WDR33_CAEEL
ID WDR33_CAEEL Reviewed; 809 AA.
AC U4PCM1; A0A5S9MNP8; U4PN22;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=pre-mRNA 3' end processing protein pfs-2 {ECO:0000305};
DE AltName: Full=Polyadenylation factor subunit homolog 2 {ECO:0000303|PubMed:20530551};
GN Name=pfs-2 {ECO:0000303|PubMed:20530551, ECO:0000312|WormBase:R06A4.9a};
GN ORFNames=R06A4.9 {ECO:0000312|EMBL:CDH93484.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ARG-147.
RX PubMed=20530551; DOI=10.1242/dev.049692;
RA Van Epps H., Dai Y., Qi Y., Goncharov A., Jin Y.;
RT "Nuclear pre-mRNA 3'-end processing regulates synapse and axon development
RT in C. elegans.";
RL Development 137:2237-2250(2010).
CC -!- FUNCTION: Essential for both cleavage and polyadenylation of pre-mRNA
CC 3' ends (By similarity). Involved in neuron development, probably by
CC regulating pre-mRNA 3'-end processing (PubMed:20530551).
CC {ECO:0000250|UniProtKB:Q9C0J8, ECO:0000269|PubMed:20530551}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:20530551}.
CC Note=Also localizes to a small subnuclear ring in neurons. In neurons,
CC partially co-localizes with sydn-1 in the nucleus.
CC {ECO:0000269|PubMed:20530551}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:R06A4.9a};
CC IsoId=U4PCM1-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R06A4.9b};
CC IsoId=U4PCM1-2; Sequence=VSP_060922;
CC Name=c {ECO:0000312|WormBase:R06A4.9c};
CC IsoId=U4PCM1-3; Sequence=VSP_060923, VSP_060924;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and in some non-neuronal
CC cells. {ECO:0000269|PubMed:20530551}.
CC -!- DOMAIN: The C-terminus is required for the regulation of synapse and
CC axon development. {ECO:0000269|PubMed:20530551}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a sydn-1, eri-1 and
CC syd-2 mutant background suppresses ectopic axon branches and synapse
CC defects and causes sterility. {ECO:0000269|PubMed:20530551}.
CC -!- MISCELLANEOUS: [Isoform a]: (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR33 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA0059168.1; -; Genomic_DNA.
DR EMBL; BX284602; CDH93484.2; -; Genomic_DNA.
DR EMBL; BX284602; CDH93485.1; -; Genomic_DNA.
DR RefSeq; NP_001293597.1; NM_001306668.1.
DR RefSeq; NP_001293598.1; NM_001306669.1.
DR AlphaFoldDB; U4PCM1; -.
DR SMR; U4PCM1; -.
DR IntAct; U4PCM1; 1.
DR STRING; 6239.R06A4.9a; -.
DR EPD; U4PCM1; -.
DR PaxDb; U4PCM1; -.
DR PeptideAtlas; U4PCM1; -.
DR EnsemblMetazoa; R06A4.9a.1; R06A4.9a.1; WBGene00011051. [U4PCM1-1]
DR EnsemblMetazoa; R06A4.9b.1; R06A4.9b.1; WBGene00011051. [U4PCM1-2]
DR EnsemblMetazoa; R06A4.9c.1; R06A4.9c.1; WBGene00011051. [U4PCM1-3]
DR WormBase; R06A4.9a; CE21113; WBGene00011051; pfs-2. [U4PCM1-1]
DR WormBase; R06A4.9b; CE48640; WBGene00011051; pfs-2. [U4PCM1-2]
DR WormBase; R06A4.9c; CE53932; WBGene00011051; pfs-2. [U4PCM1-3]
DR eggNOG; KOG0284; Eukaryota.
DR GeneTree; ENSGT00730000111130; -.
DR HOGENOM; CLU_014193_0_0_1; -.
DR OrthoDB; 604979at2759; -.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-CEL-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:U4PCM1; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011051; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; U4PCM1; baseline and differential.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:WormBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045245; Pfs2-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22836; PTHR22836; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; Nucleus; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..809
FT /note="pre-mRNA 3' end processing protein pfs-2"
FT /id="PRO_0000447209"
FT REPEAT 131..170
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 173..212
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 215..254
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 257..298
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 301..340
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 343..385
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 387..426
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 531..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060922"
FT VAR_SEQ 173..219
FT /note="AHDSAIRALKWASNEQWLLSADQGGYVKYWQPNMNNAHMFSAHKDEA -> V
FT KHTTRWITILYIMFTFLCSTNKVFTSFLMRHFAVFDVNKRFSFGIF (in isoform
FT c)"
FT /id="VSP_060923"
FT VAR_SEQ 220..809
FT /note="Missing (in isoform c)"
FT /id="VSP_060924"
FT MUTAGEN 147
FT /note="R->Q: In ju608; decrease in brood size with no
FT defect in locomotion, body size, behavior and synapses.
FT Suppresses abnormal synapse formation in a sydn-1 (ju541)
FT mutant background. Suppresses multivulva formation in a
FT lin-15(n765ts) mutant background."
FT /evidence="ECO:0000269|PubMed:20530551"
SQ SEQUENCE 809 AA; 90057 MW; 1F22E34789248C72 CRC64;
MNGGMMRGNQ MPNVTLTIQP STSSMQNSQP RIMNNHHHPH NRFQREHVMP DVMGDGPGRR
LRKNVANVRR HVDYVSTVLN HCENRLWQYG KQRILQQPDI LYQQYAVPAD STPDVPVDCI
LTKFIRTAMN KVKCPVYSVC WSPEGKRLIT GCQTGEFTLW NGTAFNFETI LQAHDSAIRA
LKWASNEQWL LSADQGGYVK YWQPNMNNAH MFSAHKDEAI RGLAFAPTDV KFATASDDGT
ARVWDFARYT EERVLRGHGA EVRCIDWHPT KGLIATGSRD TQQPVKIWDP KSGSCLATLQ
EHKSSVMAVE FNKNGNWLLT GGRDHLVKMY DIRMMKEMRT YRAHKKEVIS LAWHPIHEGL
FVSGGGDGSI VYWMVDGEKE IGLLEHAHDQ AIWSMKWHPL GHILATGSND NNTKFWARNR
PGDTVEDIFG LSNTNMIGHL DKEREPRMAP PKPSIETQET YRPDTFIPGM GLDEHLYEQL
NRDHNMMTTD STLLVPDDLT RQNFAPMIGA KRTLIKQPPA KKAQRQFERM WNNSKGIGAG
SDDFTTMKGG LGREDAEGAQ FGPSKSFLGP PTTGGSLLGP SQPRPQEFRS VPPPQQQQGP
PPNWRHQGPP MSGPGQGYGP PGRMGGNQGG WQRPPPQGSY GGQGPPQGSY GGQGTLQGSY
ASQQGPPPRQ IQHIPSDIDY RTAPSSSNGS TGDVDMRTMV PNQPPSGEPE HWRGPPPVSH
QQQSQQQHPP PINMQRMDPR RDPRMLSGRS DQLSPSGPPP QQQQSSAQQG GKNQWMPQFE
AGQNQNQGNY AGNRGGGVGG RGRGRGQPY
