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   27-MAR-2024, entry version 133.
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}.
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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   GlyCosmos; Q9JJQ0; 1 site, No reported glycans.
DR   GlyGen; Q9JJQ0; 1 site.
DR   iPTMnet; Q9JJQ0; -.
DR   PhosphoSitePlus; Q9JJQ0; -.
DR   EPD; Q9JJQ0; -.
DR   jPOST; Q9JJQ0; -.
DR   MaxQB; Q9JJQ0; -.
DR   PaxDb; 10090-ENSMUSP00000139269; -.
DR   PeptideAtlas; Q9JJQ0; -.
DR   ProteomicsDB; 289574; -.
DR   Pumba; Q9JJQ0; -.
DR   Antibodypedia; 25067; 99 antibodies from 20 providers.
DR   DNASU; 55981; -.
DR   Ensembl; ENSMUST00000098566.5; ENSMUSP00000096165.5; ENSMUSG00000079469.11.
DR   Ensembl; ENSMUST00000183746.8; ENSMUSP00000138885.2; ENSMUSG00000079469.11.
DR   Ensembl; ENSMUST00000184035.8; ENSMUSP00000139269.2; ENSMUSG00000079469.11.
DR   Ensembl; ENSMUST00000184389.8; ENSMUSP00000139076.2; ENSMUSG00000079469.11.
DR   GeneID; 55981; -.
DR   KEGG; mmu:55981; -.
DR   UCSC; uc009qqs.1; mouse.
DR   AGR; MGI:1891825; -.
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; FNNYGYL; -.
DR   OrthoDB; 37262at2759; -.
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 80 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 173 other cell types or tissues.
DR   ExpressionAtlas; Q9JJQ0; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
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   PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR22760:SF4; GPI MANNOSYLTRANSFERASE 3; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
DR   Genevisible; Q9JJQ0; MM.
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
//