POMT2_DANRE
ID POMT2_DANRE Reviewed; 756 AA.
AC F1Q8R9; A1L2B0; E0CZK0; Q0PIP2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein O-mannosyl-transferase 2 {ECO:0000303|PubMed:18632251};
DE EC=2.4.1.109 {ECO:0000269|PubMed:20466645};
GN Name=pomt2 {ECO:0000303|PubMed:18632251};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:ABH03467.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=18632251; DOI=10.1016/j.ygeno.2008.05.008;
RA Moore C.J., Goh H.T., Hewitt J.E.;
RT "Genes required for functional glycosylation of dystroglycan are conserved
RT in zebrafish.";
RL Genomics 92:159-167(2008).
RN [2] {ECO:0000312|EMBL:BAJ15896.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20466645; DOI=10.1093/glycob/cwq069;
RA Avsar-Ban E., Ishikawa H., Manya H., Watanabe M., Akiyama S., Miyake H.,
RA Endo T., Tamaru Y.;
RT "Protein O-mannosylation is necessary for normal embryonic development in
RT zebrafish.";
RL Glycobiology 20:1089-1102(2010).
RN [3] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000312|EMBL:AAI29429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAI29429.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000269|PubMed:20466645}.
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 Evidence={ECO:0000269|PubMed:20466645};
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 Evidence={ECO:0000269|PubMed:20466645};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:20466645}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y6A1}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Has particularly strong
CC expression in ovary, testis, liver, brain, muscle, heart and eye.
CC {ECO:0000269|PubMed:20466645}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout development (PubMed:18632251,
CC PubMed:20466645). Highest expression levels are found at 0 hours post-
CC fertilization (hpf), probably due to perdurance of maternal transcripts
CC (PubMed:20466645). Expression levels remain high at 6 hpf and decrease
CC rapidly by 12 hpf, followed by a second moderate peak in expression at
CC 24 hpf (PubMed:20466645). Ubiquitously expressed during early stages of
CC development (PubMed:18632251, PubMed:20466645). At 16-24 hpf, mainly
CC found in eye, brain and somites (PubMed:18632251, PubMed:20466645). At
CC 30 hpf, has strongest expression in forebrain, cerebellum and hindbrain
CC (PubMed:18632251). {ECO:0000269|PubMed:18632251,
CC ECO:0000269|PubMed:20466645}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC developmental delays at 18 hours post fertilization (hpf). At 48-72 hpf
CC the tail is abnormally twisted, and pericardium formation and eye
CC pigmentation are also abnormal. Swim bladders are incompletely formed.
CC Glycosylation of alpha-dystroglycan (dag1) is severely reduced.
CC {ECO:0000269|PubMed:20466645}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI29429.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI64586.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ826749; ABH03467.1; -; mRNA.
DR EMBL; AB281276; BAJ15896.1; -; mRNA.
DR EMBL; BX950192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129428; AAI29429.1; ALT_SEQ; mRNA.
DR EMBL; BC164586; AAI64586.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001038498.1; NM_001045033.1.
DR RefSeq; XP_005158842.1; XM_005158785.3.
DR AlphaFoldDB; F1Q8R9; -.
DR SMR; F1Q8R9; -.
DR STRING; 7955.ENSDARP00000111637; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR PaxDb; F1Q8R9; -.
DR Ensembl; ENSDART00000077307; ENSDARP00000071774; ENSDARG00000055027.
DR Ensembl; ENSDART00000126273; ENSDARP00000111637; ENSDARG00000055027.
DR GeneID; 563878; -.
DR KEGG; dre:563878; -.
DR CTD; 29954; -.
DR ZFIN; ZDB-GENE-070112-1002; pomt2.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000156829; -.
DR HOGENOM; CLU_008438_5_1_1; -.
DR InParanoid; F1Q8R9; -.
DR OMA; DANDVWR; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; F1Q8R9; -.
DR TreeFam; TF300552; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:F1Q8R9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000055027; Expressed in blastula and 36 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IGI:ZFIN.
DR GO; GO:0035269; P:protein O-linked mannosylation; IGI:ZFIN.
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 Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..756
FT /note="Protein O-mannosyl-transferase 2"
FT /id="PRO_0000442138"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 344..400
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 410..466
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 471..528
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CONFLICT 33
FT /note="P -> H (in Ref. 4; AAI29429/AAI64586 and 2;
FT BAJ15896)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="V -> A (in Ref. 2; BAJ15896 and 4; AAI29429/
FT AAI64586)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="R -> M (in Ref. 2; BAJ15896)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="E -> G (in Ref. 2; BAJ15896 and 4; AAI29429/
FT AAI64586)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="H -> R (in Ref. 1; ABH03467)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> P (in Ref. 4; AAI29429/AAI64586)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="L -> P (in Ref. 1; ABH03467)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="Y -> F (in Ref. 4; AAI29429/AAI64586)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="W -> R (in Ref. 2; BAJ15896)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="N -> S (in Ref. 1; ABH03467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 85711 MW; 90A0B81EBD07E126 CRC64;
MDVRPKENFS QRQDTSAVRH RKTCKVNERA EIPSQPHNGT INGVNKRITK REGGEHISSP
SRDAHVPVFI LALVIVLSVS TRFYKITEPP HVCWDETHFG KMGSYYINRT FFFDVHPPLG
KMLIGLAGYL TGYDGTFPFI KPGDKYEHHN YWGMRAFCAA LGSCLPPFAF LVVLELSQSS
TAALIAASLL IFDTGCITLS QYILLDPILM FFIMGSVLCM VKFNTQRLGP FSFSWWFWLL
LTGLCLSGSL GVKFVGLFVI LLVGINTALD LWRLLGDLSL SLVDFGKHLL ARVFGLIMLP
LFLYTTIFAI HFIVLNRSGP GDGFFSSAFQ SRLIGNNLHN ASMPEYLAYG SVITVKNLRI
AGGYLHSHWH LYPEGVGAHQ QQVTAYLHKD YNNLWLVKRL DNSDDLTGSP ELVRHGDIIR
LEHKETTRNL HSHFHEAPLT KKHLQVTGYG INGSGDVNDL WQVEVCGGRK GDPVKVLRSK
VRFLHRATGC VLCSSGKTLP KWGWEQVEVT CSPYVKETPN SQWNIEDHIN PKLPNISLAV
LKPTFLEILW ESHIVMIRGN SGLKPKDNEM NSKPWHWPIN YQGLRFSGVN ETEYRVYLLG
NPVIWWLNLL SLALFVILLT VASLAVQRRV KMEGMMKVHC HTLMEGGGML FLGWLLHYLP
FYIMGRILYY HHYFPAMMFS SMLTGITLDI LLQNLQLLFS SSLSHYLMRG GQSVLLLGFI
YSFYLFHPLS YGMRGPLAHD SASSMAGLRW MESWEF
