ID GLTL5_MOUSE Reviewed; 431 AA.
AC Q9D4M9; A6H655; Q810S4; Q9CW06;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 24-JAN-2024, entry version 130.
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 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 [LARGE SCALE MRNA].
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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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).
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. {ECO:0000269|PubMed:24398516}.
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 (PubMed:24398516).
CC {ECO:0000269|PubMed:24398516}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Mainly expressed in the round
CC and elongated spermatids during spermiogenesis, not in the outermost
CC cells of the seminiferous tubules, which contain spermatogonia and
CC somatic Sertoli cells. Present in the juxtanuclear space in the round
CC spermatids, not in the acrosomal vesicles. In the elongating
CC spermatids, localizes strongly in the acroplaxome, the region between
CC the developing acrosome and nucleus. During differentiation, also
CC weakly detected in the transient manchette containing microtubules. In
CC epididymal spermatozoa, weakly detected in the midpiece, but
CC concentrates mainly in the neck region around the head-tail coupling
CC apparatus (at protein level). {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 -!- DISRUPTION PHENOTYPE: Heterozygous mice show male infertility because
CC of immotile sperm: glycolytic enzymes required for sperm motility are
CC decreased, their protein loading into acrosomes disrupted, and aberrant
CC localization of the ubiquitin-proteasome system is observed. Females
CC show normal fertility. {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 that contributes to the
CC glycopeptide specificity, and lacks the conserved His residue in
CC position 341. No glycosyltransferase activity has been detected in an
CC in vitro assay (PubMed:24398516). {ECO:0000305|PubMed:24398516}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49554.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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_mou_523";
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DR EMBL; AK005605; BAB24147.1; -; mRNA.
DR EMBL; AK016415; BAB30220.1; -; mRNA.
DR EMBL; BC049554; AAH49554.1; ALT_SEQ; mRNA.
DR EMBL; BC145757; AAI45758.1; -; mRNA.
DR CCDS; CCDS19132.1; -.
DR RefSeq; NP_080725.2; NM_026449.3.
DR AlphaFoldDB; Q9D4M9; -.
DR SMR; Q9D4M9; -.
DR STRING; 10090.ENSMUSP00000030778; -.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyCosmos; Q9D4M9; 3 sites, No reported glycans.
DR GlyGen; Q9D4M9; 3 sites.
DR PhosphoSitePlus; Q9D4M9; -.
DR PaxDb; 10090-ENSMUSP00000030778; -.
DR ProteomicsDB; 263376; -.
DR Antibodypedia; 2318; 114 antibodies from 21 providers.
DR DNASU; 67909; -.
DR Ensembl; ENSMUST00000030778.9; ENSMUSP00000030778.3; ENSMUSG00000028938.10.
DR GeneID; 67909; -.
DR KEGG; mmu:67909; -.
DR UCSC; uc008wsr.1; mouse.
DR AGR; MGI:1915159; -.
DR CTD; 168391; -.
DR MGI; MGI:1915159; Galntl5.
DR VEuPathDB; HostDB:ENSMUSG00000028938; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000162156; -.
DR InParanoid; Q9D4M9; -.
DR OMA; FNWHLQF; -.
DR OrthoDB; 202750at2759; -.
DR PhylomeDB; Q9D4M9; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR BioGRID-ORCS; 67909; 0 hits in 78 CRISPR screens.
DR PRO; PR:Q9D4M9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D4M9; Protein.
DR Bgee; ENSMUSG00000028938; Expressed in seminiferous tubule of testis and 10 other cell types or tissues.
DR ExpressionAtlas; Q9D4M9; baseline and differential.
DR Genevisible; Q9D4M9; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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 InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11675:SF17; INACTIVE POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE-LIKE PROTEIN 5; 1.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 1: Evidence at protein level;
KW Differentiation; Disulfide bond; Endosome; Glycoprotein; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..431
FT /note="Inactive polypeptide N-
FT acetylgalactosaminyltransferase-like protein 5"
FT /id="PRO_0000059145"
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..431
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 114..224
FT /note="Catalytic subdomain A"
FT REGION 282..344
FT /note="Catalytic subdomain B"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..336
FT /evidence="ECO:0000250"
FT DISULFID 327..403
FT /evidence="ECO:0000250"
FT CONFLICT 176
FT /note="K -> E (in Ref. 1; BAB30220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 49874 MW; 60DFB7F8243A7B04 CRC64;
MKSVIIQGLF CGFLAIGLWA SMLLLFLHLE QEDMLENEKE ELLKKRSLGK NAHQQTRHSE
DVTHDEVNFS DPELIQGLRR YGLNAIMSRR LGIEREVPDS RDKICQQKHY PFNLPTASII
ICFYNEEFNT LLRAVSSVVN LSPQHLLEEI ILVDDMSEFD DLKDKLDYYL EIFRGKVKLI
RNKKREGLIR SKMIGASRAS GDILVFLDSH CEVNRVWLEP LLHAIAKDHK MVVCPIIDVI
NELTLDYMAA PIVRGAFDWN LNLRWDNVFA YELDGPEGPS TPIRSPAMTG GIFAINRHYF
NELGQYDNGM DICGGENVEL SLRIWMCGGQ LFILPCSRVG YNSKALSQHR RANQSALSRN
LLRVVHVWLD EYKGNFFLQR PSLTYVSCGN ISERVELRKR LGCKSFQWYL DNIFPELEPF
NTERKRKKNR F
//
