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Protein

Synaptonemal complex protein 3

Gene

Sycp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase (PubMed:11311943, PubMed:22761579). Required for centromere pairing during meiosis in male germ cells (PubMed:22761579). Required for normal meiosis during spermatogenesis and male fertility (PubMed:10678170). Plays a lesser role in female fertility (PubMed:10678170, PubMed:12004129). Required for efficient phosphorylation of HORMAD1 and HORMAD2 (PubMed:22346761).5 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: MGI

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chiasma assembly Source: UniProtKB
  • female meiosis chromosome segregation Source: UniProtKB
  • female meiosis chromosome separation Source: UniProtKB
  • female meiosis sister chromatid cohesion Source: UniProtKB
  • lateral element assembly Source: MGI
  • meiotic DNA repair synthesis Source: MGI
  • meiotic nuclear division Source: MGI
  • mitotic nuclear division Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • spermatogenesis Source: UniProtKB
  • spermatogenesis, exchange of chromosomal proteins Source: MGI
  • sperm chromatin condensation Source: MGI
  • synapsis Source: MGI
  • synaptonemal complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Meiosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptonemal complex protein 3
Short name:
SCP-3
Gene namesi
Name:Sycp3
Synonyms:Scp31 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:109542. Sycp3.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: MGI
  • condensed chromosome Source: MGI
  • condensed nuclear chromosome Source: MGI
  • condensed nuclear chromosome, centromeric region Source: MGI
  • lateral element Source: UniProtKB
  • male germ cell nucleus Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • synaptonemal complex Source: MGI
  • transverse filament Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Homozygous males with null mutations have smaller testes and are sterile, due to massive apoptotic cell death of male germ cells during meiotic prophase. Spermatocytes fail to form axial/lateral elements and synaptonemal complexes, and the chromosomes in the mutant spermatocytes do not synapse (PubMed:10678170). In contrast, females are fertile and generate healthy offspring. However, they exhibit a sharp reduction in litter size that increases with advancing maternal age (PubMed:10678170, PubMed:12004129). In contrast to wild-type, a high percentage of the mutant embryos display aneuploidy (PubMed:12004129).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Synaptonemal complex protein 3PRO_0000223044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei218 – 2181PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP70281.
PRIDEiP70281.

PTM databases

PhosphoSiteiP70281.

Expressioni

Tissue specificityi

Detected in oocytes (PubMed:16717126). Detected in spermatocytes and testis (at protein level) (PubMed:10678170, PubMed:16717126, PubMed:22761579).3 Publications

Gene expression databases

CleanExiMM_SYCP3.

Interactioni

Subunit structurei

Component of the lateral elements of synaptonemal complexes (PubMed:16717126). Homotetramer; the tetrameric helix bundles assemble end to end into long homopolimeric fibers that exhibit a transversal striation with a periodicity of about 20 nm (in vitro) (By similarity). Interacts with SYCP2 (PubMed:16717126).By similarity1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi203598. 2 interactions.
IntActiP70281. 3 interactions.
MINTiMINT-8144355.
STRINGi10090.ENSMUSP00000020252.

Structurei

3D structure databases

ProteinModelPortaliP70281.
SMRiP70281. Positions 99-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 766Interaction with DNABy similarity
Regioni87 – 926Important for oligomerization and fiber formationBy similarity
Regioni106 – 1094Interaction with DNABy similarity
Regioni249 – 2546Important for oligomerization and fiber formationBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili84 – 241158Sequence analysisBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 1094Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi123 – 250128Gln-richAdd
BLAST

Domaini

Composed of a long central coiled coil domain. The N-terminal and C-terminal regions interact with DNA.By similarity

Sequence similaritiesi

Belongs to the XLR/SYCP3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IJ2Y. Eukaryota.
ENOG4111MZD. LUCA.
HOGENOMiHOG000236293.
HOVERGENiHBG100390.
InParanoidiP70281.
KOiK19528.
PhylomeDBiP70281.

Family and domain databases

InterProiIPR006888. XLR/SYCP3/FAM9_dom.
[Graphical view]
PfamiPF04803. Cor1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGCGDSDS SPEPLSKHLK MVPGGRKHSG KSGKPPLVDQ PKKAFDFEKD
60 70 80 90 100
DKDLSGSEED VADEKAPVID KHGKKRSAGI IEDVGGEVQN MLEKFGADIN
110 120 130 140 150
KALLAKRKRI EMYTKASFKA SNQKIEQIWK TQQEEIQKLN NEYSQQFMNV
160 170 180 190 200
LQQWELDIQK FEEQGEKLSN LFRQQQKIFQ QSRIVQSQRM FAMKQIHEQF
210 220 230 240 250
IKSLEDVEKN NDNLFTGTQS ELKKEMAMLQ KKVMMETQQQ EMANVRKSLQ

SMLF
Length:254
Mass (Da):29,347
Last modified:February 1, 1997 - v1
Checksum:iE0121D58A8DCD2EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911F → K in BAE20894 (PubMed:16141072).Curated
Sequence conflicti193 – 1931M → I in BAE20894 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08485 mRNA. Translation: CAA69719.1.
Y08486 Genomic DNA. Translation: CAA69720.1.
AF181478
, AF181473, AF181474, AF181475, AF181476, AF181477 Genomic DNA. Translation: AAG17538.1.
AK131949 mRNA. Translation: BAE20894.1.
CCDSiCCDS24111.1.
RefSeqiNP_035647.2. NM_011517.2.
UniGeneiMm.297977.

Genome annotation databases

GeneIDi20962.
KEGGimmu:20962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08485 mRNA. Translation: CAA69719.1.
Y08486 Genomic DNA. Translation: CAA69720.1.
AF181478
, AF181473, AF181474, AF181475, AF181476, AF181477 Genomic DNA. Translation: AAG17538.1.
AK131949 mRNA. Translation: BAE20894.1.
CCDSiCCDS24111.1.
RefSeqiNP_035647.2. NM_011517.2.
UniGeneiMm.297977.

3D structure databases

ProteinModelPortaliP70281.
SMRiP70281. Positions 99-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203598. 2 interactions.
IntActiP70281. 3 interactions.
MINTiMINT-8144355.
STRINGi10090.ENSMUSP00000020252.

PTM databases

PhosphoSiteiP70281.

Proteomic databases

PaxDbiP70281.
PRIDEiP70281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20962.
KEGGimmu:20962.

Organism-specific databases

CTDi50511.
MGIiMGI:109542. Sycp3.

Phylogenomic databases

eggNOGiENOG410IJ2Y. Eukaryota.
ENOG4111MZD. LUCA.
HOGENOMiHOG000236293.
HOVERGENiHBG100390.
InParanoidiP70281.
KOiK19528.
PhylomeDBiP70281.

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSiSycp3. mouse.
NextBioi299914.
PROiP70281.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SYCP3.

Family and domain databases

InterProiIPR006888. XLR/SYCP3/FAM9_dom.
[Graphical view]
PfamiPF04803. Cor1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, TISSUE SPECIFICITY.
  5. "Female germ cell aneuploidy and embryo death in mice lacking the meiosis-specific protein SCP3."
    Yuan L., Liu J.G., Hoja M.R., Wilbertz J., Nordqvist K., Hoeoeg C.
    Science 296:1115-1118(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Mouse SYCP2 is required for synaptonemal complex assembly and chromosomal synapsis during male meiosis."
    Yang F., De La Fuente R., Leu N.A., Baumann C., McLaughlin K.J., Wang P.J.
    J. Cell Biol. 173:497-507(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYCP2, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10; SER-11; SER-55; SER-77 AND THR-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  8. "Synaptonemal complex components persist at centromeres and are required for homologous centromere pairing in mouse spermatocytes."
    Bisig C.G., Guiraldelli M.F., Kouznetsova A., Scherthan H., Hoeoeg C., Dawson D.S., Pezza R.J.
    PLoS Genet. 8:E1002701-E1002701(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "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.

Entry informationi

Entry nameiSYCP3_MOUSE
AccessioniPrimary (citable) accession number: P70281
Secondary accession number(s): Q3V2A4, Q549A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 13, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.