SACA3_MOUSE
ID SACA3_MOUSE Reviewed; 221 AA.
AC Q9D9X8; Q5SUU3; Q6PKP1; Q6PX67;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sperm acrosome membrane-associated protein 3;
DE AltName: Full=Lysozyme-like protein 3;
DE AltName: Full=Sperm lysozyme-like protein 1;
DE Short=mSLLP1;
DE Contains:
DE RecName: Full=Sperm acrosome membrane-associated protein 3, membrane form;
DE Contains:
DE RecName: Full=Sperm acrosome membrane-associated protein 3, processed form;
GN Name=Spaca3; Synonyms=Lyc3, Lyzl3, Sllp1;
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 [GENOMIC DNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=16014814; DOI=10.1095/biolreprod.105.041889;
RA Zhang K., Gao R., Zhang H., Cai X., Shen C., Wu C., Zhao S., Yu L.;
RT "Molecular cloning and characterization of three novel lysozyme-like genes,
RT predominantly expressed in the male reproductive system of humans,
RT belonging to the c-type lysozyme/alpha-lactalbumin family.";
RL Biol. Reprod. 73:1064-1071(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-221 (ISOFORMS 1/2), FUNCTION IN
RP FERTILIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=15982649; DOI=10.1016/j.ydbio.2005.05.008;
RA Herrero M.B., Mandal A., Digilio L.C., Coonrod S.A., Maier B., Herr J.C.;
RT "Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding
RT and fertilization.";
RL Dev. Biol. 284:126-142(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH ASTL.
RX PubMed=22206759; DOI=10.1016/j.ydbio.2011.12.021;
RA Sachdev M., Mandal A., Mulders S., Digilio L.C., Panneerdoss S.,
RA Suryavathi V., Pires E., Klotz K.L., Hermens L., Herrero M.B.,
RA Flickinger C.J., van Duin M., Herr J.C.;
RT "Oocyte specific oolemmal SAS1B involved in sperm binding through intra-
RT acrosomal SLLP1 during fertilization.";
RL Dev. Biol. 363:40-51(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-221, AND DISULFIDE BONDS.
RA Zheng H., Mandal A., Shumilin I.A., Chruszcz M., Herr J.C., Minor W.;
RL Submitted (APR-2006) to the PDB data bank.
CC -!- FUNCTION: Sperm surface membrane protein that may be involved in sperm-
CC egg plasma membrane adhesion and fusion during fertilization. It could
CC be a potential receptor for the egg oligosaccharide residue N-
CC acetylglucosamine, which is present in the extracellular matrix over
CC the egg plasma membrane. The processed form has no detectable
CC bacteriolytic activity in vitro (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15982649}.
CC -!- SUBUNIT: Interacts with ASTL. {ECO:0000269|PubMed:22206759}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000305|PubMed:15982649}; Single-pass type II membrane
CC protein {ECO:0000305|PubMed:15982649}. Note=Anterior acrosome in non-
CC capacitated spermatozoa and retained in the equatorial segment and in
CC the luminal face of both the inner and outer acrosomal membranes
CC following capacitation and the acrosome reaction.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9X8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9X8-2; Sequence=VSP_021330;
CC -!- TISSUE SPECIFICITY: The processed form is expressed in sperm (at
CC protein level). Expressed strongly in testis and epididymis and weakly
CC in pancreas. {ECO:0000269|PubMed:15982649,
CC ECO:0000269|PubMed:16014814}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Thr-
CC 128 and Asn-145 are present instead of the conserved Glu and Asp which
CC are active site residues. It is therefore expected that this protein
CC lacks hydrolase activity. {ECO:0000305}.
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; AY572448; AAS77887.1; -; mRNA.
DR EMBL; AK006357; BAB24544.1; -; mRNA.
DR EMBL; AL645842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100503; AAI00504.1; -; mRNA.
DR EMBL; AY601763; AAT07446.1; -; mRNA.
DR CCDS; CCDS25136.1; -. [Q9D9X8-2]
DR RefSeq; NP_083643.1; NM_029367.1. [Q9D9X8-2]
DR RefSeq; XP_011247596.1; XM_011249294.2.
