SPD2_CAEEL
ID SPD2_CAEEL Reviewed; 824 AA.
AC P91870;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Spindle-defective protein 2;
GN Name=spd-2 {ECO:0000312|WormBase:F32H2.3};
GN ORFNames=F32H2.3 {ECO:0000312|WormBase:F32H2.3};
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 MUTAGENESIS
RP OF GLY-573; GLY-615 AND ARG-710.
RX PubMed=15068791; DOI=10.1016/s1534-5807(04)00066-8;
RA Kemp C.A., Kopish K.R., Zipperlen P., Ahringer J., O'Connell K.F.;
RT "Centrosome maturation and duplication in C. elegans require the coiled-
RT coil protein SPD-2.";
RL Dev. Cell 6:511-523(2004).
RN [2]
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15186742; DOI=10.1016/j.cub.2004.04.012;
RA Pelletier L., Oezlu N., Hannak E., Cowan C., Habermann B., Ruer M.,
RA Mueller-Reichert T., Hyman A.A.;
RT "The Caenorhabditis elegans centrosomal protein SPD-2 is required for both
RT pericentriolar material recruitment and centriole duplication.";
RL Curr. Biol. 14:863-873(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17115027; DOI=10.1038/ncb1511;
RA Cowan C.R., Hyman A.A.;
RT "Cyclin E-Cdk2 temporally regulates centrosome assembly and establishment
RT of polarity in Caenorhabditis elegans embryos.";
RL Nat. Cell Biol. 8:1441-1447(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-615.
RX PubMed=19081077; DOI=10.1016/j.devcel.2008.09.018;
RA Song M.H., Aravind L., Mueller-Reichert T., O'Connell K.F.;
RT "The conserved protein SZY-20 opposes the Plk4-related kinase ZYG-1 to
RT limit centrosome size.";
RL Dev. Cell 15:901-912(2008).
CC -!- FUNCTION: Required both for centrosome duplication and maturation
CC (PubMed:15068791, PubMed:15186742, PubMed:19081077). Required for
CC pericentriolar material (PCM) recruitment (PubMed:15068791,
CC PubMed:15186742). {ECO:0000269|PubMed:15068791,
CC ECO:0000269|PubMed:15186742, ECO:0000269|PubMed:19081077}.
CC -!- INTERACTION:
CC P91870; P91349: spd-5; NbExp=3; IntAct=EBI-320962, EBI-322479;
CC P91870; Q9GT24: zyg-1; NbExp=6; IntAct=EBI-320962, EBI-323555;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:15068791,
CC ECO:0000269|PubMed:15186742}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:15186742,
CC ECO:0000269|PubMed:19081077}. Note=Localizes to the centriole
CC throughout the cell cycle and accumulates on the PCM during mitosis
CC (PubMed:15068791, PubMed:15186742). Requires spd-5 for its accumulation
CC on the PCM (PubMed:15068791, PubMed:15186742). Recruitment to the
CC centrosome during prophase of the 1-cell embryo is regulated by the
CC cye-1/cdk-2 complex (PubMed:17115027). {ECO:0000269|PubMed:15068791,
CC ECO:0000269|PubMed:15186742, ECO:0000269|PubMed:17115027}.
CC -!- DEVELOPMENTAL STAGE: Associates with centrosomes, during nearly all of
CC the developmental stages. In the hermaphrodite gonad, it localizes as
CC discrete perinuclear foci in the mitotic portion of the germline. These
CC foci are also evident during the early stages of oogenesis but are
CC absent in mature oocytes. In contrast, in mature sperm these foci are
CC present with each male gamete containing a single dot adjacent to the
CC nucleus. Similarly, in meiotic stage embryos, a single expression dot
CC is observed next to the male pronucleus. In slightly older embryos, one
CC or two perinuclear foci are observed. The intensity of the foci
CC increase with the age of the embryos and at mitosis it localizes to
CC both spindle poles. As embryos progress through anaphase and telophase,
CC the intensity of staining gradually diminishes. Careful examination of
CC the staining pattern at this stage reveals a diffuse expression
CC centered on one or two very bright dots corresponding to both
CC centrioles as well the pericentriolar region.
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DR EMBL; AY340594; AAQ17186.1; -; mRNA.
DR EMBL; Z81523; CAB04243.1; -; Genomic_DNA.
DR PIR; T21675; T21675.
DR RefSeq; NP_492414.1; NM_060013.4.
DR AlphaFoldDB; P91870; -.
DR BioGRID; 38145; 16.
