位置:首页 > 蛋白库 > SAS4_CAEEL
SAS4_CAEEL
ID   SAS4_CAEEL              Reviewed;         808 AA.
AC   P34402;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Spindle assembly abnormal protein 4;
GN   Name=sas-4; ORFNames=F10E9.8;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12636923; DOI=10.1016/s1534-5807(03)00062-5;
RA   Leidel S., Goenczy P.;
RT   "SAS-4 is essential for centrosome duplication in C. elegans and is
RT   recruited to daughter centrioles once per cell cycle.";
RL   Dev. Cell 4:431-439(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12600319; DOI=10.1016/s0092-8674(03)00117-x;
RA   Kirkham M., Mueller-Reichert T., Oegema K., Grill S., Hyman A.A.;
RT   "SAS-4 is a C. elegans centriolar protein that controls centrosome size.";
RL   Cell 112:575-587(2003).
RN   [5]
RP   INTERACTION WITH HYLS-1.
RX   PubMed=19656802; DOI=10.1101/gad.1810409;
RA   Dammermann A., Pemble H., Mitchell B.J., McLeod I., Yates J.R. III,
RA   Kintner C., Desai A.B., Oegema K.;
RT   "The hydrolethalus syndrome protein HYLS-1 links core centriole structure
RT   to cilia formation.";
RL   Genes Dev. 23:2046-2059(2009).
CC   -!- FUNCTION: Required for centrosome duplication. Plays a central role in
CC       determining centrosome size. {ECO:0000269|PubMed:12600319,
CC       ECO:0000269|PubMed:12636923}.
CC   -!- SUBUNIT: Interacts with hyls-1; leading to hyls-1 localization into
CC       newly forming centrioles. {ECO:0000269|PubMed:19656802}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:12600319,
CC       ECO:0000269|PubMed:12636923}. Note=Localizes to the centrosome
CC       throughout the cell cycle. Localizes to a tiny dot in the center of
CC       centrosome. Recruited to the centrosome once per cell cycle, at the
CC       time of organelle duplication and remains stably associated after.
CC   -!- DEVELOPMENTAL STAGE: Localizes to centrosomes both in sperm and in the
CC       syncytial part of the gonad. Staining in the gonad disappears as the
CC       meiotic nuclei cellularizes to form oocytes, presumably marking the
CC       point at which the centrioles are lost during oogenesis. In newly
CC       fertilized embryos, it is localized to a discrete spot near the sperm-
CC       derived pronucleus. Then, it remains attached to the centrosome
CC       throughout the rest of development. {ECO:0000269|PubMed:12600319,
CC       ECO:0000269|PubMed:12636923}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ539470; CAD62434.1; -; mRNA.
DR   EMBL; FO081105; CCD69136.1; -; Genomic_DNA.
DR   RefSeq; NP_498828.2; NM_066427.5.
DR   AlphaFoldDB; P34402; -.
DR   SMR; P34402; -.
DR   BioGRID; 41376; 21.
DR   IntAct; P34402; 12.
DR   STRING; 6239.F10E9.8; -.
DR   EPD; P34402; -.
DR   PaxDb; P34402; -.
DR   PRIDE; P34402; -.
DR   EnsemblMetazoa; F10E9.8.1; F10E9.8.1; WBGene00004726.
DR   GeneID; 176172; -.
DR   KEGG; cel:CELE_F10E9.8; -.
DR   UCSC; F10E9.8; c. elegans.
DR   CTD; 40859; -.
DR   WormBase; F10E9.8; CE29756; WBGene00004726; sas-4.
DR   eggNOG; ENOG502SYI4; Eukaryota.
DR   HOGENOM; CLU_018365_0_0_1; -.
DR   InParanoid; P34402; -.
DR   OMA; EFRLRWY; -.
DR   OrthoDB; 1111973at2759; -.
DR   PRO; PR:P34402; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00004726; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0007099; P:centriole replication; IMP:WormBase.
DR   GO; GO:0045185; P:maintenance of protein location; IMP:WormBase.
PE   1: Evidence at protein level;
KW   Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Reference proteome.
FT   CHAIN           1..808
FT                   /note="Spindle assembly abnormal protein 4"
FT                   /id="PRO_0000097592"
FT   REGION          1..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          161..181
FT                   /evidence="ECO:0000255"
FT   COILED          314..503
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        30..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  92206 MW;  722C4509D3ACA97B CRC64;
     MASDENIGAD GEQKPSRPFL RKGQGTARFR MPRNNKTSAG APPTSELSSA SSPSINVPRF
     SLSNALPNSA RTVDSGISNE DETRPPTTAS LPMDQPSLSS SPENRLNPAP SVAEEHGHSG
     QHAEEEEDND TDEVSAMPSF VPDEPSTLVN SDHELSDDAL KYKNAAAEFK AFERRMDSMR
     SASTITTSLA TPSSCAPSNS SEPPTRSTPI MNDLGVGPNN HNWPSSMQEL SGISLETPQA
     RPLGSNRINQ LVRSEAQTGI SLLQHHERPT VTAPLRRNDM MNSSRQNPQN GNVQDENRPE
     HVYDQPIHVP GSSLDRQKLE IEIRRHRNLN IQLRDTIAHL DYAEESVHTT KRQLEEKISE
     VNNFKKELIE EFKKCKKGVE EEFEKKFEKI KEDYDELYEK LKRDQRDLER DQKILKKGTG
     ERNKEFTETI ATLRDKLRAS ETKNAQYRQD IRVRDEKLKK KDEEIEKLQK DGNRLKSTLQ
     TLEKRVKQLR TEKERDDKEK EMFAKVAMNR KTSNPVPPVL NQSVPISITS NGPSRHPSSS
     SLTTFRKPST SNRERGVSWA DEPNEQSLEA VPQEFLMMPV KEMPGKFGKC TIYRDSLGET
     SKVTDTIANG LLFEYSNGDL RWVNRQNAVN IYISAVDKTV RIDLPTYNIS IIHTFQRQVE
     VLRPGNNITL ISIKRREVRT DLIYQNGMYK TEIFNRDGRY VTKDFSNQEV SRKYNPGTHT
     YRDNQCRYVL VTDYNDFELV EPEFRLRWYQ GDPTGLNNQY ILKIIGRPEC SEKTLRLEVN
     LSTCEGTLET AEMIGDKRRK TTLFQWKK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024