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   27-MAR-2024, entry version 160.
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}.
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; 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   GlyCosmos; Q8BGQ4; 6 sites, No reported glycans.
DR   GlyGen; Q8BGQ4; 6 sites.
DR   iPTMnet; Q8BGQ4; -.
DR   PhosphoSitePlus; Q8BGQ4; -.
DR   MaxQB; Q8BGQ4; -.
DR   PaxDb; 10090-ENSMUSP00000035260; -.
DR   ProteomicsDB; 291635; -. [Q8BGQ4-1]
DR   ProteomicsDB; 291636; -. [Q8BGQ4-2]
DR   ProteomicsDB; 291637; -. [Q8BGQ4-3]
DR   Pumba; Q8BGQ4; -.
DR   Antibodypedia; 67; 146 antibodies from 23 providers.
DR   DNASU; 217734; -.
DR   Ensembl; ENSMUST00000037788.6; ENSMUSP00000035260.5; ENSMUSG00000034126.6. [Q8BGQ4-1]
DR   Ensembl; ENSMUST00000222634.2; ENSMUSP00000152370.2; ENSMUSG00000034126.6. [Q8BGQ4-2]
DR   GeneID; 217734; -.
DR   KEGG; mmu:217734; -.
DR   UCSC; uc007oij.1; mouse. [Q8BGQ4-1]
DR   AGR; MGI:2444430; -.
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; MCGWDDN; -.
DR   OrthoDB; 5489060at2759; -.
DR   PhylomeDB; Q8BGQ4; -.
DR   TreeFam; TF300552; -.
DR   Reactome; R-MMU-5173105; O-linked glycosylation.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 217734; 4 hits in 78 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 223 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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:0071711; P:basement membrane organization; IMP:MGI.
DR   GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
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   GO; GO:0150103; P:reactive gliosis; IMP:MGI.
DR   Gene3D; 2.80.10.50; -; 1.
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; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
DR   Genevisible; Q8BGQ4; MM.
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
//