UNC87_CAEEL
ID UNC87_CAEEL Reviewed; 565 AA.
AC P37806; Q6EZG6; Q9TYS6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein unc-87;
DE AltName: Full=Uncoordinated protein 87;
GN Name=unc-87; ORFNames=F08B6.4;
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 [GENOMIC DNA / MRNA], FUNCTION, ALTERNATIVE SPLICING
RP (ISOFORMS A AND B), AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7929573; DOI=10.1083/jcb.127.1.79;
RA Goetinck S.D., Waterston R.H.;
RT "The Caenorhabditis elegans muscle-affecting gene unc-87 encodes a novel
RT thin filament-associated protein.";
RL J. Cell Biol. 127:79-93(1994).
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).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-207.
RX PubMed=7929572; DOI=10.1083/jcb.127.1.71;
RA Goetinck S., Waterston R.H.;
RT "The Caenorhabditis elegans UNC-87 protein is essential for maintenance,
RT but not assembly, of bodywall muscle.";
RL J. Cell Biol. 127:71-78(1994).
RN [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH F-ACTIN, AND DOMAIN.
RX PubMed=11096113; DOI=10.1074/jbc.m009561200;
RA Kranewitter W.J., Ylanne J., Gimona M.;
RT "UNC-87 is an actin-bundling protein.";
RL J. Biol. Chem. 276:6306-6312(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ALA-207.
RX PubMed=17684058; DOI=10.1242/jcs.013516;
RA Yamashiro S., Gimona M., Ono S.;
RT "UNC-87, a calponin-related protein in C. elegans, antagonizes ADF/cofilin-
RT mediated actin filament dynamics.";
RL J. Cell Sci. 120:3022-3033(2007).
RN [6]
RP FUNCTION, INTERACTION WITH MYOSIN AND F-ACTIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25717181; DOI=10.1091/mbc.e14-10-1483;
RA Ono K., Obinata T., Yamashiro S., Liu Z., Ono S.;
RT "UNC-87 isoforms, Caenorhabditis elegans calponin-related proteins,
RT interact with both actin and myosin and regulate actomyosin
RT contractility.";
RL Mol. Biol. Cell 26:1687-1698(2015).
CC -!- FUNCTION: Thin filament-associated protein that is implicated in actin
CC bundling and actin filament dynamics (PubMed:7929573, PubMed:7929572,
CC PubMed:11096113, PubMed:17684058, PubMed:25717181). Exhibits F-actin
CC cross-linking activity (PubMed:11096113, PubMed:17684058). Required for
CC the maintenance of sarcomeric actin organization in striated muscles
CC (PubMed:7929573, PubMed:7929572). Competes with unc-60 isoform b for
CC actin binding and protects actin filaments from depolymerization by
CC unc-60, thereby contributing to actin filament stability
CC (PubMed:17684058). Cooperates with myosin to form actomyosin bundles
CC and inhibits actomyosin ATPase activity and actomyosin motility
CC (PubMed:25717181). Might protect the myofilaments from mechanical
CC stress (PubMed:7929572). {ECO:0000269|PubMed:11096113,
CC ECO:0000269|PubMed:17684058, ECO:0000269|PubMed:25717181,
CC ECO:0000269|PubMed:7929572, ECO:0000269|PubMed:7929573}.
CC -!- FUNCTION: [Isoform b]: Acts as a negative regulator of myosin-dependent
CC contractility of smooth muscle-like cells in the somatic gonad.
CC {ECO:0000269|PubMed:25717181}.
CC -!- SUBUNIT: Monomer (PubMed:11096113). Interacts with F-actin
CC (PubMed:11096113, PubMed:25717181). Interacts with myosin
CC (PubMed:25717181). {ECO:0000269|PubMed:11096113,
CC ECO:0000269|PubMed:25717181}.
CC -!- INTERACTION:
CC P37806; G5EGG0: uso-1; NbExp=3; IntAct=EBI-319806, EBI-311986;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000269|PubMed:17684058, ECO:0000269|PubMed:25717181}. Note=Absent
CC from the distal edges of the thin filament. Isoform b: Partially
CC overlaps with the region where myo-3 is located.
CC {ECO:0000269|PubMed:17684058, ECO:0000269|PubMed:25717181}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P37806-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P37806-2; Sequence=VSP_000757, VSP_020110;
CC Name=c;
CC IsoId=P37806-3; Sequence=VSP_020109;
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscles
CC (PubMed:17684058). Isoform a: Expression in the pharynx, anal depressor
CC muscle, uterine muscle, vulva and unidentified neurons in the head and
CC the ventral region (PubMed:25717181). Isoform b: Expression in the body
CC wall muscles, spermatheca, vulva and in the myoepithelial sheath
CC (PubMed:25717181). {ECO:0000269|PubMed:17684058,
CC ECO:0000269|PubMed:25717181}.
CC -!- DOMAIN: Calponin-like repeats 1-3 are required for actin binding and
CC acting bundling activity. {ECO:0000269|PubMed:11096113}.
CC -!- DISRUPTION PHENOTYPE: Defects in the structure and function of body
CC wall muscle, resulting in variable paralysis (PubMed:7929573).
