SPAG1_MOUSE
ID SPAG1_MOUSE Reviewed; 901 AA.
AC Q80ZX8; Q8CCK7; Q9QZJ3; Q9QZJ4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sperm-associated antigen 1;
DE AltName: Full=Infertility-related sperm protein Spag-1;
DE AltName: Full=TPR-containing protein involved in spermatogenesis;
DE Short=TPIS;
GN Name=Spag1; Synonyms=Tpis;
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] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Fetal skin, and Testis;
RX PubMed=10527845; DOI=10.1006/bbrc.1999.1477;
RA Takaishi M., Huh N.-H.;
RT "A tetratricopeptide repeat-containing protein gene, tpis, whose expression
RT is induced with differentiation of spermatogenic cells.";
RL Biochem. Biophys. Res. Commun. 264:81-85(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-359; SER-739 AND
RP SER-740, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and 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).
CC -!- FUNCTION: May play a role in the cytoplasmic assembly of the ciliary
CC dynein arms (By similarity). May play a role in fertilization. Binds
CC GTP and has GTPase activity (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q07617}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07617}. Dynein
CC axonemal particle {ECO:0000250|UniProtKB:Q07617}. Note=Colocalizes with
CC tubulin. {ECO:0000250|UniProtKB:Q07617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80ZX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80ZX8-2; Sequence=VSP_012684;
CC Name=3;
CC IsoId=Q80ZX8-3; Sequence=VSP_012685;
CC -!- TISSUE SPECIFICITY: Detected in cerebellum, tongue, esophagus,
CC forestomach, sperm and testis. {ECO:0000269|PubMed:10527845}.
CC -!- DEVELOPMENTAL STAGE: Expression is very low in embryonic epidermis at
CC 13.5 dpc and increases from 14.5 dpc to 16.5 dpc. In young mice
CC expression increases in the testis of 2 to 6 weeks old animals, and
CC then remains stable. {ECO:0000269|PubMed:10527845}.
CC -!- MISCELLANEOUS: Antibodies against SPAG1 interfere with fertilization.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27944.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF181252; AAF06160.1; -; mRNA.
DR EMBL; AF181253; AAF06161.1; -; mRNA.
DR EMBL; AK032601; BAC27944.1; ALT_INIT; mRNA.
DR EMBL; BC046313; AAH46313.1; -; mRNA.
DR CCDS; CCDS37061.1; -. [Q80ZX8-1]
DR PIR; JC7111; JC7111.
DR RefSeq; NP_036161.2; NM_012031.3. [Q80ZX8-1]
DR RefSeq; XP_006520138.1; XM_006520075.2.
DR RefSeq; XP_006520139.1; XM_006520076.3. [Q80ZX8-1]
DR RefSeq; XP_006520141.1; XM_006520078.3. [Q80ZX8-3]
DR RefSeq; XP_006520142.1; XM_006520079.3.
DR RefSeq; XP_017172125.1; XM_017316636.1. [Q80ZX8-1]
DR RefSeq; XP_017172126.1; XM_017316637.1.
DR AlphaFoldDB; Q80ZX8; -.
DR SMR; Q80ZX8; -.
DR BioGRID; 205078; 4.
DR STRING; 10090.ENSMUSP00000047335; -.
DR iPTMnet; Q80ZX8; -.
DR PhosphoSitePlus; Q80ZX8; -.
DR EPD; Q80ZX8; -.
DR MaxQB; Q80ZX8; -.
DR PaxDb; Q80ZX8; -.
DR PeptideAtlas; Q80ZX8; -.
DR PRIDE; Q80ZX8; -.
DR ProteomicsDB; 257298; -. [Q80ZX8-1]
DR ProteomicsDB; 257299; -. [Q80ZX8-2]
DR ProteomicsDB; 257300; -. [Q80ZX8-3]
DR Antibodypedia; 26172; 170 antibodies from 19 providers.
DR DNASU; 26942; -.
DR Ensembl; ENSMUST00000047348; ENSMUSP00000047335; ENSMUSG00000037617. [Q80ZX8-1]
DR Ensembl; ENSMUST00000171205; ENSMUSP00000132233; ENSMUSG00000037617. [Q80ZX8-1]
DR GeneID; 26942; -.
DR KEGG; mmu:26942; -.
