MGT4D_MOUSE
ID MGT4D_MOUSE Reviewed; 373 AA.
AC Q9D4R2; E2F697; E9QM08;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D {ECO:0000305};
DE AltName: Full=N-acetylglucosaminyltransferase MGAT1 inhibitory protein;
DE Short=GlcNAcT-I inhibitory protein {ECO:0000303|PubMed:20805325};
DE Short=GnT1IP {ECO:0000303|PubMed:20805325};
GN Name=Mgat4d {ECO:0000312|MGI:MGI:1914805};
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 [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MGAT1; MGAT3 AND
RP MAN2A2, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=20805325; DOI=10.1083/jcb.201004102;
RA Huang H.H., Stanley P.;
RT "A testis-specific regulator of complex and hybrid N-glycan synthesis.";
RL J. Cell Biol. 190:893-910(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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).
RN [5]
RP FUNCTION (ISOFORM 2), INTERACTION WITH MGAT1, SUBCELLULAR LOCATION, AND
RP SELF-ASSOCIATION.
RX PubMed=26371870; DOI=10.7554/elife.08916;
RA Huang H.H., Hassinen A., Sundaram S., Spiess A.N., Kellokumpu S.,
RA Stanley P.;
RT "GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal
RT domain.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: [Isoform 2]: May play a role in male spermatogenesis. In
CC vitro acts as inhibitor of MGAT1 activity causing cell surface proteins
CC to carry mainly high mannose N-glycans. The function is mediated by its
CC lumenal domain and occurs specifically in the Golgi. A catalytic
CC glucosyltransferase activity is not detected. May be involved in
CC regulation of Sertoli-germ cell interactions during specific stages of
CC spermatogenesis. {ECO:0000269|PubMed:20805325,
CC ECO:0000269|PubMed:26371870}.
CC -!- SUBUNIT: Isoform 2 self-associates; specifically in the endoplasmic
CC reticulum prior to its translocation to the Golgi. Isoform 1 and
CC isoform 2 interact with MGAT1, MGAT3 and MAN2A2; isoform 2 interacts
CC specifically with MGAT1 in the Golgi. {ECO:0000269|PubMed:20805325,
CC ECO:0000269|PubMed:26371870}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20805325}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:20805325}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:20805325}; Single-pass type II
CC membrane protein {ECO:0000305|PubMed:20805325}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:20805325}; Single-pass type II membrane
CC protein {ECO:0000305|PubMed:20805325}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q4V8F8}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q4V8F8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GnT1IP-S;
CC IsoId=Q9D4R2-1; Sequence=Displayed;
CC Name=2; Synonyms=GnT1IP-L;
CC IsoId=Q9D4R2-2; Sequence=VSP_058925;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are specifically expressed
CC in testis. Isoform 2 is expressed in spermatocytes but not in
CC spermatids. Isoform 1 is expressed in spermatids.
CC {ECO:0000269|PubMed:20805325}.
CC -!- DEVELOPMENTAL STAGE: Expression of isoform 1 and isoform 2 is up-
CC regulated in testis at postnatal day 17; isoform 1 maintains similar
CC expression levels until the adult; expression of isoform 2 peaks at
CC postnatal day 22 and is barely detected in the adult.
CC {ECO:0000269|PubMed:20805325}.
CC -!- PTM: Isoform 2 is N-glycosylated; consisting of high-mannose and/or
CC hybrid glycans. {ECO:0000269|PubMed:20805325}.
CC -!- MISCELLANEOUS: For isoform 1 inhibition of MGAT1 activity is
CC demonstrated in vitro upon forced membrane-association. Its rat
CC ortholog is the most abundant protein in testis Golgi preparations.
CC {ECO:0000305|PubMed:20805325, ECO:0000305|PubMed:26371870}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=GlcNAcT
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_582";
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DR EMBL; HM067443; ADL28272.1; -; mRNA.
DR EMBL; AK016272; BAB30173.1; -; mRNA.
DR EMBL; AC155304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS22451.1; -. [Q9D4R2-1]
DR RefSeq; NP_080509.2; NM_026233.2. [Q9D4R2-1]
DR AlphaFoldDB; Q9D4R2; -.
DR SMR; Q9D4R2; -.
DR STRING; 10090.ENSMUSP00000041629; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q9D4R2; 3 sites.
DR PhosphoSitePlus; Q9D4R2; -.
DR PaxDb; Q9D4R2; -.
DR PRIDE; Q9D4R2; -.
DR ProteomicsDB; 290227; -. [Q9D4R2-1]
DR ProteomicsDB; 290228; -. [Q9D4R2-2]
DR Antibodypedia; 50004; 66 antibodies from 15 providers.
DR DNASU; 67555; -.
DR Ensembl; ENSMUST00000038692; ENSMUSP00000041629; ENSMUSG00000035057. [Q9D4R2-1]
DR GeneID; 67555; -.
DR KEGG; mmu:67555; -.
DR UCSC; uc009mkb.1; mouse. [Q9D4R2-1]
DR CTD; 152586; -.
DR MGI; MGI:1914805; Mgat4d.
DR VEuPathDB; HostDB:ENSMUSG00000035057; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000161998; -.
DR HOGENOM; CLU_027046_2_0_1; -.
DR InParanoid; Q9D4R2; -.
DR OMA; CISRMNQ; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9D4R2; -.
DR TreeFam; TF324570; -.
DR BioGRID-ORCS; 67555; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D4R2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D4R2; protein.
DR Bgee; ENSMUSG00000035057; Expressed in spermatocyte and 7 other tissues.
DR Genevisible; Q9D4R2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060051; P:negative regulation of protein glycosylation; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Differentiation; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase-like protein MGAT4D"
FT /id="PRO_0000311677"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..373
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MCLGESVGDLRTVATAPWEGEQARGVKDAGSVPVQPGVGSDAATM
FT (in isoform 2)"
FT /id="VSP_058925"
FT CONFLICT 5
FT /note="N -> D (in Ref. 2; BAB30173)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> G (in Ref. 2; BAB30173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 43300 MW; F7802251E51752C5 CRC64;
MKAKNVNLLF AFVAVLLFGF SCFCISRMNQ TNNQLINCRN HVLEFKEIML RLKNKSENHH
QDLMQVLYQM KRKAAHTTRS SGNFLEKKGS ILSQHETLPN QFEVLKYFLP HLRTAGKLYP
AIATSKGRAG VSFALGISTI NRGNHTYLKQ TLTSVLSRMT PEEEEDSVVI VSVADTDESY
LKSVVRMVKT KFRKQVQSGV LEVISIPTLF YPQTLLDKKT KTDSESWQIK QVLDFCILML
YAQPKATYYL QLEDDIVAKK MYFTKMKDFV NSLTSKNWFF IEFSVLGFIG KLFRSKDLTD
FVHFFLMFYE TKPIDILLDD IFLIRVCISG EPVRSCLQRK KGFRIQYRPS LFQHVGTQSS
FPGREQHLKD NYY