DR DIP; DIP-25500N; -.
DR IntAct; P91870; 7.
DR STRING; 6239.F32H2.3.1; -.
DR iPTMnet; P91870; -.
DR EPD; P91870; -.
DR PaxDb; P91870; -.
DR PeptideAtlas; P91870; -.
DR EnsemblMetazoa; F32H2.3.1; F32H2.3.1; WBGene00004953.
DR GeneID; 172712; -.
DR KEGG; cel:CELE_F32H2.3; -.
DR UCSC; F32H2.3.1; c. elegans.
DR CTD; 39850; -.
DR WormBase; F32H2.3; CE09878; WBGene00004953; spd-2.
DR eggNOG; ENOG502RT76; Eukaryota.
DR HOGENOM; CLU_341384_0_0_1; -.
DR InParanoid; P91870; -.
DR OMA; CHYEKQP; -.
DR OrthoDB; 1078008at2759; -.
DR SignaLink; P91870; -.
DR PRO; PR:P91870; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004953; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0007099; P:centriole replication; IMP:WormBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:WormBase.
DR GO; GO:0090222; P:centrosome-templated microtubule nucleation; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:WormBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:InterPro.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR039103; Spd-2/CEP192.
DR PANTHER; PTHR16029; PTHR16029; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Reference proteome.
FT CHAIN 1..824
FT /note="Spindle-defective protein 2"
FT /id="PRO_0000072112"
FT REGION 16..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..131
FT /evidence="ECO:0000255"
FT COILED 304..324
FT /evidence="ECO:0000255"
FT COMPBIAS 16..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 573
FT /note="G->S: In or183; induces centrosome defects leading
FT to defects in bipolar spindle assembly."
FT /evidence="ECO:0000269|PubMed:15068791"
FT MUTAGEN 615
FT /note="G->E: In or188; results in centrosome duplication
FT defects resulting in failure to assemble the bipolar
FT spindle. In some animals, the embryonic lethaliy phenotype
FT is rescued in a szy-20 (bs52) loss of function mutant
FT background with 65% of embryos displaying centrosome
FT duplication."
FT /evidence="ECO:0000269|PubMed:15068791,
FT ECO:0000269|PubMed:19081077"
FT MUTAGEN 710
FT /note="R->Q: In oj29; induces centrosome defects leading to
FT defects in bipolar spindle assembly."
FT /evidence="ECO:0000269|PubMed:15068791"
SQ SEQUENCE 824 AA; 91531 MW; 6D8AA983F162A1E5 CRC64;
MEDDAPMNLC NEQFEEIEDS PIDDNDNESF YNADGDVELE EEEVHETPKN FKNGGRFKTN
MTNPKVNDLT TIEEKNEDLR SAASSRSASR PASVMSDKSF SSQFEFQSGG ENAIEEYTNQ
VFADENKADL LFPETSKFMN GASPPKDKHH SWEPSIHHYD KQPPPDIQTN SPVFGNLNHR
KNKLIPQARA KPGANDNEIV ERDNDENVPT TSDKSAFITS PMNSTNHDEK TSTPKRPTNR
KIGQYQGPNF DLSSIYVGSP QHQNTSISTG QQMPTSSYSH AHSETMMTNQ TINESMVRRV
LNGNNKNQDL FAALEEARKR RAAQPSKPDF RINTTRTRVP IKPTSARHSG NVVSSTSNDN
TTAASSKDLT TSRKAMETFR QNASMADATN SNTASMTSIL STISTARTDI SRSSRNHGGG
FSNTSVSTVI PANNGNVSLS HGRDGRDSVS SVRTMSRASS TSTVYAGSTF SGVSKPLRIH
AKRVAFGCVA VGETLRVEVE VENISDRQCL VRASTDSTTP VYQILDNKLT MVDPKKSIKF
QVSFSPSSVG RYQVIMSIEV PAQNFIHKIP MWGNGGIAKF VPTSPDLQQT INQSEYAMCT
SCAKRISFKI SNSAGTRDGF AMIKVFDSAM RQLPDGCVAF FPAPGFIVKK KSDKRVDIRI
DSSYIDLHDE NNFRTSSSLS TASTTSSFQR RILPGAKFFV HVVWGEETMR TRLRLLEVRT
GQHQLIDGHD FTSFQFSDEE VLRAVPVGFP AIKPEDRDLF AASYRSFFIN FFTSTTEFRA
ATSRKKKEIC SNDDSTLLET TAFRNQTFVN DVTIVPNTRF SNRK
