APTG1_ARATH
ID APTG1_ARATH Reviewed; 548 AA.
AC Q94A15; Q9LEQ5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Mannosyltransferase APTG1 {ECO:0000305};
DE EC=2.4.1.-;
DE AltName: Full=Glycosyltransferase 22 {ECO:0000303|PubMed:24905498};
DE AltName: Full=Protein ABNORMAL POLLEN TUBE GUIDANCE 1 {ECO:0000303|PubMed:24963069, ECO:0000303|PubMed:27872247};
GN Name=APTG1 {ECO:0000303|PubMed:24963069, ECO:0000303|PubMed:27872247};
GN Synonyms=GT22 {ECO:0000303|PubMed:24905498};
GN OrderedLocusNames=At5g14850 {ECO:0000312|Araport:AT5G14850};
GN ORFNames=T9L3.150 {ECO:0000312|EMBL:CAC01884.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24963069; DOI=10.1104/pp.114.236133;
RA Dai X.R., Gao X.-Q., Chen G.H., Tang L.L., Wang H., Zhang X.S.;
RT "ABNORMAL POLLEN TUBE GUIDANCE1, an endoplasmic reticulum-localized
RT mannosyltransferase homolog of GLYCOSYLPHOSPHATIDYLINOSITOL10 in yeast and
RT PHOSPHATIDYLINOSITOL GLYCAN ANCHOR BIOSYNTHESIS B in human, is required for
RT Arabidopsis pollen tube micropylar guidance and embryo development.";
RL Plant Physiol. 165:1544-1556(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27872247; DOI=10.1104/pp.16.01719;
RA Gao H., Zhang Y., Wang W., Zhao K., Liu C., Bai L., Li R., Guo Y.;
RT "Two membrane-anchored aspartic proteases contribute to pollen and ovule
RT development.";
RL Plant Physiol. 173:219-239(2017).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis (PubMed:24963069). Required for the pollen tube
CC micropylar guidance and embryo development by regulating GPI-anchor
CC mediated protein localization (e.g. COBL10 and A36) (PubMed:24963069,
CC PubMed:27872247). {ECO:0000269|PubMed:24963069,
CC ECO:0000269|PubMed:27872247}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24963069}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed, mainly in vascular tissues, in
CC leaves, roots, stems, flowers, siliques and pollen, and, to a lower
CC extent, in seedlings. {ECO:0000269|PubMed:24963069}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vascular tissue of seedlings, leaves,
CC root tips, inflorescence stems and flowers (PubMed:24963069). In
CC pistils, detected in the ovary walls, styles, mature embryo sacs and
CC developing embryos (PubMed:24963069). In pollen grains, mostly present
CC in mature grains at anthesis and in germinated pollen tubes
CC (PubMed:24963069). {ECO:0000269|PubMed:24963069}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at the globular or earlier
CC stages (PubMed:24963069). Compromised pollen tubes micropylar guidance,
CC but normal pollen germination and tube growth, associated with an
CC abnormal localization of GPI-anchored proteins (e.g. COBL10)
CC (PubMed:24963069). Impaired apical plasma membrane localization of
CC COBL10 in pollen tubes, important for the growth of pollen tubes in the
CC transmitting tract of pistil (PubMed:24963069). Lost A36 plasma
CC membrane and cytoplasmic punctate localization which displays a
CC constitutive reticular localization (PubMed:27872247).
CC {ECO:0000269|PubMed:24963069, ECO:0000269|PubMed:27872247}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01884.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138692; AHL38632.1; -; mRNA.
DR EMBL; AL391149; CAC01884.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92081.1; -; Genomic_DNA.
DR EMBL; AY050456; AAK91470.1; -; mRNA.
DR EMBL; AY120693; AAM52236.1; -; mRNA.
DR PIR; T51430; T51430.
DR RefSeq; NP_568305.1; NM_121489.2.
DR AlphaFoldDB; Q94A15; -.
DR STRING; 3702.AT5G14850.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR PaxDb; Q94A15; -.
DR ProteomicsDB; 175714; -.
DR EnsemblPlants; AT5G14850.1; AT5G14850.1; AT5G14850.
DR GeneID; 831337; -.
DR Gramene; AT5G14850.1; AT5G14850.1; AT5G14850.
DR KEGG; ath:AT5G14850; -.
DR Araport; AT5G14850; -.
DR TAIR; locus:2185485; AT5G14850.
DR eggNOG; KOG1771; Eukaryota.
DR HOGENOM; CLU_012353_2_1_1; -.
DR InParanoid; Q94A15; -.
DR OrthoDB; 901894at2759; -.
DR PhylomeDB; Q94A15; -.
DR PRO; PR:Q94A15; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94A15; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IGI:TAIR.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR InterPro; IPR039521; PIG-B/GPI10.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..548
FT /note="Mannosyltransferase APTG1"
FT /id="PRO_0000450670"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 548 AA; 62701 MW; 125D3BEA0BF6A098 CRC64;
MDIRKRKNAG GDGDGGADGA SVNVGDEPDS FGGRIGSPRR IFLFCLAFRV VNALLIQTYF
NPDEHWQSLE VAHRTIFGYG YMTWEWKRGI RSYLHPMLFA FLYKLLQVTG LDTPYIMIKA
PRLMQSIFSA IGDLYLYKLS DALYGGNVAT WSLFCQMANW FIFFCLNRTF SNCLETVLTI
MGLYYWPCIR DSSIDYPVNR KWGLVIAALA CAIRPTSAVI WLYVGMLELF LTPNKVKFII
LEVIPIGSLV LGFTCLLDRL MYGSWVIVPL NFLKFNFLSS GGDYYGTHPW HWYFTQGFLV
MLFTFTPFSI AGIIKSKNQK LSALILWVLA IYSILGHKEF RFVLPVLPIA LIFSGYAFAQ
MEVSGSSSSS SVTKKKQVPR QNHTKWSPKL RLSVYFLLAT NIPMALYMSL FHQRGTEDAM
NYLSDEAYKG RVKSILFLMP CHSTPYYSTL HRNIPMQFLD CTPSAEKGEL DESDQFLVNP
LGFASELARN WSEPPSHIVL FASEETKLRD FMIQHSFKEV RRFFHAHFKV DRDLQSSVVV
YVVNHAFP
