GLTL5_HUMAN
ID GLTL5_HUMAN Reviewed; 443 AA.
AC Q7Z4T8; Q75KN2; Q75MD3; Q8NCV4; Q8WW05; Q9UDR9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
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;
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Guo J.H., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-124.
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=24398516; DOI=10.1073/pnas.1310777111;
RA Takasaki N., Tachibana K., Ogasawara S., Matsuzaki H., Hagiuda J.,
RA Ishikawa H., Mochida K., Inoue K., Ogonuki N., Ogura A., Noce T., Ito C.,
RA Toshimori K., Narimatsu H.;
RT "A heterozygous mutation of GALNTL5 affects male infertility with
RT impairment of sperm motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1120-1125(2014).
RN [5]
RP VARIANT ALA-206.
RX PubMed=28206990; DOI=10.1038/gim.2016.225;
RA Gershoni M., Hauser R., Yogev L., Lehavi O., Azem F., Yavetz H.,
RA Pietrokovski S., Kleiman S.E.;
RT "A familial study of azoospermic men identifies three novel causative
RT mutations in three new human azoospermia genes.";
RL Genet. Med. 19:998-1006(2017).
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.
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=Q7Z4T8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4T8-2; Sequence=VSP_011227, VSP_011228;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis. Weakly or not expressed
CC in other tissues. {ECO:0000269|PubMed:24398516}.
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 -!- DISEASE: Note=Defects in GALNTL5 have been found in a patient with
CC primary infertility due to asthenozoospermia.
CC {ECO:0000269|PubMed:24398516}.
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. No glycosyltransferase activity has been
CC detected in an in vitro assay (PubMed:24398516).
CC {ECO:0000305|PubMed:24398516}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20912.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97318.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC polypeptide N-acetylgalactosaminyltransferase-like protein 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_498";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF440400; AAM20912.1; ALT_FRAME; mRNA.
DR EMBL; AF440404; AAP97318.1; ALT_FRAME; mRNA.
DR EMBL; AC006017; AAD45823.1; -; Genomic_DNA.
DR EMBL; AC074257; AAS07457.1; -; Genomic_DNA.
DR EMBL; AC099345; AAS07428.1; -; Genomic_DNA.
DR EMBL; BC022021; AAH22021.1; -; mRNA.
DR CCDS; CCDS5929.1; -. [Q7Z4T8-1]
DR RefSeq; NP_660335.2; NM_145292.3. [Q7Z4T8-1]
DR RefSeq; XP_006715925.1; XM_006715862.3. [Q7Z4T8-1]
DR AlphaFoldDB; Q7Z4T8; -.
DR SMR; Q7Z4T8; -.
DR BioGRID; 127959; 6.
DR IntAct; Q7Z4T8; 2.
DR STRING; 9606.ENSP00000479207; -.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q7Z4T8; 1 site.
DR iPTMnet; Q7Z4T8; -.
DR MetOSite; Q7Z4T8; -.
DR PhosphoSitePlus; Q7Z4T8; -.
DR BioMuta; GALNTL5; -.
DR DMDM; 322510123; -.
DR MassIVE; Q7Z4T8; -.
DR PaxDb; Q7Z4T8; -.
DR PeptideAtlas; Q7Z4T8; -.
DR PRIDE; Q7Z4T8; -.
DR ProteomicsDB; 69232; -. [Q7Z4T8-1]
DR ProteomicsDB; 69233; -. [Q7Z4T8-2]
DR Antibodypedia; 2318; 99 antibodies from 20 providers.
DR DNASU; 168391; -.
DR Ensembl; ENST00000392800.7; ENSP00000376548.2; ENSG00000106648.14. [Q7Z4T8-1]
DR Ensembl; ENST00000416062.5; ENSP00000411071.1; ENSG00000106648.14. [Q7Z4T8-2]
DR Ensembl; ENST00000431418.6; ENSP00000392582.2; ENSG00000106648.14. [Q7Z4T8-1]
DR Ensembl; ENST00000448366.6; ENSP00000400106.2; ENSG00000106648.14. [Q7Z4T8-2]
DR Ensembl; ENST00000616416.4; ENSP00000479207.1; ENSG00000106648.14. [Q7Z4T8-1]
DR GeneID; 168391; -.
DR KEGG; hsa:168391; -.
DR MANE-Select; ENST00000392800.7; ENSP00000376548.2; NM_145292.4; NP_660335.2.
DR UCSC; uc003wkp.4; human. [Q7Z4T8-1]
DR CTD; 168391; -.
DR DisGeNET; 168391; -.
DR GeneCards; GALNTL5; -.
DR HGNC; HGNC:21725; GALNTL5.
DR HPA; ENSG00000106648; Tissue enriched (testis).
DR MIM; 615133; gene.
DR neXtProt; NX_Q7Z4T8; -.
DR OpenTargets; ENSG00000106648; -.
DR PharmGKB; PA134934705; -.
DR VEuPathDB; HostDB:ENSG00000106648; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000162156; -.
DR HOGENOM; CLU_013477_0_0_1; -.
DR InParanoid; Q7Z4T8; -.
DR OMA; TRNKMCL; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q7Z4T8; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q7Z4T8; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q7Z4T8; -.
DR BioGRID-ORCS; 168391; 10 hits in 1065 CRISPR screens.
DR GenomeRNAi; 168391; -.
DR Pharos; Q7Z4T8; Tbio.
DR PRO; PR:Q7Z4T8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7Z4T8; protein.
DR Bgee; ENSG00000106648; Expressed in sperm and 59 other tissues.
DR ExpressionAtlas; Q7Z4T8; baseline and differential.
DR Genevisible; Q7Z4T8; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IMP: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_0000059143"
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 124..133
FT /note="CLQKHYPARL -> GCSGVPGQPL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011227"
FT VAR_SEQ 134..443
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011228"
FT VARIANT 124
FT /note="C -> R (in dbSNP:rs6960270)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019592"
FT VARIANT 206
FT /note="G -> A (in dbSNP:rs61729482)"
FT /evidence="ECO:0000269|PubMed:28206990"
FT /id="VAR_080036"
SQ SEQUENCE 443 AA; 51427 MW; 4E96286FD6D9EB2D CRC64;
MRNAIIQGLF YGSLTFGIWT ALLFIYLHHN HVSSWQKKSQ EPLSAWSPGK KVHQQIIYGS
EQIPKPHVIV KRTDEDKAKS MLGTDFNHTN PELHKELLKY GFNVIISRSL GIEREVPDTR
SKMCLQKHYP ARLPTASIVI CFYNEECNAL FQTMSSVTNL TPHYFLEEII LVDDMSKVDD
LKEKLDYHLE TFRGKVKIIR NKKREGLIRA RLIGASHASG DVLVFLDSHC EVNRVWLEPL
LHAIAKDPKM VVCPLIDVID DRTLEYKPSP LVRGTFDWNL QFKWDNVFSY EMDGPEGSTK
PIRSPAMSGG IFAIRRHYFN EIGQYDKDMD FWGRENLELS LRIWMCGGQL FIIPCSRVGH
ISKKQTGKPS TIISAMTHNY LRLVHVWLDE YKEQFFLRKP GLKYVTYGNI RERVELRKRL
GCKSFQWYLD NVFPELEASV NSL
