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SYC2L_XENLA
ID   SYC2L_XENLA             Reviewed;         977 AA.
AC   Q90WN7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Synaptonemal complex protein 2-like;
DE            Short=SCP-2-like;
DE   AltName: Full=145 kDa nucleolar protein {ECO:0000303|PubMed:11739789};
GN   Name=sycp2l; Synonyms=no145 {ECO:0000303|PubMed:11739789};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-42; 44-52; 54-60;
RP   112-117; 348-360; 375-380; 440-450; 525-537; 622-626; 763-782; 894-910;
RP   915-926 AND 940-953, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Ovary;
RX   PubMed=11739789; DOI=10.1091/mbc.12.12.3904;
RA   Kneissel S., Franke W.W., Gall J.G., Heid H., Reidenbach S., Schnoelzer M.,
RA   Spring H., Zentgraf H., Schmidt-Zachmann M.S.;
RT   "A novel karyoskeletal protein: characterization of protein NO145, the
RT   major component of nucleolar cortical skeleton in Xenopus oocytes.";
RL   Mol. Biol. Cell 12:3904-3918(2001).
RN   [2]
RP   UBIQUITINATION, PHOSPHORYLATION, PROTEASOMAL DEGRADATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=17374641; DOI=10.1242/jcs.000166;
RA   Voltmer-Irsch S., Kneissel S., Adenot P.G., Schmidt-Zachmann M.S.;
RT   "Regulatory mechanisms governing the oocyte-specific synthesis of the
RT   karyoskeletal protein NO145.";
RL   J. Cell Sci. 120:1412-1422(2007).
CC   -!- FUNCTION: Oocyte-specific protein that localizes to centromeres at the
CC       dictyate stage and regulates the survival of primordial oocytes.
CC       {ECO:0000250|UniProtKB:A0A0M3U1B0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A0M3U1B0}.
CC       Chromosome, centromere {ECO:0000250|UniProtKB:A0A0M3U1B0}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:11739789}. Note=Localized to the
CC       synaptonemal complex lateral elements in late diplotene oocytes, while
CC       it is absent on the synaptonemal complex of leptotene, zygotene,
CC       pachytene and early diplotene oocytes. Localizes to centromeres in
CC       dictyate oocytes (By similarity). Detected in nuclear granules and
CC       sizable aggregates (By similarity). Localized in a cage-like cortical
CC       structure around the entire nucleolus, consisting of a meshwork of
CC       patches and filaments. {ECO:0000250|UniProtKB:A0A0M3U1B0,
CC       ECO:0000250|UniProtKB:Q5T4T6, ECO:0000269|PubMed:11739789}.
CC   -!- TISSUE SPECIFICITY: Expressed in immature oocytes (at protein level).
CC       Expressed in the ovary. {ECO:0000269|PubMed:11739789}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in oocytes throughout oogenesis.
CC       Undetectable in eggs and during early embryonic stages up to the
CC       tailbud stage (at protein level). Expressed during early embryonic
CC       stages beyond stage 8 (mid-blastula transition; MBT).
CC       {ECO:0000269|PubMed:11739789, ECO:0000269|PubMed:17374641}.
CC   -!- PTM: Ubiquitinated and gradually degraded by the proteasome during
CC       oocyte maturation. {ECO:0000269|PubMed:17374641}.
CC   -!- PTM: Phosphorylated in maturing oocytes, before its degradation.
CC       {ECO:0000269|PubMed:17374641}.
CC   -!- SIMILARITY: Belongs to the SYCP2 family. {ECO:0000305}.
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DR   EMBL; AJ249963; CAC80718.2; -; mRNA.
DR   RefSeq; NP_001082126.1; NM_001088657.1.
DR   AlphaFoldDB; Q90WN7; -.
DR   SMR; Q90WN7; -.
DR   GeneID; 398239; -.
DR   KEGG; xla:398239; -.
DR   CTD; 398239; -.
DR   Xenbase; XB-GENE-919983; sycp2l.S.
DR   OrthoDB; 285929at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 398239; Expressed in gastrula and 7 other tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR024835; SYCP2-like.
DR   InterPro; IPR041322; SYCP2_ARLD.
DR   InterPro; IPR040560; SYCP2_SLD.
DR   PANTHER; PTHR15607; PTHR15607; 1.
DR   Pfam; PF18581; SYCP2_ARLD; 1.
DR   Pfam; PF18584; SYCP2_SLD; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..977
FT                   /note="Synaptonemal complex protein 2-like"
FT                   /id="PRO_0000333810"
FT   REGION          447..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..824
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  111354 MW;  82CB1A58656E056F CRC64;
     MSEDGAQTAE KMDTHTQYYL ESLIIDALKG KGFQKIIELF DGKVIFSSQF HNKLLLSQLD
     KLINKELDRN EFKHVSVLMK CIQHFCKNDC QESSTLIHQG LVSKMVLWFE RTVDFLRISK
     EATLLTLVED FYDSALVICK CNCEDGKRQL LDSFLIRLGH LVTEKWVACH LRLEALRTIN
     CILDSISRED KKKLHCSEDL CELTKDLART IQEAGDYDIQ VAISEALCRM MGKKFRDSFV
     HQWFEDNFLA DAFKEIKDKE FETDCRKFLN CLNSRHQSNK GVYTFPCITV FTDLDELKKP
     QDENMENFWI DFNAGSQCVS FYIHNTEGSL WDSVRLLKES VNNYTLKEND GQQMLGIYLK
     DPQVINTNDV TKVKIYFEPK HDIKSAIKRV FEDINEIHSN PVELDSTEGL IDIGNSLASH
     TVITTATTFK QWKRNQANKM DSASDILGSQ TSEHSSTTKT SSANRSVQKS LSNADSHEIV
     IESVPLEAVI TIADEQPNTA QFQDDMDDAI FQGAASDVPA KDSSQEIIII TEASADKEFA
     AKKTQGIFQF QGYSDTLASD QVSDAKKKIL LPKQSTERAT PASRYRASMN SPLQRTSSAY
     RSHLFCESNE VTSNTESERS WIQDFKNKSA VKSADYSCEK TRNKSKRKVL PLASESGDDE
     KQVDTTETVA RFTSRKEMHR PEDINPKSPH SAELKLPGIS ALLTPGDSRS QSKSDYRYQS
     AIDDQDIMDP VEEASSPEMS IDHNKEPKNG HDEVYASGPL NRSVDGNNIY HAADTLQHAT
     GKRKHKTCER EEIPFKPRKL FSSTEKNVNR SAADSEDSED VFYSESHDQD LAEASVLSAF
     DSFTKELKRK FLTRYKRIEN RANHVLKSSH QQVSTVLNEI HQCRLQKINH FNKIVVHELS
     SLEAEVQALK QFEKETLDFW EDQYVKMNTF CSSQTQRIKT MDSALLETIS NLKNVIQKTT
     KEEVSNTEEH IQNKLLK
 
 
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