MGT4D_RAT
ID MGT4D_RAT Reviewed; 372 AA.
AC Q4V8F8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D {ECO:0000305};
DE AltName: Full=Glycosyltransferase 54 domain-containing protein {ECO:0000303|PubMed:25808494};
DE Short=GL54D {ECO:0000303|PubMed:25808494};
GN Name=Mgat4d {ECO:0000312|RGD:1310572};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=25808494; DOI=10.1091/mbc.e14-12-1632;
RA Au C.E., Hermo L., Byrne E., Smirle J., Fazel A., Simon P.H., Kearney R.E.,
RA Cameron P.H., Smith C.E., Vali H., Fernandez-Rodriguez J., Ma K.,
RA Nilsson T., Bergeron J.J.;
RT "Expression, sorting, and segregation of Golgi proteins during germ cell
RT differentiation in the testis.";
RL Mol. Biol. Cell 26:4015-4032(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:0000269|PubMed:25808494}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:25808494}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:25808494}.
CC -!- DEVELOPMENTAL STAGE: Detected in the Golgi apparatus of pachytene
CC spermatocytes beginning at stage VII and extending up to stage XIV.
CC Detected in the Golgi apparatus of spermatids at steps 1-15 of
CC spermatogenesis. {ECO:0000269|PubMed:25808494}.
CC -!- PTM: N-glycosylated. O-glycosylated; further modified with terminal
CC sialic acid residues. {ECO:0000269|PubMed:25808494}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; BC097408; AAH97408.1; -; mRNA.
DR RefSeq; NP_001020837.1; NM_001025666.1.
DR AlphaFoldDB; Q4V8F8; -.
DR SMR; Q4V8F8; -.
DR STRING; 10116.ENSRNOP00000004982; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q4V8F8; 2 sites.
DR iPTMnet; Q4V8F8; -.
DR PhosphoSitePlus; Q4V8F8; -.
DR PaxDb; Q4V8F8; -.
DR PRIDE; Q4V8F8; -.
DR GeneID; 304646; -.
DR KEGG; rno:304646; -.
DR CTD; 152586; -.
DR RGD; 1310572; Mgat4d.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR HOGENOM; CLU_027046_2_0_1; -.
DR InParanoid; Q4V8F8; -.
DR OMA; CISRMNQ; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q4V8F8; -.
DR TreeFam; TF324570; -.
DR PRO; PR:Q4V8F8; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000003695; Expressed in testis.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
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 Differentiation; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..372
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase-like protein MGAT4D"
FT /id="PRO_0000311678"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..372
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 372 AA; 43112 MW; 536B4E8F34046368 CRC64;
MKTKNVNLLF ALVAVLLFGF SCFCISRMNQ TNNQLINCRN HVLEFKETML RLKNKSENNH
QNLVKVLHQL KHKVAPAKPS GSILEKKVNM LDQDETVFNQ FEVLKFFLPH LRTAGNIYPD
IAIGRQRAGV SFALGITTID RGNHTYLKQT LTSVLSRMTP EEEEDSVVIV SVADTDENYL
KSVVHMVKTR FRKQVQSGAL EVISIPALFY PQTLLEKKTT KNAKNWQIKQ VLDFCILMLY
AQPKATYYLQ LEDDIVAKKM YFTKMKDFVN SVTSKDWFYI EFSVLGFIGK LFRSKDLMDF
VHFFLIFYRA KPIDVLLDDI ALLRMCSFGG PLRSCLQLKR EVRVQYKPSL FQHVGTHSSF
PGREQHLKDH YY
