POMT1_DANRE
ID POMT1_DANRE Reviewed; 720 AA.
AC F1QF89; E0CZJ9; Q08C27; Q0PIP3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein O-mannosyl-transferase 1 {ECO:0000303|PubMed:18632251};
DE EC=2.4.1.109 {ECO:0000269|PubMed:20466645};
GN Name=pomt1 {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:ABH03466.1}
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:BAJ15895.1}
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:AAI24441.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAI24441.1};
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 testis, ovary, brain, liver and heart.
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). 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
CC hpf, the tail is slightly curved and somite boundaries are also
CC abnormally curved. Swim bladders are incompletely formed. Glycosylation
CC of alpha-dystroglycan (dag1) is severely reduced.
CC {ECO:0000269|PubMed:20466645}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; DQ826748; ABH03466.1; -; mRNA.
DR EMBL; AB281275; BAJ15895.1; -; mRNA.
DR EMBL; CU856180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124440; AAI24441.1; -; mRNA.
DR EMBL; BC165221; AAI65221.1; -; mRNA.
DR RefSeq; NP_001041532.2; NM_001048067.2.
DR AlphaFoldDB; F1QF89; -.
DR SMR; F1QF89; -.
DR STRING; 7955.ENSDARP00000086435; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR PaxDb; F1QF89; -.
DR Ensembl; ENSDART00000092002; ENSDARP00000086435; ENSDARG00000067670.
DR Ensembl; ENSDART00000182712; ENSDARP00000157635; ENSDARG00000112005.
DR Ensembl; ENSDART00000188552; ENSDARP00000155683; ENSDARG00000067670.
DR GeneID; 569769; -.
DR KEGG; dre:569769; -.
DR CTD; 10585; -.
DR ZFIN; ZDB-GENE-060929-966; pomt1.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000158049; -.
DR HOGENOM; CLU_008438_1_0_1; -.
DR InParanoid; F1QF89; -.
DR OMA; FWTQNDT; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; F1QF89; -.
DR TreeFam; TF300552; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:F1QF89; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000067670; Expressed in early embryo and 19 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..720
FT /note="Protein O-mannosyl-transferase 1"
FT /id="PRO_0000442137"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 291..354
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 365..422
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 426..486
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CONFLICT 101
FT /note="W -> R (in Ref. 1; ABH03466)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="N -> D (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..174
FT /note="HK -> PQ (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="F -> L (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="F -> S (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> Q (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Q -> R (in Ref. 2; BAJ15895 and 4; AAI24441/
FT AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Q -> H (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="V -> M (in Ref. 1; ABH03466)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="M -> I (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> S (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> R (in Ref. 2; BAJ15895 and 4; AAI24441/
FT AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="H -> R (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="L -> R (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> S (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="M -> K (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="L -> I (in Ref. 4; AAI24441/AAI65221)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="V -> A (in Ref. 2; BAJ15895)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="L -> F (in Ref. 2; BAJ15895 and 4; AAI24441/
FT AAI65221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 82084 MW; 9B26C1D319A7579E CRC64;
MQCVKLPVSV TVEINVLLLA VTALALFTRL YGIHFPKAVV FDEVYYGQFL SLYMKQVFFI
DESGPPFGHM ILALGAYLGG FDGNFVWNRI GAEYPGNVPV WSLRLIPALA GSFCVPLAYL
VVVELGYSHF SALGACALLL MENSLIVQSR FMLLESVLIF FLLLAVLSYL RFHKARNSFF
KWFWLVICGV SCAFGIGVKY MGMFTYFLLL SLAAVHTWQL IGDQTLSHGK VMFQVLVRFL
ALVVLPVIMY LGFFYIHLTL LYRSGPHDQM MSSAFQASLE GGLARITQGQ PLDVAFGSQV
TLRTVSGKPV PCWLHSHKAN YPIRYENGRG SSHQQQVTCY PFKDVNNWWI IKDPGRQSLV
VSSPPKPVRH GDIIQLLHGM TTRYLNTHDV AAPMSPHSQE VSGYIDFNVS MPAQNLWRVD
IVNRESEKEI WKTILSEVRL VHVNTSAVLK LSGASLPEWG FKQLEVVGDK IYKGYQQTGM
WNVEEHRYGR SQEPKERELE LKSPTHSDVN KNLTFMAKFL ELQWKMLTVK NEESEHKYSS
SPLEWITMDT NIAYWLHPSS NAQIHFIGNI VTWTTGNITL VVYCLLFLTY LLRRRRKVED
IPQDSWEQLV LAGVVCLGGW AVNYLPFFLM EKTLFLYHYL PALTFKILQI PIVTEHLYIH
VLRSSAQQKA FGGVILAVLC SVYMSYHSLS PLTYGQPALT SDKLAELRWR ESWDILLRKR
