SPAG8_MOUSE
ID SPAG8_MOUSE Reviewed; 470 AA.
AC Q3V0Q6; B9EKF1; Q5UAV3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sperm-associated antigen 8 {ECO:0000312|MGI:MGI:3056295};
DE AltName: Full=Sperm membrane protein 1 {ECO:0000250|UniProtKB:Q99932};
DE Short=SMP-1 {ECO:0000250|UniProtKB:Q99932};
DE AltName: Full=Sperm membrane protein BS-84 {ECO:0000250|UniProtKB:Q99932};
GN Name=Spag8 {ECO:0000312|MGI:MGI:3056295};
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 {ECO:0000312|EMBL:AAI50869.1};
RN [1] {ECO:0000312|EMBL:AAV31155.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis {ECO:0000312|EMBL:AAV31155.1};
RA Di Q., Wang L.F., Miao S.Y., Zhang X.D., Qiao Y.;
RT "Mouse homolog gene of SPAG8 (Homo sapiens sperm associated antigen 8).";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAE21448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000081696,
RC ECO:0000312|Proteomes:UP000000589};
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] {ECO:0000312|EMBL:EDL02455.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAI50869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI50869.1};
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 [6] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17187156; DOI=10.1111/j.1745-7262.2007.00247.x;
RA Cheng G.Y., Shi J.L., Wang M., Hu Y.Q., Liu C.M., Wang Y.F., Xu C.;
RT "Inhibition of mouse acrosome reaction and sperm-zona pellucida binding by
RT anti-human sperm membrane protein 1 antibody.";
RL Asian J. Androl. 9:23-29(2007).
RN [7]
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 [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FHL5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=20488182; DOI=10.1016/j.febslet.2010.05.016;
RA Wu H., Chen Y., Miao S., Zhang C., Zong S., Koide S.S., Wang L.;
RT "Sperm associated antigen 8 (SPAG8), a novel regulator of activator of CREM
RT in testis during spermatogenesis.";
RL FEBS Lett. 584:2807-2815(2010).
CC -!- FUNCTION: Plays a role in spermatogenesis by enhancing the binding of
CC CREM isoform tau to its coactivator FHL5 and increasing the FHL5-
CC regulated transcriptional activation of CREM isoform tau
CC (PubMed:20488182). Involved in the acrosome reaction and in binding of
CC sperm to the zona pellucida (PubMed:17187156). Plays a role in
CC regulation of the cell cycle by controlling progression through the
CC G2/M phase, possibly by delaying the activation of CDK1 which is
CC required for entry into mitosis (By similarity). May play a role in
CC fertility and microtubule formation through interaction with RANBP9 (By
CC similarity). {ECO:0000250|UniProtKB:Q99932,
CC ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:20488182}.
CC -!- SUBUNIT: Interacts with FHL5 (via second LIM domain) (PubMed:20488182).
CC Interacts with RANBP9 (By similarity). {ECO:0000250|UniProtKB:Q99932,
CC ECO:0000269|PubMed:20488182}.
CC -!- INTERACTION:
CC Q3V0Q6; Q9WTX7: Fhl5; NbExp=5; IntAct=EBI-7981981, EBI-7530396;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20488182}. Nucleus
CC {ECO:0000269|PubMed:20488182}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:20488182}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:E1BNS6}. Note=In mature sperm cells, detected in
CC the acrosomal region of the head and in the middle piece of the tail
CC (PubMed:20488182). Localized to the nucleus and cytoplasm of
CC spermatocytes and round spermatids while, in elongating spermatids,
CC expressed in the cytoplasm but not in the nucleus (PubMed:20488182).
CC During the cell cycle, localized on the microtubule-organizing center
CC (MTOC) during prophase. In metaphase, extends along spindle
CC microtubules. In anaphase, detected on the astral microtubules and mid-
CC zone. In telophase, remains at the mid-zone. After cytokinesis, returns
CC to the MTOC (By similarity). Microtubule inner protein (MIP) part of
CC the dynein-decorated doublet microtubules (DMTs) in cilia axoneme (By
CC similarity). {ECO:0000250|UniProtKB:E1BNS6,
CC ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:20488182}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3V0Q6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V0Q6-2; Sequence=VSP_058322, VSP_058323;
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level). Not
CC detected in brain, heart, kidney, spleen, liver, lung, thymus and colon
CC (at protein level). {ECO:0000269|PubMed:20488182}.
CC -!- DEVELOPMENTAL STAGE: In the testis, expressed at low levels at 3 weeks
CC with levels markedly elevated by 4 weeks and into adulthood (at protein
CC level). {ECO:0000269|PubMed:20488182}.
