POMT2_MOUSE
ID POMT2_MOUSE Reviewed; 820 AA.
AC Q8BGQ4; Q8R4Z0;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein O-mannosyl-transferase 2;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
GN Name=Pomt2;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3), TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Testis;
RX PubMed=12460945; DOI=10.1093/glycob/cwf086;
RA Willer T., Amselgruber W., Deutzmann R., Strahl S.;
RT "Characterization of POMT2, a novel member of the PMT protein O-
RT mannosyltransferase family specifically localized to the acrosome of
RT mammalian spermatids.";
RL Glycobiology 12:771-783(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ;
RA Wang X., Jigami Y.;
RT "A putative mouse O-mannosyltransferase POMT2.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. Coexpression of both POMT1 and POMT2 is
CC necessary for enzyme activity, expression of either POMT1 or POMT2
CC alone is insufficient. Essentially dedicated to O-mannosylation of
CC alpha-DAG1 and few other proteins but not of cadherins and
CC protocaherins. {ECO:0000250|UniProtKB:Q9UKY4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BGQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGQ4-2; Sequence=VSP_007597, VSP_007598, VSP_007599;
CC Name=3;
CC IsoId=Q8BGQ4-3; Sequence=VSP_007597;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the acrosome of cap
CC phase spermatids, in spermatocytes and liver. Isoform 1 seems to be
CC testis-specific. {ECO:0000269|PubMed:12460945}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12460945}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced by use of an alternative
CC promoter. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; AY090481; AAM12047.1; -; mRNA.
DR EMBL; AY090482; AAM12048.1; -; mRNA.
DR EMBL; AY090483; AAM09080.1; -; Genomic_DNA.
DR EMBL; AY090483; AAM09081.1; -; Genomic_DNA.
DR EMBL; AY028993; AAK30026.1; -; Genomic_DNA.
DR EMBL; AF246235; AAL85627.1; -; mRNA.
DR EMBL; AK050915; BAC34458.1; -; mRNA.
DR EMBL; BC052045; AAH52045.1; -; mRNA.
DR CCDS; CCDS26070.1; -. [Q8BGQ4-1]
DR RefSeq; NP_700464.2; NM_153415.4. [Q8BGQ4-1]
DR AlphaFoldDB; Q8BGQ4; -.
DR SMR; Q8BGQ4; -.
DR BioGRID; 229958; 2.
DR STRING; 10090.ENSMUSP00000035260; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyConnect; 2426; 1 N-Linked glycan (1 site). [Q8BGQ4-2]
DR GlyGen; Q8BGQ4; 6 sites.
DR iPTMnet; Q8BGQ4; -.
DR PhosphoSitePlus; Q8BGQ4; -.
DR MaxQB; Q8BGQ4; -.
DR PaxDb; Q8BGQ4; -.
DR PRIDE; Q8BGQ4; -.
DR ProteomicsDB; 291635; -. [Q8BGQ4-1]
DR ProteomicsDB; 291636; -. [Q8BGQ4-2]
DR ProteomicsDB; 291637; -. [Q8BGQ4-3]
DR Antibodypedia; 67; 132 antibodies from 22 providers.
DR DNASU; 217734; -.
DR Ensembl; ENSMUST00000037788; ENSMUSP00000035260; ENSMUSG00000034126. [Q8BGQ4-1]
DR Ensembl; ENSMUST00000222634; ENSMUSP00000152370; ENSMUSG00000034126. [Q8BGQ4-2]
DR GeneID; 217734; -.
DR KEGG; mmu:217734; -.
DR UCSC; uc007oij.1; mouse. [Q8BGQ4-1]
DR CTD; 29954; -.
DR MGI; MGI:2444430; Pomt2.
DR VEuPathDB; HostDB:ENSMUSG00000034126; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000156829; -.
DR HOGENOM; CLU_008438_5_1_1; -.
DR InParanoid; Q8BGQ4; -.
DR OMA; DANDVWR; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q8BGQ4; -.
DR TreeFam; TF300552; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 217734; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Pomt2; mouse.
DR PRO; PR:Q8BGQ4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BGQ4; protein.
DR Bgee; ENSMUSG00000034126; Expressed in spermatid and 221 other tissues.
DR Genevisible; Q8BGQ4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; ISO:MGI.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS50919; MIR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..820
FT /note="Protein O-mannosyl-transferase 2"
FT /id="PRO_0000121489"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 404..460
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 473..529
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 534..591
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12460945,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.2"
FT /id="VSP_007597"
FT VAR_SEQ 667..673
FT /note="VWWLNLV -> SIPALSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007598"
FT VAR_SEQ 674..820
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007599"
SQ SEQUENCE 820 AA; 92386 MW; 7DDD8FC582E012A7 CRC64;
MLYASGRLLA ARAATTLSAP PRARGPALRG KRRELQIPWH LETPSYDPLT GQRTRPGVPP
ARRVILRKGR MPPAIGGGLA GSELRPRRGR CVPQAARAVS RDVVPQAAAR KLKRPAWSSR
RFQAAGWWAT LAVVTLLSFA TRFHRLDQPA HICWDETHFG KMGSYYINRT FFFDVHPPLG
KMLIGLAGYL SGYDGTFLFQ KPGDRYEHHS YMGMRGFCAF LGSWLIPFAY LTVLDLSKSF
PAALLTAALL TFDTGCLTLS QYILLDPILM FFIMAAMLSM VKYNSCANRP FSAPWWFWLS
LTGISLAGAL GVKFVGLFII VQVGLNTISD LWHLFGDLSL SLVTVGKHLT ARILCLIVLP
LVLYVTIFAV HVMVLNKSGP GDGFFSSAFQ ARLSGNSLHN ASIPEHLAYG SVITVKNLRM
AIGYLHSHRH LYPEGIGARQ QQVTTYLHKD YNNLWIIKKY NANTDPLDPS FPVEFVRHGD
IIRLEHKETT RNLHSHYHEA PLTRKHYQVT GYGINGTGDS NDFWRIEVVN RKFGNRIKVL
RSRIRLIHLV TGCVLGSSGK ILPKWGWEQL EVTCTPYLKE TTNSIWNIEE HINPKLPNIS
LDVLQPSFPE ILLESHMVMI RGNNGLKPKD NEFTSKPWHW PINYQGLRFS GANDTDFRVY
LLGNPVVWWL NLVSIVLYLL SGSTIAVAMQ RGIQLPAELQ GLTKVLLRGG GQLLLGWMLH
YFPFFLMGRI LYFHHYFPAM LFSSMLTGIL WDTLLRLCAW GLAPSPLGRR IHAVGILSLL
LTTAYSFYLF HPLAYGMVGP LAQEPESPMA GLRWLESWDF
