SACA1_MOUSE
ID SACA1_MOUSE Reviewed; 305 AA.
AC Q9DA48;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sperm acrosome membrane-associated protein 1;
DE Flags: Precursor;
GN Name=Spaca1;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22949614; DOI=10.1242/dev.081778;
RA Fujihara Y., Satouh Y., Inoue N., Isotani A., Ikawa M., Okabe M.;
RT "SPACA1-deficient male mice are infertile with abnormally shaped sperm
RT heads reminiscent of globozoospermia.";
RL Development 139:3583-3589(2012).
CC -!- FUNCTION: Plays a role in acrosome expansion and establishment of
CC normal sperm morphology during spermatogenesis. Important for male
CC fertility. {ECO:0000269|PubMed:22949614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC inner membrane {ECO:0000269|PubMed:22949614}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Primarily found in the equatorial
CC segment of the acrosome (PubMed:22949614). The tyrosine phosphorylated
CC protein localizes to a smaller region within the equatorial segment (By
CC similarity). Also expressed weakly in the principal segment (By
CC similarity). {ECO:0000250|UniProtKB:D5K8A9,
CC ECO:0000250|UniProtKB:Q9HBV2}.
CC -!- TISSUE SPECIFICITY: Testis specific (at protein level).
CC {ECO:0000269|PubMed:22949614}.
CC -!- DEVELOPMENTAL STAGE: Detected in testis from 3 weeks of age onwards.
CC {ECO:0000269|PubMed:22949614}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22949614}.
CC -!- DISRUPTION PHENOTYPE: Males are sterile, while female fertility is not
CC affected. Spermatozoa have significantly impaired swimming ability. The
CC sperm head has a rounded shape instead of the normal hook-shaped
CC morphology. The acrosome membrane does not associate normally with the
CC nuclear envelope or intermediate filament bundles, and fails to expand
CC along the nuclear surface. The sperm nucleus remains globular and
CC mitochondria appear disorganized. {ECO:0000269|PubMed:22949614}.
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DR EMBL; AK006187; BAB24447.1; -; mRNA.
DR CCDS; CCDS18026.1; -.
DR RefSeq; NP_080569.1; NM_026293.3.
DR AlphaFoldDB; Q9DA48; -.
DR STRING; 10090.ENSMUSP00000029927; -.
DR GlyGen; Q9DA48; 1 site.
DR iPTMnet; Q9DA48; -.
DR PhosphoSitePlus; Q9DA48; -.
DR PaxDb; Q9DA48; -.
DR PRIDE; Q9DA48; -.
DR ProteomicsDB; 256583; -.
DR Antibodypedia; 18684; 125 antibodies from 21 providers.
DR Ensembl; ENSMUST00000029927; ENSMUSP00000029927; ENSMUSG00000028264.
DR GeneID; 67652; -.
DR KEGG; mmu:67652; -.
DR UCSC; uc008sfz.1; mouse.
DR CTD; 81833; -.
DR MGI; MGI:1914902; Spaca1.
DR VEuPathDB; HostDB:ENSMUSG00000028264; -.
DR eggNOG; ENOG502S339; Eukaryota.
DR GeneTree; ENSGT00390000004211; -.
DR HOGENOM; CLU_080745_0_0_1; -.
DR InParanoid; Q9DA48; -.
DR OMA; FIIVNWA; -.
DR OrthoDB; 1279146at2759; -.
DR PhylomeDB; Q9DA48; -.
DR TreeFam; TF336918; -.
DR BioGRID-ORCS; 67652; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9DA48; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DA48; protein.
DR Bgee; ENSMUSG00000028264; Expressed in spermatid and 79 other tissues.
DR ExpressionAtlas; Q9DA48; baseline and differential.
DR Genevisible; Q9DA48; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd13783; SPACA1; 1.
DR InterPro; IPR037878; SPACA1.
DR PANTHER; PTHR47223; PTHR47223; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..305
FT /note="Sperm acrosome membrane-associated protein 1"
FT /id="PRO_0000248153"
FT TOPO_DOM 29..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 29..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBV2"
FT MOD_RES 279
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D5K8A9"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D5K8A9"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 305 AA; 33343 MW; 9D68F7322E2DB398 CRC64;
MRARGAGCPA GLLAVGWLIL VGLQASQASN VTSSGGGVQE PAVAREGESE SESESEEEAE
NEGEVPESET TAEADAEEEV QNRTIVKEVE FGMCTVTCGV GIREVILTNG CPGGESKCVV
RVEECRGPVD CGWGKPISEN LDSARLSCVH ISPENRFKYV WKLLKPDQQP VILTNDSAVL
EITREIRPLA FECDTLDNNE MVASVKFTVY TTNELQMRRS SRPDTDAVLV FVLTIGVIIC
IFVIFVLIFI IINWAAVKSF WGSKTSATEI QSELSSMRYK DSTSLDQSPT DIPVHEDDAL
SEWNE
