4C CRC64;
MGLLDPSQKE VLRFAVNCRI LTLVLQALFN LIIPDHHADA FCPPRLAPSG SADQLVEGLL
GGLSRWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLMGTE LLRPLQGLLS QRSCLLVSVA
LLNLLFSVLA AVALHDLGCL VLHCPRQALC AALLFCISPA NVFLAAGYSE ALFAFLTFSA
MGQLERGRGW ASGLLFALAA GVRSNGLVSL GFLLHSQCRG FCSSLAVLSP WKPLVKLMAS
VCLSVLIVSL PFALFQYRAY IQFCSPGSAP SIPEPLLQLA ADKGYRLAGE NAPPWCSWDL
PLIYNYIQDV YWNVGLLRYY ELKQVPNFLL ATPVTVLVVW ATWTYVTTHP WLCLTLGLQR
TKDRENPEKP HRGFLSPKVF VYLVHAAALL VFGGLCMHVQ VLTRFLASST PIMYWFPAHL
LQDQEPLLRC VDTEPGKLPQ EKSPPGQKAP RNCLMKLFYD WKRCSPVTRC VLVYFLTYWL
LGLILHCNFL PWT
