PAT9_CAEEL
ID PAT9_CAEEL Reviewed; 470 AA.
AC Q22829;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc finger protein pat-9 {ECO:0000305};
DE AltName: Full=Paralyzed arrest at two-fold pat-9 {ECO:0000312|WormBase:T27B1.2};
GN Name=pat-9 {ECO:0000312|WormBase:T27B1.2};
GN Synonyms=ztf-19 {ECO:0000312|WormBase:T27B1.2};
GN ORFNames=T27B1.2 {ECO:0000312|WormBase:T27B1.2};
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22616817; DOI=10.1186/2045-3701-2-18;
RA Liu Q., Jones T.I., Bachmann R.A., Meghpara M., Rogowski L., Williams B.D.,
RA Jones P.L.;
RT "C. elegans PAT-9 is a nuclear zinc finger protein critical for the
RT assembly of muscle attachments.";
RL Cell Biosci. 2:18-18(2012).
CC -!- FUNCTION: Probable transcription factor; required for proper
CC organization of muscle myofilaments and for their recruitment to the M
CC line. {ECO:0000269|PubMed:22616817}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22616817}. Chromosome
CC {ECO:0000269|PubMed:22616817}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle and gonad (at protein
CC level). {ECO:0000269|PubMed:22616817}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis and throughout
CC all developmental stages (at protein level) (PubMed:22616817).
CC Expressed in body wall muscle in embryos, young larvae and adults (at
CC protein level) (PubMed:22616817). {ECO:0000269|PubMed:22616817}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes paralysis and
CC arrested elongation at the two-fold stage of embryonic development.
CC {ECO:0000269|PubMed:22616817}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BX284606; CCD72790.1; -; Genomic_DNA.
DR PIR; T34392; T34392.
DR RefSeq; NP_510680.2; NM_078279.3.
DR AlphaFoldDB; Q22829; -.
DR SMR; Q22829; -.
DR IntAct; Q22829; 2.
DR STRING; 6239.T27B1.2; -.
DR EPD; Q22829; -.
DR PaxDb; Q22829; -.
DR PeptideAtlas; Q22829; -.
DR EnsemblMetazoa; T27B1.2.1; T27B1.2.1; WBGene00003933.
DR GeneID; 181714; -.
DR KEGG; cel:CELE_T27B1.2; -.
DR UCSC; T27B1.2.1; c. elegans.
DR CTD; 181714; -.
DR WormBase; T27B1.2; CE38558; WBGene00003933; pat-9.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000169555; -.
DR HOGENOM; CLU_565297_0_0_1; -.
DR InParanoid; Q22829; -.
DR OMA; CNARFNR; -.
DR OrthoDB; 836090at2759; -.
DR PhylomeDB; Q22829; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003933; Expressed in embryo and 3 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0051153; P:regulation of striated muscle cell differentiation; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Chromosome; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..470
FT /note="Zinc finger protein pat-9"
FT /id="PRO_0000454143"
FT ZN_FING 84..106
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 112..134
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..230
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22616817"
FT COMPBIAS 196..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 52437 MW; F1411E91D48DE61D CRC64;
MENRTPMQHH SGYEIVKSEP PSTPKTLIKS SYMENTPEMV FGSFPIHSGF CTQVVTHTDP
MNNNNQPKTN ANGRALAADR KRPYPCNLCS SKFGSKMELE EHQNSHTGQK PFECDTCNAR
FNRRSTLWNH KRIHSDAKPF VCTVCQMTFK WKNSLKCHKD MHQRKNETSA HLDNDLRQLT
YATAAKRKLQ MEQEENGGLP ASSSASSVIS HPLITTTSGN KKRSKAAKAK QTPSSLATTL
SQVHLGAVQP LHASALVPPS DHQIDLDTTS LDSLMQSQNQ NFLMQLYGYS DDGRHNGGML
SLDDTMLSNL SDSKSDSGSS SGGLSIQLPM QTINMLNFRN LGTQQLPPVH QLASSLPSVS
SGMDYVNVNQ HDSHYIVSQP DMMLGNQPLY HNGSFANIEK SNPHNNQFTI DSCVLLPSSR
QDYPFDYTMV NQQYPMQEQV HDQTVGVSVV QQHYAEQAHA HGKTVPHEQW
