Q9D9X8 (SACA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sperm acrosome membrane-associated protein 3

Alternative name(s):
Lysozyme-like protein 3
Sperm lysozyme-like protein 1
Short name=mSLLP1

Cleaved into the following 2 chains:

1. Sperm acrosome membrane-associated protein 3, membrane form
2. Sperm acrosome membrane-associated protein 3, processed form

Gene names

Name:	Spaca3
Synonyms:	Lyc3, Lyzl3, Sllp1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.5
Subcellular location	Cytoplasmic vesicle › secretory vesicle › 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. Ref.5 Isoform 2: Secreted Potential Ref.5.
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

Keywords
Cellular component	Cytoplasmic vesicle Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro sperm-egg recognition Inferred from mutant phenotype Ref.5. Source: MGI
Cellular component	acrosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	lysozyme activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Sperm acrosome membrane-associated protein 3, membrane form

PRO_0000256221

Chain

95 – 221

127

Sperm acrosome membrane-associated protein 3, processed form

PRO_0000256222

Regions

Topological domain

1 – 69

69

Cytoplasmic Potential

Transmembrane

70 – 90

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

91 – 221

131

Extracellular Potential

Sites

Site

93 – 94

2

Cleavage; to produce processed form By similarity

Amino acid modifications

Disulfide bond

99 ↔ 219

Ref.6

Disulfide bond

123 ↔ 207

Ref.6

Disulfide bond

157 ↔ 172

Ref.6

Disulfide bond

168 ↔ 186

Ref.6

Natural variations

Alternative sequence

1 – 58

58

Missing in isoform 2.

VSP_021330

Experimental info

Sequence conflict

61

1

A → P in BAB24544. Ref.2

Sequence conflict

66 – 67

2

PR → SI in BAB24544. Ref.2

Sequence conflict

212

1

L → P in AAS77887. Ref.1

Secondary structure

1

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221

Helix Strand Turn

Details...

Helix

98 – 107

10

Helix

113 – 115

3

Helix

118 – 129

12

Beta strand

136 – 138

3

Beta strand

144 – 146

3

Turn

147 – 150

4

Turn

153 – 155

3

Beta strand

156 – 158

3

Beta strand

160 – 162

3

Helix

172 – 176

5

Helix

181 – 190

10

Helix

196 – 199

4

Helix

201 – 206

6

Turn

207 – 209

3

Helix

213 – 215

3

Turn

216 – 218

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: E122BB82C730AA3B	FASTA	221	25,020
	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
	Isoform 2 [UniParc]. Checksum: 9FC152947A1B1A27	FASTA	163	18,438
	10 20 30 40 50 60 MEARSRAPRR QLCPPGITWL ALAYLLSCLL ASSKAKVFSR CELAKEMHDF GLDGYRGYNL 70 80 90 100 110 120 ADWVCLAYYT SGFNTNAVDH EADGSTNNGI FQISSRRWCR TLASNGPNLC RIYCTDLLNN 130 140 150 160 DLKDSIVCAM KIVQEPLGLG YWEAWRHHCQ GRDLSDWVDG CDF

References

	« Hide 'large scale' referencesShow '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. , 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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] 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.
[6]	Zheng H., Mandal A., Shumilin I.A., Chruszcz M., Herr J.C., Minor W. Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-221, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00113242.
IPI00874397.

RefSeq

NP_083643.1. NM_029367.1.

UniGene

Mm.26988.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GOI	X-ray	2.30	A/B/C	93-221	[»]

ProteinModelPortal

Q9D9X8.

SMR

Q9D9X8. Positions 93-220.

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSite

Q9D9X8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000103222; ENSMUSP00000099511; ENSMUSG00000053184.
ENSMUST00000103223; ENSMUSP00000099512; ENSMUSG00000053184.

GeneID

75622.

KEGG

mmu:75622.

UCSC

uc007kmk.1. mouse.

Organism-specific databases

CTD

124912.

MGI

MGI:1922872. Spaca3.

Phylogenomic databases

eggNOG

maNOG19753.

GeneTree

ENSGT00550000074398.

HOGENOM

HBG505822.

HOVERGEN

HBG052297.

InParanoid

Q9D9X8.

Gene expression databases

ArrayExpress

Q9D9X8.

Bgee

Q9D9X8.

CleanEx

MM_SPACA3.

Genevestigator

Q9D9X8.

GermOnline

ENSMUSG00000053184. Mus musculus.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

343538.

SOURCE

Search...

Entry information

Entry name

SACA3_MOUSE

Accession

Primary (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:	September 21, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program