PARV_CAEEL
ID PARV_CAEEL Reviewed; 375 AA.
AC O16785;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Paralyzed arrest at two-fold protein 6;
DE AltName: Full=Actopaxin homolog;
DE AltName: Full=Parvin-like protein;
GN Name=pat-6 {ECO:0000312|WormBase:T21D12.4};
GN ORFNames=T21D12.4 {ECO:0000312|WormBase:T21D12.4};
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 [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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PAT-4,
RP IDENTIFICATION IN A COMPLEX WITH UNC-112 AND PAT-4, AND MUTAGENESIS OF
RP PHE-275.
RX PubMed=12781130; DOI=10.1016/s0960-9822(03)00372-5;
RA Lin X., Qadota H., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-6/actopaxin plays a critical role in the assembly of
RT integrin adhesion complexes in vivo.";
RL Curr. Biol. 13:922-932(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [4]
RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471;
RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F.,
RA Jacobson L.A., Szewczyk N.J.;
RT "Calpains mediate integrin attachment complex maintenance of adult muscle
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002471-E1002471(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA Benian G.M.;
RT "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT is required for myofilament stability in Caenorhabditis elegans.";
RL Mol. Biol. Cell 24:601-616(2013).
CC -!- FUNCTION: Involved in the regulation of cell adhesion and cytoskeleton
CC organization. Component of an integrin containing attachment complex,
CC which is required for muscle development and maintenance
CC (PubMed:22253611). During embryonic development, required to recruit
CC cpna-1, unc-89 and myofilaments to newly forming integrin attachments
CC composed of integrins pat-2/pat-3, pat-4 and unc-112 (PubMed:12781130,
CC PubMed:23283987). Also required to reposition the integrin-based
CC attachments so that they form the highly ordered array of dense body
CC and M-line attachments that are characteristic of mature muscle cells
CC (PubMed:12781130, PubMed:23283987). During the formation of
CC neuromuscular junctions at the larval stage, negatively regulates
CC membrane protrusion from body wall muscles (PubMed:16495308).
CC {ECO:0000269|PubMed:12781130, ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:23283987}.
CC -!- SUBUNIT: May interact (via calponin-homology (CH) 2 domain) with pat-4
CC (via kinase domain) (PubMed:12781130). May form a complex with unc-112
CC and pat-4 (PubMed:12781130). Component of an integrin containing
CC attachment complex, composed of at least pat-2, pat-3, pat-4, pat-6,
CC unc-52, unc-97 and unc-112 (PubMed:22253611).
CC {ECO:0000269|PubMed:12781130, ECO:0000305|PubMed:22253611}.
CC -!- INTERACTION:
CC O16785; Q9TZC4: pat-4; NbExp=4; IntAct=EBI-328106, EBI-1564527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12781130}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:23283987}. Perikaryon
CC {ECO:0000269|PubMed:12781130}. Cell projection, axon
CC {ECO:0000269|PubMed:12781130}. Note=Colocalizes with integrins and pat-
CC 4/ILK (PubMed:12781130). Colocalizes to M line and dense bodies with
CC cpna-1 (PubMed:23283987). {ECO:0000269|PubMed:12781130,
CC ECO:0000269|PubMed:23283987}.
CC -!- TISSUE SPECIFICITY: Expressed from 1.5 stage embryos, mostly within the
CC muscle cells (PubMed:12781130, PubMed:23283987). In adult
CC hermaphrodites, expressed in the attachments of other muscles,
CC including the uterine, anal depressor, anal sphincter, and vulval
CC muscles, as well as in the spermatheca and the distal tip cells
CC (PubMed:12781130). Expressed in mechanosensory receptor neurons ALML/R,
CC PLML/R, AVM, and PVM (PubMed:12781130). Localizes at body wall muscle
CC attachments (PubMed:12781130, PubMed:23283987).
CC {ECO:0000269|PubMed:12781130, ECO:0000269|PubMed:23283987}.
CC -!- DOMAIN: The calponin-homology (CH) domains are essential for its
CC function during attachment assembly and the interaction with pat-4.
CC -!- DISRUPTION PHENOTYPE: In mutant embryos, abnormal accumulation of cpna-
CC 1 into large foci in body wall muscle cells (PubMed:23283987). RNAi-
CC mediated knockdown results in impaired mobility, mitochondrial
CC fragmentation and disrupted integrin attachment complexes in muscle
CC (PubMed:22253611). This leads to degradation of muscle proteins in the
CC cytosol, myofibrillar defects and disruption of sarcomere organization
CC (PubMed:22253611). RNAi-mediated knockdown in L4 larval stage, causes
CC ectopic membrane extensions from body wall muscles (PubMed:16495308).
CC {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:22253611,
CC ECO:0000269|PubMed:23283987}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; BX284604; CCD72524.1; -; Genomic_DNA.
DR PIR; T28710; T28710.
DR RefSeq; NP_499891.1; NM_067490.5.
DR AlphaFoldDB; O16785; -.
DR SMR; O16785; -.
DR BioGRID; 42010; 17.
DR DIP; DIP-25618N; -.
DR IntAct; O16785; 3.
DR STRING; 6239.T21D12.4; -.
DR iPTMnet; O16785; -.
DR EPD; O16785; -.
DR PaxDb; O16785; -.
DR PeptideAtlas; O16785; -.
DR PRIDE; O16785; -.
DR EnsemblMetazoa; T21D12.4.1; T21D12.4.1; WBGene00003932.
DR GeneID; 176848; -.
DR KEGG; cel:CELE_T21D12.4; -.
DR UCSC; T21D12.4; c. elegans.
DR CTD; 176848; -.
DR WormBase; T21D12.4; CE18268; WBGene00003932; pat-6.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR HOGENOM; CLU_047624_2_0_1; -.
DR InParanoid; O16785; -.
DR OMA; QIRIEVP; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; O16785; -.
DR Reactome; R-CEL-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-CEL-446353; Cell-extracellular matrix interactions.
DR Reactome; R-CEL-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR PRO; PR:O16785; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003932; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0055002; P:striated muscle cell development; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028433; Parvin.
DR PANTHER; PTHR12114; PTHR12114; 1.
DR Pfam; PF00307; CH; 2.
DR PIRSF; PIRSF039131; Parvin; 1.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Cell projection; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..375
FT /note="Paralyzed arrest at two-fold protein 6"
FT /id="PRO_0000121587"
FT DOMAIN 99..206
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 266..373
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 275
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:12781130"
SQ SEQUENCE 375 AA; 43001 MW; F9DB8B807671D0C1 CRC64;
MSTLGRSKTP SRDEPKKPGV FEKLSGTLSR KKKAPEDEHG NQGGAHHATD EDEVLELELE
GREALDQSLV PVLARNIWLE EGEIRRYLTK ETARDQKLAQ VVDLLIYWLN EELADQRIVV
RHLQEDLFDG QIIQKLLEKL EQIRIEVPEV SQSEEGQRQK LQIVVQTANR ILGQPREQEK
WSADLIHQKD FTAIIQLLVL LALHYRAPVR FPDNVVANVV VAQKEHGQVK THRITEQITT
VQTELAPKGT RDAFDTLFDY GPDKLAHVKT SLLAFCNKHL NKINLEVSDL DNQFQDGVFL
VLLVGLLEGY FVPLYHFNLQ VQSHEEKVKN VQFAFKLMED TGLEKPRSRV QDIANGDVKS
TLRLLHLLFT KYKHI
