MGT4D_HUMAN
ID MGT4D_HUMAN Reviewed; 374 AA.
AC A6NG13;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 3.
DT 03-AUG-2022, entry version 90.
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;
DE Short=GnT1IP;
GN Name=MGAT4D {ECO:0000312|HGNC:HGNC:43619};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16773575; DOI=10.1086/504639;
RA Hodgson U., Pulkkinen V., Dixon M., Peyrard-Janvid M., Rehn M., Lahermo P.,
RA Ollikainen V., Salmenkivi K., Kinnula V., Kere J., Tukiainen P.,
RA Laitinen T.;
RT "ELMOD2 is a candidate gene for familial idiopathic pulmonary fibrosis.";
RL Am. J. Hum. Genet. 79:149-154(2006).
RN [3]
RP TISSUE SPECIFICITY.
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: May play a role in male spermatogenesis. In vitro acts as
CC inhibitor of MGAT1 activity causing cell surface proteins to carry
CC mainly high mannose N-glycans. The function is mediated by its lumenal
CC 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:0000250|UniProtKB:Q9D4R2}.
CC -!- SUBUNIT: May self-associate; specifically in the endoplasmic reticulum
CC prior to its translocation to the Golgi. Interacts with MGAT1, MGAT3
CC and MAN2A2; may interact with MGTA1 specifically in the Golgi.
CC {ECO:0000250|UniProtKB:Q9D4R2, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q4V8F8}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q4V8F8}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Poorly expressed in testis
CC biopsies from men with impaired spermatogenesis.
CC {ECO:0000269|PubMed:16773575, ECO:0000269|PubMed:26371870}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AC093671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS64066.1; -.
DR RefSeq; NP_001264282.1; NM_001277353.1.
DR AlphaFoldDB; A6NG13; -.
DR BioGRID; 127455; 1.
DR IntAct; A6NG13; 1.
DR STRING; 9606.ENSP00000421185; -.
DR GlyGen; A6NG13; 4 sites.
DR BioMuta; MGAT4D; -.
DR MassIVE; A6NG13; -.
DR PaxDb; A6NG13; -.
DR PeptideAtlas; A6NG13; -.
DR PRIDE; A6NG13; -.
DR Antibodypedia; 50004; 66 antibodies from 15 providers.
DR DNASU; 152586; -.
DR Ensembl; ENST00000511113.6; ENSP00000421185.1; ENSG00000205301.12.
DR GeneID; 152586; -.
DR KEGG; hsa:152586; -.
DR MANE-Select; ENST00000511113.6; ENSP00000421185.1; NM_001277353.2; NP_001264282.1.
DR UCSC; uc031shc.2; human.
DR CTD; 152586; -.
DR DisGeNET; 152586; -.
DR GeneCards; MGAT4D; -.
DR HGNC; HGNC:43619; MGAT4D.
DR HPA; ENSG00000205301; Tissue enriched (testis).
DR MIM; 610310; gene.
DR neXtProt; NX_A6NG13; -.
DR OpenTargets; ENSG00000205301; -.
DR VEuPathDB; HostDB:ENSG00000205301; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000161998; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; A6NG13; -.
DR PathwayCommons; A6NG13; -.
DR SignaLink; A6NG13; -.
DR BioGRID-ORCS; 152586; 14 hits in 920 CRISPR screens.
DR GenomeRNAi; 152586; -.
DR Pharos; A6NG13; Tdark.
DR PRO; PR:A6NG13; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; A6NG13; protein.
DR Bgee; ENSG00000205301; Expressed in left testis and 32 other tissues.
DR ExpressionAtlas; A6NG13; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Differentiation; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..374
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase-like protein MGAT4D"
FT /id="PRO_0000311676"
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..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 374 AA; 43743 MW; 5A7BF88C45D265AB CRC64;
MRTKQVNLLI TLVAVALFSF SCFSIYRITQ TNNQLINCRN HILEFKENML HLRNKTEKNT
QEMMKVLNRM KYEITKREIL SGNLVAQKAD ILNKNETVSN TFEDLKFFFP HLRKEGRIYP
DVIIGKGKTG VSFALGISTV NRGNYSYLKQ TLTSVVSRMT LSQEKDSVVI VLVADSNEDY
LHSVVKMITK KFKRQVRSGS LEVISIPAFL YSSMLNAKHL AEASQKLASW RIKQVLDFCI
LLLYAQPKAK YYLQLEDDII AKEMYFTKIT DFVGNISSNN WFFIEFSMLG FIGKLFRSED
LTHFVRFFLM FYKEKPIDWL LNDIFQVKVC DAGEDLRNCM KRKKQIRIQY KPSLFQHVGI
HSSFPRKEQY EKKI
