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P70281 (SYCP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptonemal complex protein 3
Short name=SCP-3
Gene names
Name:Sycp3
Synonyms:Scp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the transverse filaments of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for axial elements (AE) in meiotic cells and for assembly of the synaptonemal complex. May be important for testis development and male fertility. Required for efficient phosphorylation of HORMAD1 and HORMAD2. Ref.4 Ref.5

Subunit structure

Interacts with SYCP2 By similarity.

Subcellular location

Nucleus By similarity. Chromosome. Note: In tripartite segments of synaptonemal complexes, irrespective of whether these are synapsed or unsynapsed By similarity. Ref.5

Post-translational modification

Phosphorylated. Ref.5

Disruption phenotype

Homozygous males with null mutations were sterile due to massive apoptotic cell death during meiotic prophase. Failed to form axial/lateral elements and SCs, and the chromosomes in the mutant spermatocytes did not synapse. In contrast, females were fertile and generated healthy offspring. However, they exhibited a sharp reduction in litter size that increased with advancing maternal age. Ref.4

Sequence similarities

Belongs to the XLR/SYCP3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Synaptonemal complex protein 3
PRO_0000223044

Regions

Coiled coil115 – 252138 Potential
Motif106 – 1094Nuclear localization signal Potential
Compositional bias123 – 250128Gln-rich

Experimental info

Sequence conflict1911F → K Ref.3
Sequence conflict1931M → I Ref.3

Sequences

Sequence LengthMass (Da)Tools
P70281 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E0121D58A8DCD2EA

FASTA25429,347
        10         20         30         40         50         60 
MLRGCGDSDS SPEPLSKHLK MVPGGRKHSG KSGKPPLVDQ PKKAFDFEKD DKDLSGSEED 

        70         80         90        100        110        120 
VADEKAPVID KHGKKRSAGI IEDVGGEVQN MLEKFGADIN KALLAKRKRI EMYTKASFKA 

       130        140        150        160        170        180 
SNQKIEQIWK TQQEEIQKLN NEYSQQFMNV LQQWELDIQK FEEQGEKLSN LFRQQQKIFQ 

       190        200        210        220        230        240 
QSRIVQSQRM FAMKQIHEQF IKSLEDVEKN NDNLFTGTQS ELKKEMAMLQ KKVMMETQQQ 

       250 
EMANVRKSLQ SMLF

« Hide

References

« Hide 'large scale' references
[1]"The mouse synaptosomal complex protein gene Sycp3 maps to band C of chromosome 10."
Klink A., Lee M., Cooke H.J.
Mamm. Genome 8:376-377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Liver and Testis.
[2]"The genomic structure of SYCP3, a meiosis-specific gene encoding a protein of the chromosome core."
Botelho R.J., DiNicolo L., Tsao N., Karaiskakis A., Tarsounas M., Moens P.B., Pearlman R.E.
Biochim. Biophys. Acta 1518:294-299(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic stem cell.
[4]"The murine SCP3 gene is required for synaptonemal complex assembly, chromosome synapsis, and male fertility."
Yuan L., Liu J.G., Zhao J., Brundell E., Daneholt B., Hoog C.
Mol. Cell 5:73-83(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Phosphorylation of chromosome core components may serve as axis marks for the status of chromosomal events during mammalian meiosis."
Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D., Hoeoeg C.
PLoS Genet. 8:E1002485-E1002485(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08485 mRNA. Translation: CAA69719.1.
Y08486 Genomic DNA. Translation: CAA69720.1.
AF181478 expand/collapse EMBL AC list , AF181473, AF181474, AF181475, AF181476, AF181477 Genomic DNA. Translation: AAG17538.1.
AK131949 mRNA. Translation: BAE20894.1.
IPIIPI00137653.
RefSeqNP_035647.2. NM_011517.2.
UniGeneMm.297977.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP70281. 1 interaction.

PTM databases

PhosphoSiteP70281.

Proteomic databases

PaxDbP70281.
PRIDEP70281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID20962.
KEGGmmu:20962.

Organism-specific databases

CTD50511.
MGIMGI:109542. Sycp3.

Phylogenomic databases

eggNOGNOG27405.
HOGENOMHOG000236293.
HOVERGENHBG100390.
InParanoidP70281.
OrthoDBEOG4N8R5W.

Enzyme and pathway databases

ReactomeREACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

CleanExMM_SYCP3.
GenevestigatorP70281.
GermOnlineENSMUSG00000020059. Mus musculus.

Family and domain databases

InterProIPR006888. Cor1/Xlr/Xmr.
[Graphical view]
PANTHERPTHR19368. PTHR19368. 1 hit.
PfamPF04803. Cor1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYCP3. mouse.
NextBio299914.
SOURCESearch...

Entry information

Entry nameSYCP3_MOUSE
AccessionPrimary (citable) accession number: P70281
Secondary accession number(s): Q3V2A4, Q549A7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents