SPAT6_MOUSE
ID SPAT6_MOUSE Reviewed; 488 AA.
AC Q3U6K5; A2AED7; Q3V104; Q8BW97; Q99MU6; Q9D9J1; Q9DAI3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Spermatogenesis-associated protein 6 {ECO:0000305};
DE AltName: Full=Kinesin-related protein;
DE Flags: Precursor;
GN Name=Spata6 {ECO:0000312|MGI:MGI:1915196}; Synonyms=Hash;
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 [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
RX PubMed=12771232; DOI=10.1093/molehr/gag047;
RA Oh C., Aho H., Shamsadin R., Nayernia K., Mueller C., Sancken U.,
RA Szpirer C., Engel W., Adham I.M.;
RT "Characterization, expression pattern and chromosomal localization of the
RT spermatogenesis associated 6 gene (Spata6).";
RL Mol. Hum. Reprod. 9:321-330(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Lung, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND INTERACTION WITH MYL6.
RX PubMed=25605924; DOI=10.1073/pnas.1424648112;
RA Yuan S., Stratton C.J., Bao J., Zheng H., Bhetwal B.P., Yanagimachi R.,
RA Yan W.;
RT "Spata6 is required for normal assembly of the sperm connecting piece and
RT tight head-tail conjunction.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E430-E439(2015).
CC -!- FUNCTION: Required for formation of the sperm connecting piece during
CC spermiogenesis. Sperm connecting piece is essential for linking the
CC developing flagellum to the head during late spermiogenesis
CC (PubMed:12771232, PubMed:25605924). May be involved in myosin-based
CC microfilament transport through interaction with myosin subunits
CC (PubMed:25605924). {ECO:0000269|PubMed:12771232,
CC ECO:0000269|PubMed:25605924}.
CC -!- SUBUNIT: Interacts with MYL6. {ECO:0000269|PubMed:25605924}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cell projection, cilium,
CC flagellum {ECO:0000269|PubMed:25605924}. Note=Specifically localizes to
CC the segmented columns and the capitulum of the sperm connecting piece.
CC {ECO:0000269|PubMed:25605924}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U6K5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U6K5-2; Sequence=VSP_023278;
CC Name=3;
CC IsoId=Q3U6K5-3; Sequence=VSP_023279, VSP_023280;
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing spermatids and
CC mature spermatozoa (at protein level) (PubMed:25605924). Isoform 1 is
CC weakly expressed in testis, ovary, thymus and placenta. Isoform 2 and
CC isoform 3 are testis-specific. Expression isw higher in spermatids than
CC in spermatocytes and spermatogonia (PubMed:12771232).
CC {ECO:0000269|PubMed:12771232, ECO:0000269|PubMed:25605924}.
CC -!- DEVELOPMENTAL STAGE: Weak expression of isoform 1 is seen throughout
CC testicular development. Isoform 2 and isoform 3 could not be detected
CC until postnatal day 15. Expressed from postnatal day 20, and thereafter
CC increased. Expressed in blastocysts and in embryos from 8.5 dpc-12.5
CC dpc. After 13.5 dpc, the level of expression decreases. Expressed at
CC 9.5-10.5 dpc in the neural tube, in somites and limb buds.
CC {ECO:0000269|PubMed:12771232}.
CC -!- DISRUPTION PHENOTYPE: Male are sterile due to disruption of sperm
CC connecting piece formation, leading to acephalic spermatozoa in the
CC epididymis and ejaculates. {ECO:0000269|PubMed:25605924}.
CC -!- SIMILARITY: Belongs to the SPATA6 family. {ECO:0000305}.
CC -!- CAUTION: Knockout experiments to inactivate Spata6 were first attempted
CC but were unsuccessful, because chimeras did not transmit the targeted
CC allele to their progeny, generating high-percentage of lethality for
CC chimeric embryos (PubMed:12771232). This suggests that genes other than
CC Spata6 may have been targeted or affected in this study
CC (PubMed:25605924). {ECO:0000269|PubMed:12771232,
CC ECO:0000305|PubMed:25605924}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK20995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF291465; AAK20995.1; ALT_INIT; mRNA.
DR EMBL; AK053170; BAC35292.1; -; mRNA.
DR EMBL; AK005819; BAB24255.1; -; mRNA.
DR EMBL; AK006861; BAB24768.1; -; mRNA.
DR EMBL; AK132771; BAE21349.1; -; mRNA.
DR EMBL; AK153098; BAE31719.1; -; mRNA.
DR EMBL; AL627076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38836.1; -. [Q3U6K5-1]
DR RefSeq; NP_080746.3; NM_026470.3. [Q3U6K5-1]
DR RefSeq; XP_006503412.1; XM_006503349.3.
