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Reviewed, UniProtKB/Swiss-Prot Q9D9X8 (SACA3_MOUSE)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sperm acrosome membrane-associated protein 3
Alternative name(s):
    Sperm lysozyme-like protein 1
      Short name=mSLLP1
    Lysozyme-like protein 3
Cleaved into the following 2 chains:
    1- Recommended name:
            Sperm acrosome membrane-associated protein 3, membrane form
    2- Recommended name:
            Sperm acrosome membrane-associated protein 3, processed form
Gene names
Name: Spaca3
Synonyms: Lyc3, Lyzl3, Sllp1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro By similarity.

Subcellular location

Acrosome membrane; Single-pass type II membrane protein Probable. Note: Anterior acrosome in non-capacitated spermatozoa and retained in the equatorial segment and in the luminal face of both the inner and outer acrosomal membranes following capacitation and the acrosome reaction.

Isoform 2: Secreted Potential.

Tissue specificity

The processed form is expressed in sperm (at protein level). Expressed strongly in testis and epididymis and weakly in pancreas. Ref.1 Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Caution

Lacks the conserved Glu and Asp residues, respectively in positions 128 and 145, essential for activity.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D9X8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q9D9X8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Sperm acrosome membrane-associated protein 3, membrane form
PRO_0000256221
Chain95 – 221127Sperm acrosome membrane-associated protein 3, processed form
PRO_0000256222

Regions

Topological domain1 – 6969Cytoplasmic Potential
Transmembrane70 – 9021Signal-anchor for type II membrane protein Potential
Topological domain91 – 221131Extracellular Potential

Sites

Site93 – 942Cleavage; to produce processed form By similarity

Amino acid modifications

Disulfide bond99 ↔ 219 By similarity
Disulfide bond123 ↔ 207 By similarity
Disulfide bond157 ↔ 172 By similarity
Disulfide bond168 ↔ 186 By similarity

Natural variations

Alternative sequence1 – 5858Missing in isoform 2.
VSP_021330

Experimental info

Sequence conflict611A → P in BAB24544. Ref.2
Sequence conflict66 – 672PR → SI in BAB24544. Ref.2
Sequence conflict2121L → P in AAS77887. Ref.1

Secondary structure

............................. 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: E122BB82C730AA3B

FASTA22125,020
        10         20         30         40         50         60 
MGICMSMYTQ VLVPVDADGD HHILWSRFYE RWGSCFNPCA GLVNCLPPHS SALYLCHRME 

        70         80         90        100        110        120 
ARSRAPRRQL CPPGITWLAL AYLLSCLLAS SKAKVFSRCE LAKEMHDFGL DGYRGYNLAD 

       130        140        150        160        170        180 
WVCLAYYTSG FNTNAVDHEA DGSTNNGIFQ ISSRRWCRTL ASNGPNLCRI YCTDLLNNDL 

       190        200        210        220 
KDSIVCAMKI VQEPLGLGYW EAWRHHCQGR DLSDWVDGCD F 

« Hide

Isoform 2.

Checksum: 9FC152947A1B1A27
Show »

FASTA16318,438

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of three novel lysozyme-like genes, predominantly expressed in the male reproductive system of humans, belonging to the c-type lysozyme/alpha-lactalbumin family."
Zhang K., Gao R., Zhang H., Cai X., Shen C., Wu C., Zhao S., Yu L.
Biol. Reprod. 73:1064-1071(2005) [PubMed: 16014814] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Testis.
[2]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Testis.
[3]The mouse genome sequencing consortium
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[5]"Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization."
Herrero M.B., Mandal A., Digilio L.C., Coonrod S.A., Maier B., Herr J.C.
Dev. Biol. 284:126-142(2005) [PubMed: 15982649] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-221 (ISOFORMS 1/2), FUNCTION IN FERTILIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Testis.

Cross-references

Sequence databases

AY572448 mRNA. Translation: AAS77887.1.
AK006357 mRNA. Translation: BAB24544.1.
AL645842 Genomic DNA. Translation: CAI24498.1.
BC100503 mRNA. Translation: AAI00504.1.
AY601763 mRNA. Translation: AAT07446.1.
IPIIPI00113242.
IPI00874397.
RefSeqNP_083643.1.
UniGeneMm.26988

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GOIX-ray2.30A/B/C93-221[»]
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Genome annotation databases

EnsemblENSMUSG00000053184. Mus musculus. [Contig view]
GeneID75622.
KEGGmmu:75622.

Organism-specific databases

MGIMGI:1922872. Spaca3.

Phylogenomic databases

HOVERGENQ9D9X8.

Gene expression databases

ArrayExpressQ9D9X8.
BgeeQ9D9X8.
CleanExMM_SPACA3.
GermOnlineENSMUSG00000053184. Mus musculus.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio343538.
SOURCESearch...

Entry information

Entry nameSACA3_MOUSE
AccessionPrimary (citable) accession number: Q9D9X8
Secondary accession number(s): Q5SUU3, Q6PKP1, Q6PX67
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents