SYMPK_XENLA
ID SYMPK_XENLA Reviewed; 1202 AA.
AC Q7ZYV9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Symplekin;
GN Name=sympk;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH CPSF2, CPSF73, CPSF160 AND SYMPK, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12006661; DOI=10.1091/mbc.01-12-0567;
RA Hofmann I., Schnoelzer M., Kaufmann I., Franke W.W.;
RT "Symplekin, a constitutive protein of karyo- and cytoplasmic particles
RT involved in mRNA biogenesis in Xenopus laevis oocytes.";
RL Mol. Biol. Cell 13:1665-1676(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH CPEB1; CPSF2 AND PAPD4.
RX PubMed=15550246; DOI=10.1016/j.cell.2004.10.029;
RA Barnard D.C., Ryan K., Manley J.L., Richter J.D.;
RT "Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic
RT polyadenylation.";
RL Cell 119:641-651(2004).
CC -!- FUNCTION: Involved in histone mRNA 3'-end processing (By similarity).
CC Involved in the cytoplasmic polyadenylation element (CPE)-mediated
CC polyadenylation of maternal mRNAs in maturing oocytes. Serves as a
CC scaffold upon which cytoplasmic polyadenylation regulatory factors are
CC assembled. {ECO:0000250, ECO:0000269|PubMed:15550246}.
CC -!- SUBUNIT: Identification in a complex with cpsf2, cpsf73, cpsf160 and
CC sympk. Interacts with cpeb1, cpsf2 and papd4.
CC {ECO:0000269|PubMed:12006661, ECO:0000269|PubMed:15550246}.
CC -!- INTERACTION:
CC Q7ZYV9; A8KBF3: piwil2; Xeno; NbExp=3; IntAct=EBI-7191476, EBI-7191401;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12006661}. Cytoplasm
CC {ECO:0000269|PubMed:12006661}. Note=Cajal bodies (CBs).
CC -!- DOMAIN: The HEAT repeats have been determined based on 3D-structure
CC analysis of the D.melanogaster ortholog and are not detected by
CC sequence-based prediction programs.
CC -!- SIMILARITY: Belongs to the Symplekin family. {ECO:0000305}.
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DR EMBL; BC047265; AAH47265.1; -; mRNA.
DR RefSeq; NP_001079691.1; NM_001086222.2.
DR RefSeq; XP_018087329.1; XM_018231840.1.
DR AlphaFoldDB; Q7ZYV9; -.
DR SMR; Q7ZYV9; -.
DR BioGRID; 97621; 2.
DR IntAct; Q7ZYV9; 1.
DR MINT; Q7ZYV9; -.
DR MaxQB; Q7ZYV9; -.
DR PRIDE; Q7ZYV9; -.
DR GeneID; 379378; -.
DR KEGG; xla:379378; -.
DR CTD; 379378; -.
DR Xenbase; XB-GENE-941665; sympk.S.
DR OMA; QVCKVKV; -.
DR OrthoDB; 386749at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 379378; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021850; Symplekin/Pta1.
DR InterPro; IPR032460; Symplekin/Pta1_N.
DR InterPro; IPR022075; Symplekin_C.
DR PANTHER; PTHR15245:SF20; PTHR15245:SF20; 1.
DR Pfam; PF11935; SYMPK_PTA1_N; 1.
DR Pfam; PF12295; Symplekin_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1202
FT /note="Symplekin"
FT /id="PRO_0000390504"
FT REPEAT 20..54
FT /note="HEAT 1"
FT REPEAT 57..91
FT /note="HEAT 2"
FT REPEAT 94..136
FT /note="HEAT 3"
FT REPEAT 143..182
FT /note="HEAT 4"
FT REPEAT 217..256
FT /note="HEAT 5"
FT REGION 323..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 134452 MW; C0E5839897716276 CRC64;
MAVSMASQFF SQEEGTSEVV STSERVVELL NMAALATNDT KITMLKQVQE LIINKDPTLL
DNFLDEIIAF QADKSVEVRK IVVNFIEEAC KLDNELLIKL IANLHMLLKD ENVNVVKKSI
LTMTQLYKVA LQWVARSRPP SEQQESCWDL VTEMAADILL LLESDNDGMR THAVKFVESL
IVTLSPRTAD SEVPKRQDGD ISLEQIPPDH QFLKYNTLRD LGKQAVKELL KFMAHPAISS
INLTAALGSL ASIARQRPMF MAEVIQAYET LHANLPPTLA KSQVSSVRKN LKLQLLSVLR
HPSSYEYQGP ISTLLLDLGT SQGEITRHLP PPRDSNRKRA REDGEGGQKK SRTDIPLPDD
DDDKDTMQLP TIPAPAPSTQ SATDITADFV RPLLSPENVA NLVLISMVYL PDSMPASFQS
TYTPVESAGT DSQIRHLARL MATQMSAAGI GPGVEQSKDI PVDVVEEENI KPEGLVIKRR
ISALTKGQAI SVLGCQSEKT KEEEEEEDDA PLAKKRPEPI LPATQIRPSG VGGRKKVFRL
KEVTEPLTDV QIKSLKLGAV RRILQAERSV GSSGASQMRV KVLARLVTQL DISVKAEVLS
HFLNDPRMRL DLALAWLYQE YCEYQSGAGE EGYQECLIGI LTGLQERPDQ RDGVFTKVVL
EAPLLTDSAL DVLRKYCEDE GRSYLGMSTL RDLILTRPAR QFQYLHLLLD LSSHEKDKIR
QQSLHFIKRM YEKESLRPYI EKFALNYLQL LVHPNPPSVL FGADKDTEVA APWTEDTVKQ
CLYLYLALLP QNHKLIHELA SVYTEATADI KRTVLRVIET PIRGMGMNSP ELLLLVENCP
KGAETLVTRC LHILTDKVPP SPELVKRVRE LYHKRLPDVR FLIPVLNGLD KKEVIQALPK
LIKLNPIVVK EVFNRLLGTQ HGEVSSSLSP LTPGDLLVAL HNIDSSKCDM KSVIKATNLC
FSARSVYTSE VLAVVLQQLM DTTPLPMLLM RTVIQALGMY PRLGGFIMNI LTRLIYKQVW
KYPKVWEGFI KCCQRTKPQS FSVLLQLPPP QLLSVLQTSP DLRDPLLAHV RAFTPHQLAH
VPHSIMAILE AESRTDAGAE EAAQVEEEQE TPAQDIIARR LAQEKSLKKQ IEEQKGRNNQ
EMEEVAEVDP PAIFIAEEEE EESLKSQGKE EPQEDSSSNA TTAEKSPVAD EPMEEEPVEK
KD
