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Protein

Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5

Gene

Galntl5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable inactive glycosyltransferase required during spermatid development. May participate to protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region.1 Publication

Cofactori

Mn2+By similarity

GO - Molecular functioni

GO - Biological processi

  • spermatid development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5
Alternative name(s):
Polypeptide GalNAc transferase 15
Short name:
GalNAc-T15
Short name:
pp-GaNTase 15
Protein-UDP acetylgalactosaminyltransferase 15
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15
Gene namesi
Name:Galntl5
Synonyms:Galnt15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1915159. Galntl5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 431404LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Heterozygous mice show male infertility because of immotile sperm: glycolytic enzymes required for sperm motility are decreased, their protein loading into acrosomes disrupted, and aberrant localization of the ubiquitin-proteasome system is observed. Females show normal fertility.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5PRO_0000059145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi105 ↔ 336By similarity
Disulfide bondi327 ↔ 403By similarity
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence analysis
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9D4M9.
PRIDEiQ9D4M9.

PTM databases

PhosphoSiteiQ9D4M9.

Expressioni

Tissue specificityi

Expressed in testis. Mainly expressed in the round and elongated spermatids during spermiogenesis, not in the outermost cells of the seminiferous tubules, which contain spermatogonia and somatic Sertoli cells. Present in the juxtanuclear space in the round spermatids, not in the acrosomal vesicles. In the elongating spermatids, localizes strongly in the acroplaxome, the region between the developing acrosome and nucleus. During differentiation, also weakly detected in the transient manchette containing microtubules. In epididymal spermatozoa, weakly detected in the midpiece, but concentrates mainly in the neck region around the head-tail coupling apparatus (at protein level).1 Publication

Gene expression databases

BgeeiQ9D4M9.
ExpressionAtlasiQ9D4M9. baseline and differential.
GenevisibleiQ9D4M9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030778.

Structurei

3D structure databases

ProteinModelPortaliQ9D4M9.
SMRiQ9D4M9. Positions 95-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 224111Catalytic subdomain AAdd
BLAST
Regioni282 – 34463Catalytic subdomain BAdd
BLAST

Domaini

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ9D4M9.
KOiK00710.
OMAiVHVWLDE.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ9D4M9.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D4M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSVIIQGLF CGFLAIGLWA SMLLLFLHLE QEDMLENEKE ELLKKRSLGK
60 70 80 90 100
NAHQQTRHSE DVTHDEVNFS DPELIQGLRR YGLNAIMSRR LGIEREVPDS
110 120 130 140 150
RDKICQQKHY PFNLPTASII ICFYNEEFNT LLRAVSSVVN LSPQHLLEEI
160 170 180 190 200
ILVDDMSEFD DLKDKLDYYL EIFRGKVKLI RNKKREGLIR SKMIGASRAS
210 220 230 240 250
GDILVFLDSH CEVNRVWLEP LLHAIAKDHK MVVCPIIDVI NELTLDYMAA
260 270 280 290 300
PIVRGAFDWN LNLRWDNVFA YELDGPEGPS TPIRSPAMTG GIFAINRHYF
310 320 330 340 350
NELGQYDNGM DICGGENVEL SLRIWMCGGQ LFILPCSRVG YNSKALSQHR
360 370 380 390 400
RANQSALSRN LLRVVHVWLD EYKGNFFLQR PSLTYVSCGN ISERVELRKR
410 420 430
LGCKSFQWYL DNIFPELEPF NTERKRKKNR F
Length:431
Mass (Da):49,874
Last modified:August 16, 2004 - v2
Checksum:i60DFB7F8243A7B04
GO

Sequence cautioni

The sequence AAH49554.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761K → E in BAB30220 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005605 mRNA. Translation: BAB24147.1.
AK016415 mRNA. Translation: BAB30220.1.
BC049554 mRNA. Translation: AAH49554.1. Sequence problems.
BC145757 mRNA. Translation: AAI45758.1.
CCDSiCCDS19132.1.
RefSeqiNP_080725.2. NM_026449.3.
UniGeneiMm.141471.

Genome annotation databases

EnsembliENSMUST00000030778; ENSMUSP00000030778; ENSMUSG00000028938.
GeneIDi67909.
KEGGimmu:67909.
UCSCiuc008wsr.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005605 mRNA. Translation: BAB24147.1.
AK016415 mRNA. Translation: BAB30220.1.
BC049554 mRNA. Translation: AAH49554.1. Sequence problems.
BC145757 mRNA. Translation: AAI45758.1.
CCDSiCCDS19132.1.
RefSeqiNP_080725.2. NM_026449.3.
UniGeneiMm.141471.

3D structure databases

ProteinModelPortaliQ9D4M9.
SMRiQ9D4M9. Positions 95-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030778.

Protein family/group databases

CAZyiGT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteiQ9D4M9.

Proteomic databases

PaxDbiQ9D4M9.
PRIDEiQ9D4M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030778; ENSMUSP00000030778; ENSMUSG00000028938.
GeneIDi67909.
KEGGimmu:67909.
UCSCiuc008wsr.1. mouse.

Organism-specific databases

CTDi168391.
MGIiMGI:1915159. Galntl5.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ9D4M9.
KOiK00710.
OMAiVHVWLDE.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ9D4M9.
TreeFamiTF313267.

Miscellaneous databases

NextBioi325916.
PROiQ9D4M9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D4M9.
ExpressionAtlasiQ9D4M9. baseline and differential.
GenevisibleiQ9D4M9. MM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGLTL5_MOUSE
AccessioniPrimary (citable) accession number: Q9D4M9
Secondary accession number(s): A6H655, Q810S4, Q9CW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In contrast to other members of the family, lacks the C-terminal ricin B-type lectin domain that contributes to the glycopeptide specificity, and lacks the conserved His residue in position 341. No glycosyltransferase activity has been detected in an in vitro assay (PubMed:24398516).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.