DR AlphaFoldDB; Q3U6K5; -.
DR BioGRID; 212558; 1.
DR STRING; 10090.ENSMUSP00000036964; -.
DR iPTMnet; Q3U6K5; -.
DR PhosphoSitePlus; Q3U6K5; -.
DR jPOST; Q3U6K5; -.
DR MaxQB; Q3U6K5; -.
DR PaxDb; Q3U6K5; -.
DR PRIDE; Q3U6K5; -.
DR ProteomicsDB; 257337; -. [Q3U6K5-1]
DR ProteomicsDB; 257338; -. [Q3U6K5-2]
DR ProteomicsDB; 257339; -. [Q3U6K5-3]
DR Antibodypedia; 32902; 93 antibodies from 24 providers.
DR DNASU; 67946; -.
DR Ensembl; ENSMUST00000038868; ENSMUSP00000036964; ENSMUSG00000034401. [Q3U6K5-1]
DR Ensembl; ENSMUST00000153746; ENSMUSP00000114610; ENSMUSG00000034401. [Q3U6K5-3]
DR GeneID; 67946; -.
DR KEGG; mmu:67946; -.
DR UCSC; uc008udg.1; mouse. [Q3U6K5-1]
DR CTD; 54558; -.
DR MGI; MGI:1915196; Spata6.
DR VEuPathDB; HostDB:ENSMUSG00000034401; -.
DR eggNOG; ENOG502QRV3; Eukaryota.
DR GeneTree; ENSGT00530000063821; -.
DR HOGENOM; CLU_096689_1_0_1; -.
DR InParanoid; Q3U6K5; -.
DR OMA; CVNAKNY; -.
DR OrthoDB; 1154886at2759; -.
DR PhylomeDB; Q3U6K5; -.
DR TreeFam; TF328520; -.
DR BioGRID-ORCS; 67946; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Spata6; mouse.
DR PRO; PR:Q3U6K5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3U6K5; protein.
DR Bgee; ENSMUSG00000034401; Expressed in seminiferous tubule of testis and 183 other tissues.
DR ExpressionAtlas; Q3U6K5; baseline and differential.
DR Genevisible; Q3U6K5; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0097224; C:sperm connecting piece; IDA:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR027207; Spata6.
DR InterPro; IPR042769; SPATA6_fam.
DR InterPro; IPR032732; SPATA6_N.
DR PANTHER; PTHR16435; PTHR16435; 1.
DR PANTHER; PTHR16435:SF3; PTHR16435:SF3; 1.
DR Pfam; PF14909; SPATA6; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Developmental protein;
KW Differentiation; Flagellum; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Spermatogenesis; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..488
FT /note="Spermatogenesis-associated protein 6"
FT /id="PRO_0000278442"
FT REGION 176..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH7"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH7"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MU5"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH7"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023278"
FT VAR_SEQ 163..176
FT /note="DKFTYHSAPVEKSH -> EASKNLCGSRMTHL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023279"
FT VAR_SEQ 177..488
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023280"
FT CONFLICT 154
FT /note="I -> V (in Ref. 2; BAE31719)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="H -> R (in Ref. 2; BAE31719)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="C -> S (in Ref. 2; BAE21349)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="H -> Q (in Ref. 2; BAE21349)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="Y -> C (in Ref. 2; BAB24768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56101 MW; 423356D3A9471CE8 CRC64;
MPKVKALQCA LALEIRSVTC PGVVLKDKED IYLSICVFGQ YKKTQCVPAT FPLVFNARMV
FEKVFPEAVD PGDVVAQLEY DTAVFELIQL VPPVGETLST YDENTRDFMF PGPNQMSGHH
DSNRQVTMRR ISGLRGIAPK LEFSTTSVIT ECLISSRKCR TQDKFTYHSA PVEKSHGRLQ
CRTSRSQKKK SKSPERSKYC INTKNYEQPT ISSKSHSPSP YTKRRMCELS EDTRRRLAHL
NLGPYEFKKE TDKPPFVIRH VDPPSPRTDN FFGSPGRDCE RDGWVRMHSD HPHIGCCRSK
DYKVIRSPHG RDFEDPFERC EEYLSPRTCS KPQHSARTLL VHSAPSTTPK HCASPVLNRA
SLRERFHSDW CSPPNCDEIH DRVKDVLKSH QAHARHLCDE RDPEREDELE LKRSLLYRDS
AYDSDPEYSS FQRPRGSFHL DDGECWSNRA ASCKGKSHRP VFENSMDKMY RNLYKKACSS
VSHTQESF
