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SPT33_MOUSE
ID   SPT33_MOUSE             Reviewed;         132 AA.
AC   Q8C624;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Spermatogenesis-associated protein 33;
GN   Name=Spata33;
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 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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, 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   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=23844118; DOI=10.1371/journal.pone.0067882;
RA   Chen H., Yi M., Sheng Y., Cheng H., Zhou R.;
RT   "A novel testis-enriched gene Spata33 is expressed during
RT   spermatogenesis.";
RL   PLoS ONE 8:E67882-E67882(2013).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH ATG16L1 AND VDAC2.
RX   PubMed=33087875; DOI=10.1038/s41418-020-00638-2;
RA   Zhang Y., Xu X., Hu M., Wang X., Cheng H., Zhou R.;
RT   "SPATA33 is an autophagy mediator for cargo selectivity in germline
RT   mitophagy.";
RL   Cell Death Differ. 28:1076-1090(2021).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH PPP3R2; PPP3CC AND VDAC2.
RX   PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA   Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA   Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT   "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT   motility in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC   -!- FUNCTION: Plays an important role in sperm motility and male fertility
CC       (PubMed:34446558). Required for sperm midpiece flexibility and for the
CC       localization of sperm calcineurin to the mitochondria
CC       (PubMed:34446558). Promotes mitophagy as well as acts as an autophagy
CC       mediator in male germline cells (PubMed:33087875). Links damaged
CC       mitochondria to autophagosomes via its binding to the outer
CC       mitochondrial membrane protein VDAC2, as well as to key autophagy
CC       machinery component ATG16L1 (PubMed:33087875).
CC       {ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
CC   -!- SUBUNIT: Interacts (via PQIIIT motif) with PPP3R2 and PPP3CC
CC       (PubMed:34446558). Interacts with VDAC2 (PubMed:34446558,
CC       PubMed:33087875). Interacts with ATG16L1 (via WD repeats)
CC       (PubMed:33087875). Interacts with PPP3R1, PPP3CA and PPP3CB (By
CC       similarity). {ECO:0000250|UniProtKB:Q96N06,
CC       ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23844118}.
CC       Nucleus {ECO:0000269|PubMed:23844118}. Cytoplasm
CC       {ECO:0000269|PubMed:33087875}. Mitochondrion
CC       {ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the testis (at protein
CC       level) (PubMed:23844118, PubMed:34446558, PubMed:33087875). Expressed
CC       in the sperm midpiece (at protein level) (PubMed:34446558,
CC       PubMed:33087875). {ECO:0000269|PubMed:23844118,
CC       ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
CC   -!- DEVELOPMENTAL STAGE: Mainly expressed in the postpartum and adult
CC       testis. Predominantly expressed in the spermatocytes, as well as
CC       spermatogonia and round spermatids (at protein level). Expression
CC       increases during the first wave of the spermatogenesis.
CC       {ECO:0000269|PubMed:23844118}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit reduced sperm motility because of an
CC       inflexible midpiece, leading to impaired male fertility
CC       (PubMed:34446558). Spata33 knockout in Sertoli cells and spermatogenic
CC       cells suppresses mitophagy (PubMed:33087875).
CC       {ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
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DR   EMBL; AK076656; BAC36438.1; -; mRNA.
DR   EMBL; GL456146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS40510.1; -.
DR   RefSeq; NP_796253.2; NM_177279.4.
DR   AlphaFoldDB; Q8C624; -.
DR   STRING; 10090.ENSMUSP00000058002; -.
DR   iPTMnet; Q8C624; -.
DR   PhosphoSitePlus; Q8C624; -.
DR   PaxDb; Q8C624; -.
DR   PRIDE; Q8C624; -.
DR   ProteomicsDB; 263335; -.
DR   DNASU; 320869; -.
DR   Ensembl; ENSMUST00000060133; ENSMUSP00000058002; ENSMUSG00000048478.
DR   GeneID; 320869; -.
DR   KEGG; mmu:320869; -.
DR   UCSC; uc009nul.1; mouse.
DR   CTD; 124045; -.
DR   MGI; MGI:2444920; Spata33.
DR   VEuPathDB; HostDB:ENSMUSG00000048478; -.
DR   eggNOG; ENOG502TF19; Eukaryota.
DR   HOGENOM; CLU_162385_0_0_1; -.
DR   InParanoid; Q8C624; -.
DR   OMA; EWGPYYR; -.
DR   PhylomeDB; Q8C624; -.
DR   TreeFam; TF337053; -.
DR   BioGRID-ORCS; 320869; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Spata33; mouse.
DR   PRO; PR:Q8C624; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8C624; protein.
DR   Bgee; ENSMUSG00000048478; Expressed in seminiferous tubule of testis and 91 other tissues.
DR   ExpressionAtlas; Q8C624; baseline and differential.
DR   Genevisible; Q8C624; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR   GO; GO:0097226; C:sperm mitochondrial sheath; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   InterPro; IPR027930; DUF4609.
DR   PANTHER; PTHR38649; PTHR38649; 1.
DR   Pfam; PF15382; DUF4609; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..132
FT                   /note="Spermatogenesis-associated protein 33"
FT                   /id="PRO_0000282410"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..60
FT                   /note="Interaction with ATG16L1"
FT                   /evidence="ECO:0000269|PubMed:33087875"
FT   REGION          61..132
FT                   /note="Interaction with VDAC2"
FT                   /evidence="ECO:0000269|PubMed:33087875"
FT   REGION          110..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           79..84
FT                   /note="PQIIIT"
FT                   /evidence="ECO:0000305|PubMed:34446558"
FT   COMPBIAS        1..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   132 AA;  15038 MW;  E37394D6D6ED4E2C CRC64;
     MGQSKSKPRE KKEEEKSTTT LVTKSKEKVM EKEAKQSDKE SQPAESLLFA TSKHSRPSSS
     SEDKPETKQR SSKKRSVIPQ IIITRASNET LISYGIPDND EQRTIREHAD WGPYHRHRSP
     STIAAYDVHN TE
 
 
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