PIGB_MOUSE
ID PIGB_MOUSE Reviewed; 542 AA.
AC Q9JJQ0; Q3U585; Q7TQ01;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=GPI mannosyltransferase 3;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase III;
DE Short=GPI-MT-III;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class B protein;
DE Short=PIG-B;
GN Name=Pigb;
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 [MRNA].
RX PubMed=8861954; DOI=10.1002/j.1460-2075.1996.tb00800.x;
RA Takahashi M., Inoue N., Ohishi K., Maeda Y., Nakamura N., Endo Y.,
RA Fujita T., Takeda J., Kinoshita T.;
RT "PIG-B, a membrane protein of the endoplasmic reticulum with a large
RT lumenal domain, is involved in transferring the third mannose of the GPI
RT anchor.";
RL EMBO J. 15:4254-4261(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
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: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-
CC GlcN-acyl-PI during GPI precursor assembly (By similarity).
CC {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 glycosyltransferase 22 family. PIGB
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84436; BAA94827.1; -; mRNA.
DR EMBL; AK153819; BAE32195.1; -; mRNA.
DR EMBL; BC052658; AAH52658.1; -; mRNA.
DR CCDS; CCDS40687.1; -.
DR RefSeq; NP_061377.2; NM_018889.3.
DR AlphaFoldDB; Q9JJQ0; -.
DR BioGRID; 207753; 1.
DR STRING; 10090.ENSMUSP00000139269; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR GlyGen; Q9JJQ0; 1 site.
DR iPTMnet; Q9JJQ0; -.
DR PhosphoSitePlus; Q9JJQ0; -.
DR EPD; Q9JJQ0; -.
DR jPOST; Q9JJQ0; -.
DR MaxQB; Q9JJQ0; -.
DR PaxDb; Q9JJQ0; -.
DR PeptideAtlas; Q9JJQ0; -.
DR PRIDE; Q9JJQ0; -.
DR ProteomicsDB; 289574; -.
DR Antibodypedia; 25067; 95 antibodies from 20 providers.
DR DNASU; 55981; -.
DR Ensembl; ENSMUST00000098566; ENSMUSP00000096165; ENSMUSG00000079469.
DR Ensembl; ENSMUST00000183746; ENSMUSP00000138885; ENSMUSG00000079469.
DR Ensembl; ENSMUST00000184035; ENSMUSP00000139269; ENSMUSG00000079469.
DR Ensembl; ENSMUST00000184389; ENSMUSP00000139076; ENSMUSG00000079469.
DR GeneID; 55981; -.
DR KEGG; mmu:55981; -.
DR UCSC; uc009qqs.1; mouse.
DR CTD; 9488; -.
DR MGI; MGI:1891825; Pigb.
DR VEuPathDB; HostDB:ENSMUSG00000079469; -.
DR eggNOG; KOG1771; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_012353_2_0_1; -.
DR InParanoid; Q9JJQ0; -.
DR OMA; HHMVFNN; -.
DR OrthoDB; 901894at2759; -.
DR PhylomeDB; Q9JJQ0; -.
DR TreeFam; TF313518; -.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 55981; 11 hits in 75 CRISPR screens.
DR ChiTaRS; Pigb; mouse.
DR PRO; PR:Q9JJQ0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JJQ0; protein.
DR Bgee; ENSMUSG00000079469; Expressed in ascending aorta and 170 other tissues.
DR ExpressionAtlas; Q9JJQ0; baseline and differential.
DR Genevisible; Q9JJQ0; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
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 GO; GO:0006505; P:GPI anchor metabolic process; ISS:MGI.
DR GO; GO:0097502; P:mannosylation; ISO:MGI.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR InterPro; IPR039521; PIG-B/GPI10.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..542
FT /note="GPI mannosyltransferase 3"
FT /id="PRO_0000246252"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 208
FT /note="V -> I (in Ref. 1; BAA94827)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="I -> V (in Ref. 3; AAH52658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 63120 MW; D426F71B01011437 CRC64;
MESQAADYNP ASRNLHGSSG EMKLRRRKSR QYVSAQEKRS PRRGLLGENT YLVLFTIALR
ILNCFLVQTS FVPDEYWQSL EVAHRMVFSY GYLTWEWTER LRGYTYPLIF ASIYKVLHLL
GKDSVQFLIW IPRLGQALLS AVADIRLYSL LKQLENQEVA QWVFLCQLCS WFTWYCCTRT
LTNTMETSLT ALALFYYPLE GSRSVNSVKY SLLVALACVV RPTALIPWVP LLFRHFYQEQ
RKLHLTLHHF LPVGFITFSL SLIIDRIFFG QWTLVQLNFL KFNVLQNLGT FYGSHPWHWY
LSQGFPVVLG THLPFFIHGC FLAPRRLHIL LLTVLWTLLV YSMLGHKEFR FIYPVLPFCM
VFCGYSLAHL KTWRKAALSF LLLSNVPLAF YTGLVHQRGT LDVMNHIQKV CPRGPDPASA
SVFIMMPCHS TPYYSHVHCP LSMRFLQCPP DLTGKTQYLD EADMFYLNPL RWLQQEFHSN
ASLPTHLVTF NVLEKEINTF LTSGNYERAA TFFHTHWPER RTGSHIHVYE RRLPGRVNTG
GN
