SPD5_CAEEL
ID SPD5_CAEEL Reviewed; 1198 AA.
AC P91349;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Spindle-defective protein 5;
GN Name=spd-5; ORFNames=F56A3.4;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-592.
RC STRAIN=Bristol N2;
RX PubMed=12431374; DOI=10.1016/s1534-5807(02)00327-1;
RA Hamill D.R., Severson A.F., Carter J.C., Bowerman B.;
RT "Centrosome maturation and mitotic spindle assembly in C. elegans require
RT SPD-5, a protein with multiple coiled-coil domains.";
RL Dev. Cell 3:673-684(2002).
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 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).
CC -!- FUNCTION: Plays a central role in centrosome maturation and mitotic
CC spindle assembly during the first division of the zygote. Required for
CC the centrosomal localization of air-1 and zyg-9. Probably not required
CC in late embryogenesis and during larval development.
CC {ECO:0000269|PubMed:12431374}.
CC -!- INTERACTION:
CC P91349; P34331: plk-1; NbExp=3; IntAct=EBI-322479, EBI-315211;
CC P91349; P91870: spd-2; NbExp=3; IntAct=EBI-322479, EBI-320962;
CC P91349; P91349: spd-5; NbExp=4; IntAct=EBI-322479, EBI-322479;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:12431374,
CC ECO:0000269|PubMed:17115027}. Note=Component of the centrosome. First
CC expressed at two different foci in early postmeiotic one-cell stage
CC embryos, prior to pronuclear migration but after the sperm-donated
CC centriole duplication. These two foci greatly increase in size prior to
CC and during mitosis. In metaphase, it is localized throughout
CC centrosomes. In late anaphase or telophase, it surrounds a central core
CC devoid of microtubules. Its localization is independent of microtubules
CC and other centrosomal proteins (PubMed:12431374). 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:12431374,
CC ECO:0000269|PubMed:17115027}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis and during
CC postembryonic meiotic divisions that produce sperm in males.
CC {ECO:0000269|PubMed:12431374}.
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DR EMBL; FO080752; CCD66432.1; -; Genomic_DNA.
DR PIR; T29145; T29145.
DR RefSeq; NP_491539.1; NM_059138.4.
DR AlphaFoldDB; P91349; -.
DR SMR; P91349; -.
DR BioGRID; 37615; 19.
DR ComplexPortal; CPX-1357; RSA centrosome-targeting complex.
DR DIP; DIP-24727N; -.
DR IntAct; P91349; 10.
DR STRING; 6239.F56A3.4; -.
DR iPTMnet; P91349; -.
DR EPD; P91349; -.
DR PaxDb; P91349; -.
DR PeptideAtlas; P91349; -.
DR EnsemblMetazoa; F56A3.4.1; F56A3.4.1; WBGene00004955.
DR EnsemblMetazoa; F56A3.4.2; F56A3.4.2; WBGene00004955.
DR GeneID; 172155; -.
DR KEGG; cel:CELE_F56A3.4; -.
DR UCSC; F56A3.4; c. elegans.
DR CTD; 172155; -.
DR WormBase; F56A3.4; CE28834; WBGene00004955; spd-5.
DR eggNOG; ENOG502RVPP; Eukaryota.
DR HOGENOM; CLU_269384_0_0_1; -.
DR InParanoid; P91349; -.
DR OMA; ENENKHC; -.
DR OrthoDB; 421255at2759; -.
DR PhylomeDB; P91349; -.
DR SignaLink; P91349; -.
DR PRO; PR:P91349; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004955; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007098; P:centrosome cycle; IMP:WormBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:ComplexPortal.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:WormBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Reference proteome.
FT CHAIN 1..1198
FT /note="Spindle-defective protein 5"
FT /id="PRO_0000072113"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..381
FT /evidence="ECO:0000255"
FT COILED 566..603
FT /evidence="ECO:0000255"
FT COILED 694..916
FT /evidence="ECO:0000255"
FT COILED 983..1035
FT /evidence="ECO:0000255"
FT COILED 1127..1175
FT /evidence="ECO:0000255"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 592
FT /note="R->K: In OR213ts; induces defective centrosomes at
FT restrictive temperature when homozygous."
FT /evidence="ECO:0000269|PubMed:12431374"
SQ SEQUENCE 1198 AA; 135148 MW; FDFE3AAB765EA2B9 CRC64;
MEDNSVLNED SNLEHVEGQP RRSMSQPVLN VEGDKRTSST SATQQQVLSG AFSSADVRSI
PIIQTWEENK ALKTKITILR GELQMYQRRY SEAKEASQKR VKEVMDDYVD LKLGQENVQE
KMEQYKLMEE DLLAMQSRIE TSEDNFARQM KEFEAQKHAM EERIKELELS ATDANNTTVG
SFRGTLDDIL KKNDPDFTLT SGYEERKIND LEAKLLSEID KVAELEDHIQ QLRQELDDQS
ARLADSENVR AQLEAATGQG ILGAAGNAMV PNSTFMIGNG RESQTRDQLN YIDDLETKLA
DAKKENDKAR QALVEYMNKC SKLEHEIRTM VKNSTFDSSS MLLGGQTSDE LKIQIGKVNG
ELNVLRAENR ELRIRCDQLT GGDGNLSISL GQSRLMAGIA TNDVDSIGQG NETGGTSMRI
LPRESQLDDL EESKLPLMDT SSAVRNQQQF ASMWEDFESV KDSLQNNHND TLEGSFNSSM
PPPGRDATQS FLSQKSFKNS PIVMQKPKSL HLHLKSHQSE GAGEQIQNNS FSTKTASPHV
SQSHIPILHD MQQILDSSAM FLEGQHDVAV NVEQMQEKMS QIREALARLF ERLKSSAALF
EEILERMGSS DPNADKIKKM KLAFETSIND KLNVSAILEA AEKDLHNMSL NFSILEKSIV
SQAAEASRRF TIAPDAEDVA SSSLLNASYS PLFKFTSNSD IVEKLQNEVS ELKNELEMAR
TRDMRSPLNG SSGRLSDVQI NTNRMFEDLE VSEATLQKAK EENSTLKSQF AELEANLHQV
NSKLGEVRCE LNEALARVDG EQETRVKAEN ALEEARQLIS SLKHEENELK KTITDMGMRL
NEAKKSDEFL KSELSTALEE EKKSQNLADE LSEELNGWRM RTKEAENKVE HASSEKSEML
ERIVHLETEM EKLSTSEIAA DYCSTKMTER KKEIELAKYR EDFENAAIVG LERISKEISE
LTKKTLKAKI IPSNISSIQL VCDELCRRLS REREQQHEYA KVMRDVNEKI EKLQLEKDAL
EHELKMMSSN NENVPPVGTS VSGMPTKTSN QKCAQPHYTS PTRQLLHEST MAVDAIVQKL
KKTHNMSGMG PELKETIGNV INESRVLRDF LHQKLILFKG IDMSNWKNET VDQLITDLGQ
LHQDNLMLEE QIKKYKKELK LTKSAIPTLG VEFQDRIKTE IGKIATDMGG AVKEIRKK
