SPESP_MOUSE
ID SPESP_MOUSE Reviewed; 399 AA.
AC Q9D5A0; Q9D5X8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sperm equatorial segment protein 1 {ECO:0000250|UniProtKB:Q6UW49};
DE Flags: Precursor;
GN Name=Spesp1 {ECO:0000312|MGI:MGI:1913962};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=20375058; DOI=10.1242/jcs.067363;
RA Fujihara Y., Murakami M., Inoue N., Satouh Y., Kaseda K., Ikawa M.,
RA Okabe M.;
RT "Sperm equatorial segment protein 1, SPESP1, is required for fully fertile
RT sperm in mouse.";
RL J. Cell Sci. 123:1531-1536(2010).
RN [5]
RP GLYCOSYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25761597; DOI=10.1095/biolreprod.114.121095;
RA Suryavathi V., Panneerdoss S., Wolkowicz M.J., Shetty J., Sherman N.E.,
RA Flickinger C.J., Herr J.C.;
RT "Dynamic Changes in Equatorial Segment Protein 1 (SPESP1) Glycosylation
RT During Mouse Spermiogenesis.";
RL Biol. Reprod. 92:129-129(2015).
CC -!- FUNCTION: Involved in fertilization ability of sperm.
CC {ECO:0000269|PubMed:20375058, ECO:0000269|PubMed:25761597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:20375058}. Note=Small proacrosomal granules (during
CC the Golgi phase), enlarged acrosomal vesicles (during the cap phase),
CC acrosome (during the elongating phase), equatorial segment of the
CC acrosome (during the maturation phase) (By similarity). After acrosome
CC reaction localizes to the equatorial segment region in both
CC noncapacitated and capacitated, acrosome-reacted sperm
CC (PubMed:25761597). {ECO:0000250|UniProtKB:Q6UW49,
CC ECO:0000269|PubMed:25761597}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:20375058}.
CC -!- PTM: Glycosylated. In testis there are two predominant forms of 77- and
CC 67-kDa and a form of 47-kDa, whereas in epididymal sperm from caput,
CC corpus, and cauda there are two forms of 47- and 43-kDa. Testis forms
CC contain complex carbohydrate residues. Epididymal sperm forms are N-
CC glycosylated. Then undergoes significant glycosylation in the testis
CC and that the majority of these glycoconjugates are removed by the time
CC sperm reach the caput epididymis. {ECO:0000269|PubMed:25761597}.
CC -!- DISRUPTION PHENOTYPE: Knockout female mice are fertile, while the
CC average number of pups that are fathered by knockout males is
CC significantly lower than that of wild-type fathers.
CC {ECO:0000269|PubMed:20375058}.
CC -!- SIMILARITY: Belongs to the SPESP1 family. {ECO:0000305}.
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DR EMBL; AK014843; BAB29577.1; -; mRNA.
DR EMBL; AK015620; BAB29908.1; -; mRNA.
DR EMBL; BC050754; AAH50754.1; -; mRNA.
DR CCDS; CCDS23263.1; -.
DR RefSeq; NP_079997.1; NM_025721.2.
DR AlphaFoldDB; Q9D5A0; -.
DR SMR; Q9D5A0; -.
DR IntAct; Q9D5A0; 1.
DR STRING; 10090.ENSMUSP00000058522; -.
DR GlyGen; Q9D5A0; 1 site.
DR PhosphoSitePlus; Q9D5A0; -.
DR PaxDb; Q9D5A0; -.
DR PeptideAtlas; Q9D5A0; -.
DR PRIDE; Q9D5A0; -.
DR ProteomicsDB; 258719; -.
DR Antibodypedia; 51298; 81 antibodies from 16 providers.
DR DNASU; 66712; -.
DR Ensembl; ENSMUST00000056949; ENSMUSP00000058522; ENSMUSG00000046846.
DR GeneID; 66712; -.
DR KEGG; mmu:66712; -.
DR UCSC; uc009qag.1; mouse.
DR CTD; 246777; -.
DR MGI; MGI:1913962; Spesp1.
DR VEuPathDB; HostDB:ENSMUSG00000046846; -.
DR eggNOG; ENOG502SG7W; Eukaryota.
DR GeneTree; ENSGT00390000005362; -.
DR HOGENOM; CLU_787463_0_0_1; -.
DR InParanoid; Q9D5A0; -.
DR OMA; YKSQLLP; -.
DR OrthoDB; 1348911at2759; -.
DR PhylomeDB; Q9D5A0; -.
DR TreeFam; TF337441; -.
DR BioGRID-ORCS; 66712; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D5A0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D5A0; protein.
DR Bgee; ENSMUSG00000046846; Expressed in spermatid and 10 other tissues.
DR Genevisible; Q9D5A0; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IDA:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:MGI.
DR GO; GO:0035036; P:sperm-egg recognition; IDA:UniProtKB.
DR InterPro; IPR026743; Equatorial_segment.
DR PANTHER; PTHR31667; PTHR31667; 1.
DR Pfam; PF15754; SPESP1; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Developmental protein; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..399
FT /note="Sperm equatorial segment protein 1"
FT /id="PRO_0000042709"
FT REGION 136..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 170..171
FT /note="ES -> DP (in Ref. 1; BAB29908)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> Q (in Ref. 1; BAB29908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44702 MW; 41481486A6A588BD CRC64;
MKLVVLVALW LWPSSLLAYP TITVLPDEEQ NLNHYVHILQ NLIMSVPTKE QDLGKKLSSS
RTVDSAEPRS LASKVLLTPG LVSAQDVTPE SDVLIRPVDE TTNSRTRGFT LRRRRTQSTA
FWSIRPNNIS VVLRTEEPFI EKEPEPELES SRLPTEPEPE LEPEPEPVAE SRQMSEPEEE
LVTSTTPNKE LTGTSRISSM ATQPANTQAT RITVTVKTTS TMDVSTDSED VPQLSGQSEI
PSAEDLPGRH SLNTRHEDIL KKISNINAEI QQGLLGGNNS PEFKEFIKAS REHLKRSLAL
AAAAEHKLEQ MYGSNVFPEG RTSDPDNDME MIINMLYNSR SKLSDYFNIK RVPSELREKA
SVVNAELRKI LCVDQVEMQS LIKKLLSNNM KILNILNVP