DR UCSC; uc007vmn.1; mouse. [Q80ZX8-1]
DR CTD; 6674; -.
DR MGI; MGI:1349387; Spag1.
DR VEuPathDB; HostDB:ENSMUSG00000037617; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000154697; -.
DR HOGENOM; CLU_008405_1_0_1; -.
DR InParanoid; Q80ZX8; -.
DR OMA; QLHRWDG; -.
DR OrthoDB; 1070087at2759; -.
DR PhylomeDB; Q80ZX8; -.
DR TreeFam; TF106251; -.
DR BioGRID-ORCS; 26942; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Spag1; mouse.
DR PRO; PR:Q80ZX8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80ZX8; protein.
DR Bgee; ENSMUSG00000037617; Expressed in animal zygote and 172 other tissues.
DR ExpressionAtlas; Q80ZX8; baseline and differential.
DR Genevisible; Q80ZX8; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR025986; RPAP3-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13877; RPAP3_C; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Fertilization; GTP-binding; Hydrolase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..901
FT /note="Sperm-associated antigen 1"
FT /id="PRO_0000106325"
FT REPEAT 213..246
FT /note="TPR 1"
FT REPEAT 247..279
FT /note="TPR 2"
FT REPEAT 280..313
FT /note="TPR 3"
FT REPEAT 430..464
FT /note="TPR 4"
FT REPEAT 472..505
FT /note="TPR 5"
FT REPEAT 507..539
FT /note="TPR 6"
FT REPEAT 606..639
FT /note="TPR 7"
FT REPEAT 640..673
FT /note="TPR 8"
FT REGION 322..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 756..763
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2X2"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07617"
FT VAR_SEQ 1..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10527845"
FT /id="VSP_012684"
FT VAR_SEQ 1..233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012685"
FT CONFLICT 115
FT /note="C -> R (in Ref. 1; AAF06160)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="E -> A (in Ref. 1; AAF06160)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="H -> Y (in Ref. 1; AAF06160/AAF06161)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="E -> D (in Ref. 1; AAF06160/AAF06161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 901 AA; 100670 MW; C8D14100AD00D69F CRC64;
MTAKAKDCPS LWGFGTTKTF KIPIEHLDFK YIENCSDVKH LEKILYVLRS GEEGYYPELT
EFCEKCLTNL APKSRALRKD KPAETASSFS AEEWEKIDSD LKSWVSEIKR EENTCHFHDP
ENHPGVEDPL PPVRGSTCCP HSGKETYSKS KTAKKRIPRD YAEWDKFDVE KECSKIDEDY
KEKTVINNKA HLSKIETKIE TAGLTEKEKS FLANREKGKG NEAFYSGDYE EAVMYYTRSL
SALPTAIAYN NRAQAEIKLQ RWSSALEDCE KALELDPGNV KALLRRATTY KHQNKLQEAV
DDLRKVLQVE PDNDLAKKTL SEVERDLKNS EPVSELQTKG KRMVIEEVEN SGDEGGKGSA
DEREDGGSDE AAMGNIQKKL MVRRSEGGRR SRRGRTPGPR AEQQGGLRET ATASTGDSHY
PEEPRAADNP SGLKRRGNEL FRGGQFAEAA AQYSVAIAQL EPTGSANADE LSILYSNRAA
CYLKEGNCRD CIQDCNRALE LHPFSVKPLL RRAMAYETLE QYRNAYVDYK TVLQIDCGIQ
LASDSANRIA RILTELDGSK WRERLPPIPA VPTSEPLRVW LPAAETPDQD PCPNNCMPSI
TDEKMFQALK EEGNQLVKDK NYKDAISKYN ECLKINSKAC AIYTNRALCY LKLGQFEEAK
LDCEQALQID GENVKASHRL ALAQKGLENC RESGVDPSQV LLSPDSSEAA RHLDTKNDTA
PPSKGRERRR IQVQEVDGSS DEEPERPAEA SATSAPARDG VEDGGSAEPA EKLDVSKPTN
AYEFGQVLST ISARKDEEAC AHLLAITAPK DLPLLLSNKL EGDTFLLLIQ SLKSHLVAKD
PSLVYEHLLY LSKAERFKTM LTLINKGQKE QMAQLFDGLS DTQSDGLTAE DVQALRRQYE
L
