GLTL5_MACFA
ID GLTL5_MACFA Reviewed; 443 AA.
AC Q95JX4; Q95K07; Q95K42;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5;
DE AltName: Full=Polypeptide GalNAc transferase 15;
DE Short=GalNAc-T15;
DE Short=pp-GaNTase 15;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 15;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15;
GN Name=GALNTL5; Synonyms=GALNT15;
GN ORFNames=QtsA-10105, QtsA-11465, QtsA-12718;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RA Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA Sugano S.;
RT "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT libraries.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable inactive glycosyltransferase required during
CC spermatid development. May participate in protein loading into the
CC acrosomes and accumulation of ubiquitin-proteasome systems around the
CC head-tail coupling apparatus region (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000305}; Single-pass
CC type II membrane protein {ECO:0000305}. Note=Localizes to the
CC juxtanuclear region, possibly the late endosome. Not localized in the
CC Golgi apparatus in round spermatids (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95JX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95JX4-2; Sequence=VSP_011229, VSP_011230;
CC -!- TISSUE SPECIFICITY: Expressed in testis.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the C-
CC terminal ricin B-type lectin domain, which contributes to the
CC glycopeptide specificity. The precise function of the enzyme is
CC therefore unsure. {ECO:0000305}.
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DR EMBL; AB069985; BAB62930.1; -; mRNA.
DR EMBL; AB070020; BAB62965.1; -; mRNA.
DR EMBL; AB070053; BAB62998.1; -; mRNA.
DR RefSeq; NP_001274585.1; NM_001287656.1.
DR RefSeq; XP_005551282.1; XM_005551225.2.
DR AlphaFoldDB; Q95JX4; -.
DR SMR; Q95JX4; -.
DR STRING; 9541.XP_005551282.1; -.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GeneID; 102130593; -.
DR CTD; 168391; -.
DR eggNOG; KOG3736; Eukaryota.
DR OrthoDB; 606683at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Differentiation; Disulfide bond; Endosome;
KW Glycoprotein; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="Inactive polypeptide N-
FT acetylgalactosaminyltransferase-like protein 5"
FT /id="PRO_0000059144"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 133..243
FT /note="Catalytic subdomain A"
FT REGION 301..363
FT /note="Catalytic subdomain B"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..355
FT /evidence="ECO:0000250"
FT DISULFID 346..422
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011229"
FT VAR_SEQ 71..83
FT /note="KRTDEDKAESTLG -> MPAQCFLHSLQNC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011230"
FT CONFLICT 225
FT /note="I -> F (in Ref. 2; BAB62930/BAB62998)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="R -> C (in Ref. 2; BAB62930/BAB62998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51584 MW; 241C9D47694A74C3 CRC64;
MRNAIIRCLF YGSLTFGIWT ALLFIYLHHN HVSNWQKKSH EPLSAWSPGK KVHQQIIYGS
DQIPKPHVIV KRTDEDKAES TLGMDFNHTN PELHNELLKY GFNVIISRSL GIEREVPDTR
NKMCLQKHYP ARLPTASIVI CFHNEEFHAL FRTVSSVMNL TPHYFLEEII LVDDMSEVDD
LKEKLDYHLE TFRGKIKIIR NKKREGLIRA RLIGASHASG DVLVILDSHC EVNRVWLEPL
LHAIAKDPKM VVRPLIDVID DRTLEYKPSP VVRGAFDWNL QFKWDNVFSY EMDGPEGPTK
PIRSPAMSGG IFAIRRHYFN EIGQYDKDMD FWGGENLELS LRIWMCGGQL FIIPCSRVGH
ISKKQTRKTS AIISATIHNY LRLVHVWLDE YKEQFFLRKP GLKYVTYGNI HERVQLRKRL
GCKSFQWYLD NVFPELEASV NRS