CC -!- SIMILARITY: Belongs to the SPAG8 family. {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; AY769082; AAV31155.1; -; mRNA.
DR EMBL; AK132968; BAE21448.1; -; mRNA.
DR EMBL; AL732626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02455.1; -; Genomic_DNA.
DR EMBL; BC150868; AAI50869.1; -; mRNA.
DR CCDS; CCDS38743.1; -. [Q3V0Q6-2]
DR CCDS; CCDS71376.1; -. [Q3V0Q6-1]
DR RefSeq; NP_001007464.1; NM_001007463.2. [Q3V0Q6-2]
DR RefSeq; NP_001277391.1; NM_001290462.2. [Q3V0Q6-1]
DR AlphaFoldDB; Q3V0Q6; -.
DR SMR; Q3V0Q6; -.
DR IntAct; Q3V0Q6; 1.
DR MINT; Q3V0Q6; -.
DR STRING; 10090.ENSMUSP00000103502; -.
DR PhosphoSitePlus; Q3V0Q6; -.
DR PaxDb; Q3V0Q6; -.
DR PRIDE; Q3V0Q6; -.
DR ProteomicsDB; 261561; -. [Q3V0Q6-1]
DR ProteomicsDB; 261562; -. [Q3V0Q6-2]
DR Antibodypedia; 26087; 224 antibodies from 26 providers.
DR Ensembl; ENSMUST00000084646; ENSMUSP00000081696; ENSMUSG00000066196. [Q3V0Q6-1]
DR Ensembl; ENSMUST00000107870; ENSMUSP00000103502; ENSMUSG00000066196. [Q3V0Q6-2]
DR GeneID; 433700; -.
DR KEGG; mmu:433700; -.
DR UCSC; uc008sqq.1; mouse. [Q3V0Q6-1]
DR UCSC; uc008sqr.1; mouse.
DR CTD; 26206; -.
DR MGI; MGI:3056295; Spag8.
DR VEuPathDB; HostDB:ENSMUSG00000066196; -.
DR eggNOG; ENOG502S06E; Eukaryota.
DR GeneTree; ENSGT00640000091617; -.
DR InParanoid; Q3V0Q6; -.
DR OMA; HCLLYNW; -.
DR OrthoDB; 1153567at2759; -.
DR PhylomeDB; Q3V0Q6; -.
DR TreeFam; TF329075; -.
DR BioGRID-ORCS; 433700; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Spag8; mouse.
DR PRO; PR:Q3V0Q6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3V0Q6; protein.
DR Bgee; ENSMUSG00000066196; Expressed in spermatid and 67 other tissues.
DR ExpressionAtlas; Q3V0Q6; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR026124; Sperm-assoc_Ag8.
DR PANTHER; PTHR15510; PTHR15510; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Differentiation; Fertilization; Nucleus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..470
FT /note="Sperm-associated antigen 8"
FT /id="PRO_0000436205"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 407..411
FT /note="GVSDI -> VCVGD (in isoform 2)"
FT /id="VSP_058322"
FT VAR_SEQ 412..470
FT /note="Missing (in isoform 2)"
FT /id="VSP_058323"
FT CONFLICT 113
FT /note="H -> R (in Ref. 5; AAI50869)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> Q (in Ref. 5; AAI50869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 50541 MW; A68A6ACC5302CAA2 CRC64;
METTESTEGS LSRSCDVQPS SERLDTPSEP VPSSSSSPRS TAPAEAPAQY SVLTEPSSDS
LYGAPCPPAH HRGHGFGFQP FYVSCIPQDP CNMADLSSRA DPTSSYPCHS SVHGSGSGTC
GLGQSSEPSQ GSGPTSGPAP ASVPSLVSGP DSASGPDSSA SGPALASGPG PADPGQGPKF
STCIPQGYRC IPVDLAPDYN AWCQHLHWKP QRSWEPLQVS EPGVRGPYKP PEPGALGPCE
PCEPCEPPEA ESEETLCKAR PRGQCLLYNW EEERATNQLD QIPPLQDGSE SYFFRHGHQG
LLTTQPQSPM SSSTTQRDSY QLPRHICQPL RGKREAMLEM LLRHQICKEV QAEQEPARKL
FETESVTHHD YRVELVRAAP PASTKPHDYR QEQPETFWIQ RAARLPGVSD IRTLDTPFRK
NCSFSTPVPL SLGQPLPYEL ESGPHQVGVI SSLACQGGGQ GCGRTKTTPI