DR PDB; 4YF2; X-ray; 2.15 A; A/B/C=93-221.
DR PDBsum; 4YF2; -.
DR AlphaFoldDB; Q9D9X8; -.
DR SMR; Q9D9X8; -.
DR STRING; 10090.ENSMUSP00000099511; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PhosphoSitePlus; Q9D9X8; -.
DR PaxDb; Q9D9X8; -.
DR PeptideAtlas; Q9D9X8; -.
DR PRIDE; Q9D9X8; -.
DR ProteomicsDB; 260816; -. [Q9D9X8-1]
DR ProteomicsDB; 260817; -. [Q9D9X8-2]
DR Antibodypedia; 15460; 71 antibodies from 20 providers.
DR Ensembl; ENSMUST00000103222; ENSMUSP00000099511; ENSMUSG00000053184. [Q9D9X8-2]
DR Ensembl; ENSMUST00000103223; ENSMUSP00000099512; ENSMUSG00000053184. [Q9D9X8-2]
DR GeneID; 75622; -.
DR KEGG; mmu:75622; -.
DR UCSC; uc007kmk.1; mouse. [Q9D9X8-1]
DR CTD; 124912; -.
DR MGI; MGI:1922872; Spaca3.
DR VEuPathDB; HostDB:ENSMUSG00000053184; -.
DR eggNOG; ENOG502S1F5; Eukaryota.
DR GeneTree; ENSGT00940000161810; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; Q9D9X8; -.
DR OMA; MYCTDLL; -.
DR PhylomeDB; Q9D9X8; -.
DR TreeFam; TF324882; -.
DR BioGRID-ORCS; 75622; 4 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q9D9X8; -.
DR PRO; PR:Q9D9X8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D9X8; protein.
DR Bgee; ENSMUSG00000053184; Expressed in spermatid and 10 other tissues.
DR ExpressionAtlas; Q9D9X8; baseline and differential.
DR Genevisible; Q9D9X8; MM.
DR GO; GO:0043159; C:acrosomal matrix; ISO:MGI.
DR GO; GO:0002080; C:acrosomal membrane; ISO:MGI.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:UniProtKB.
DR GO; GO:0035036; P:sperm-egg recognition; IMP:MGI.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR030058; LYZL3.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF25; PTHR11407:SF25; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle; Disulfide bond;
KW Membrane; Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..221
FT /note="Sperm acrosome membrane-associated protein 3,
FT membrane form"
FT /id="PRO_0000256221"
FT CHAIN 95..221
FT /note="Sperm acrosome membrane-associated protein 3,
FT processed form"
FT /id="PRO_0000256222"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 94..221
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT SITE 93..94
FT /note="Cleavage; to produce processed form"
FT /evidence="ECO:0000250"
FT DISULFID 99..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|Ref.8"
FT DISULFID 123..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|Ref.8"
FT DISULFID 157..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|Ref.8"
FT DISULFID 168..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|Ref.8"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021330"
FT CONFLICT 61
FT /note="A -> P (in Ref. 2; BAB24544)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..67
FT /note="PR -> SI (in Ref. 2; BAB24544)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> P (in Ref. 1; AAS77887)"
FT /evidence="ECO:0000305"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:4YF2"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4YF2"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4YF2"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4YF2"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4YF2"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4YF2"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:4YF2"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4YF2"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4YF2"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:4YF2"
SQ SEQUENCE 221 AA; 25020 MW; E122BB82C730AA3B CRC64;
MGICMSMYTQ VLVPVDADGD HHILWSRFYE RWGSCFNPCA GLVNCLPPHS SALYLCHRME
ARSRAPRRQL CPPGITWLAL AYLLSCLLAS SKAKVFSRCE LAKEMHDFGL DGYRGYNLAD
WVCLAYYTSG FNTNAVDHEA DGSTNNGIFQ ISSRRWCRTL ASNGPNLCRI YCTDLLNNDL
KDSIVCAMKI VQEPLGLGYW EAWRHHCQGR DLSDWVDGCD F
