PXL1_CAEEL
ID PXL1_CAEEL Reviewed; 413 AA.
AC Q09476; A7YEM2; A7YEP3; A8WEL3; Q6AHR2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Paxillin homolog 1;
GN Name=pxl-1; Synonyms=tag-327; ORFNames=C28H8.6;
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] (ISOFORMS A; B AND C), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21633109; DOI=10.1091/mbc.e10-12-0941;
RA Warner A., Qadota H., Benian G.M., Vogl A.W., Moerman D.G.;
RT "The Caenorhabditis elegans paxillin orthologue, PXL-1, is required for
RT pharyngeal muscle contraction and for viability.";
RL Mol. Biol. Cell 22:2551-2563(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Required for myofilament organization of the pharyngeal
CC sarcomeres and for pharyngeal muscle contractions and hence for
CC pharyngeal pumping (PubMed:21633109). Together with lin-8, might be
CC required for myofilament organization in the body wall muscles
CC (PubMed:21633109). {ECO:0000269|PubMed:21633109}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cell junction, adherens junction
CC {ECO:0000269|PubMed:21633109}. Cell membrane
CC {ECO:0000269|PubMed:21633109}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:21633109}. Cell projection, podosome
CC {ECO:0000269|PubMed:21633109}. Note=Colocalizes with pat-3 to dense
CC bodies, adhesion plaques and M lines in body wall muscles. Colocalizes
CC with deb-1 in podosome-like structures in the pharyngeal muscle.
CC Requires unc-95 for the localization to dense bodies.
CC {ECO:0000269|PubMed:21633109}.
CC -!- SUBCELLULAR LOCATION: [Isoform c]: Cell projection, podosome
CC {ECO:0000269|PubMed:21633109}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q09476-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q09476-2; Sequence=VSP_035943, VSP_020533, VSP_020534,
CC VSP_020535;
CC Name=c;
CC IsoId=Q09476-3; Sequence=VSP_035944;
CC -!- TISSUE SPECIFICITY: Isoform a: Expressed in all 95 body wall muscle
CC cells as well as in the pharyngeal muscle cells (at protein level).
CC Isoform c: Expressed in the body wall muscle cells and in the
CC pharyngeal muscle cells. {ECO:0000269|PubMed:21633109}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult animals.
CC {ECO:0000269|PubMed:21633109}.
CC -!- DOMAIN: LIM zinc-binding domains 1-4 are sufficient for the
CC localization to dense bodies, adhesion plaques and M lines in body wall
CC muscles. {ECO:0000269|PubMed:21633109}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to developmental
CC arrest at larval stage L1. {ECO:0000269|PubMed:21633109}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
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DR EMBL; EU239658; ABW99674.1; -; mRNA.
DR EMBL; EU239659; ABW99675.1; -; mRNA.
DR EMBL; EU239660; ABW99676.1; -; mRNA.
DR EMBL; FO080703; CCD65967.1; -; Genomic_DNA.
DR EMBL; FO080703; CCD65977.1; -; Genomic_DNA.
DR EMBL; FO080703; CCD65976.1; -; Genomic_DNA.
DR PIR; E88469; E88469.
DR RefSeq; NP_001021185.2; NM_001026014.2. [Q09476-1]
DR RefSeq; NP_001021186.1; NM_001026015.2. [Q09476-2]
DR RefSeq; NP_001122677.1; NM_001129205.1. [Q09476-3]
DR AlphaFoldDB; Q09476; -.
DR SMR; Q09476; -.
DR BioGRID; 41053; 10.
DR DIP; DIP-27019N; -.
DR STRING; 6239.C28H8.6a; -.
DR EPD; Q09476; -.
DR PaxDb; Q09476; -.
DR PeptideAtlas; Q09476; -.
DR EnsemblMetazoa; C28H8.6a.1; C28H8.6a.1; WBGene00016197. [Q09476-1]
DR EnsemblMetazoa; C28H8.6b.1; C28H8.6b.1; WBGene00016197. [Q09476-2]
DR EnsemblMetazoa; C28H8.6c.1; C28H8.6c.1; WBGene00016197. [Q09476-3]
DR GeneID; 175831; -.
DR KEGG; cel:CELE_C28H8.6; -.
DR UCSC; C28H8.6b; c. elegans.
DR CTD; 175831; -.
DR WormBase; C28H8.6a; CE41530; WBGene00016197; pxl-1. [Q09476-1]
DR WormBase; C28H8.6b; CE37096; WBGene00016197; pxl-1. [Q09476-2]
DR WormBase; C28H8.6c; CE41531; WBGene00016197; pxl-1. [Q09476-3]
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000172970; -.
DR InParanoid; Q09476; -.
DR OMA; CSISATW; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; Q09476; -.
DR Reactome; R-CEL-180292; GAB1 signalosome.
DR Reactome; R-CEL-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-CEL-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-CEL-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR PRO; PR:Q09476; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016197; Expressed in larva and 3 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0017166; F:vinculin binding; IPI:WormBase.
DR GO; GO:0061061; P:muscle structure development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; LIM domain; Membrane; Metal-binding; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..413
FT /note="Paxillin homolog 1"
FT /id="PRO_0000355614"
FT DOMAIN 174..232
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 233..292
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 293..350
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 351..410
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 33..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:21633109"
FT /id="VSP_035943"
FT VAR_SEQ 59..119
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:21633109"
FT /id="VSP_035944"
FT VAR_SEQ 88..119
FT /note="YENESRLNPPVYSRPSVQSLLSQVEEPPIRAS -> MMRELQQRLDHFNGPN
FT YAQNSHSNHQQHHSVY (in isoform b)"
FT /evidence="ECO:0000303|PubMed:21633109"
FT /id="VSP_020533"
FT VAR_SEQ 322..343
FT /note="HCGVSFNGASFFEHNGAPLCER -> GNTHFAQQCPMDVTYFEEENAY (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:21633109"
FT /id="VSP_020534"
FT VAR_SEQ 344..413
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:21633109"
FT /id="VSP_020535"
SQ SEQUENCE 413 AA; 46453 MW; 1573744C0BC34170 CRC64;
MPSDDRFADA VKPALEALLS DLQHTTEVLR RAHISDRRSQ SRDDFEQSYD LQGNLNTQSV
SNGNITTSPY KRRSSEGKDY SKSQERIYEN ESRLNPPVYS RPSVQSLLSQ VEEPPIRASS
SRKSLGPPSQ AQSYSDVRSN GRSPSRDPLH SDSMIGTMNG ELSSKHGVNT IPKGDCAACG
KPIIGQVVIA LGKMWHPEHY TCCECGAELG QRPFFERNGR AFCEEDYHNQ FSPKCQGCHR
AITDRCVSVM NKNFHIECFT CAECNQPFGE DGFHEKNGQT YCKRDFFRLF APKCNGCSQP
ITSNFITALG THWHPDCFVC QHCGVSFNGA SFFEHNGAPL CERHYHESRG SICSQCRGAI
NGRCVAAMGR KFHPEHFRCS YCNHQLTKGT FKEVDRRPFC HKCYNNTYAL TPA