CC Disorganization of the A- and I-bands of the myofilament lattice and
CC accumulation of thin filaments in body wall muscles in adult animals
CC (PubMed:7929572). More densely aligned myosin filaments indicating
CC higher contractility of the actomyosin network (PubMed:25717181).
CC Excessive contraction of the myoepithelial sheath (PubMed:25717181).
CC {ECO:0000269|PubMed:25717181, ECO:0000269|PubMed:7929572,
CC ECO:0000269|PubMed:7929573}.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U04711; AAA81899.1; -; mRNA.
DR EMBL; U04711; AAA81900.1; ALT_INIT; mRNA.
DR EMBL; U04712; AAA81901.1; -; Genomic_DNA.
DR EMBL; U04712; AAA81902.1; -; Genomic_DNA.
DR EMBL; FO080807; CCD66936.1; -; Genomic_DNA.
DR EMBL; FO080807; CCD66937.1; -; Genomic_DNA.
DR EMBL; FO080807; CCD66938.1; -; Genomic_DNA.
DR PIR; B54800; B54800.
DR PIR; T33851; T33851.
DR RefSeq; NP_001021092.1; NM_001025921.3. [P37806-1]
DR RefSeq; NP_001021093.1; NM_001025922.2. [P37806-2]
DR AlphaFoldDB; P37806; -.
DR BioGRID; 37845; 9.
DR IntAct; P37806; 5.
DR MINT; P37806; -.
DR STRING; 6239.F08B6.4a.1; -.
DR iPTMnet; P37806; -.
DR EPD; P37806; -.
DR PaxDb; P37806; -.
DR PeptideAtlas; P37806; -.
DR EnsemblMetazoa; F08B6.4a.1; F08B6.4a.1; WBGene00006819. [P37806-1]
DR EnsemblMetazoa; F08B6.4b.1; F08B6.4b.1; WBGene00006819. [P37806-2]
DR GeneID; 172397; -.
DR KEGG; cel:CELE_F08B6.4; -.
DR UCSC; F08B6.4c.1; c. elegans. [P37806-1]
DR CTD; 172397; -.
DR WormBase; F08B6.4a; CE20658; WBGene00006819; unc-87. [P37806-1]
DR WormBase; F08B6.4b; CE27922; WBGene00006819; unc-87. [P37806-2]
DR eggNOG; ENOG502QR8I; Eukaryota.
DR InParanoid; P37806; -.
DR OMA; CRNTTYE; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; P37806; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; P37806; -.
DR PRO; PR:P37806; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006819; Expressed in larva and 4 other tissues.
DR GO; GO:0042642; C:actomyosin, myosin complex part; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0031674; C:I band; IDA:WormBase.
DR GO; GO:0001725; C:stress fiber; IDA:WormBase.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0140661; F:cytoskeletal motor inhibitor activity; IDA:WormBase.
DR GO; GO:0017022; F:myosin binding; IDA:WormBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:WormBase.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:WormBase.
DR GO; GO:0031034; P:myosin filament assembly; IDA:WormBase.
DR GO; GO:1904113; P:negative regulation of muscle filament sliding; IDA:WormBase.
DR InterPro; IPR000557; Calponin_repeat.
DR Pfam; PF00402; Calponin; 6.
DR PROSITE; PS01052; CALPONIN_1; 5.
DR PROSITE; PS51122; CALPONIN_2; 7.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Muscle protein;
KW Reference proteome; Repeat.
FT CHAIN 1..565
FT /note="Protein unc-87"
FT /id="PRO_0000204792"
FT REPEAT 237..262
FT /note="Calponin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 285..310
FT /note="Calponin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 338..363
FT /note="Calponin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 384..409
FT /note="Calponin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 431..456
FT /note="Calponin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 472..497
FT /note="Calponin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REPEAT 517..542
FT /note="Calponin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00474"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020109"
FT VAR_SEQ 1..10
FT /note="MLSFNNTTSA -> MPPTEDQVVA (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000757"
FT VAR_SEQ 11..201
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020110"
FT MUTAGEN 207
FT /note="A->V: In e1459; Disruption of myofilament
FT periodicity and thin filament accumulation at the end of
FT muscle cells."
FT /evidence="ECO:0000269|PubMed:17684058,
FT ECO:0000269|PubMed:7929572"
SQ SEQUENCE 565 AA; 62728 MW; B00CC87963F312B7 CRC64;
MLSFNNTTSA SSFQSASSRY LMSSSSSIGP PQQQSAKLFP EHFYPSGLSP RQSEALERLR
PNTASRERNI PIQFTGKNPT TNSALEEYKP VPHVQVTSPK SSIVPNFVSE QRGLQPQPTS
QAPTNYRQFV AAPRSPRGYG DYPEMTGKAS AAGDSEPVQI PIKTQTPITQ ARAQETKIPT
IVSPHPVYYY DNQEQPIQQI REEQPNATME TKVTGQGQPK RVGRWTLAQL RQTDGIIPSQ
AGWNKGDSQK LMTNFGTPRN TNTRVKSENL QEIPEDIANR THGEVRLQSG TNKYCSQRGM
TGFGSGRDVC REGVRVAQNP ADLAELPEEK IRMSEGIVRL QAGTNKYDSQ KGMTGFGTGR
RETTKMVDSK HPEYDHEKPD QSEIPLQSGT NKFASQKGMT GFGTARRETT KMVDSNHPDY
SHECSIDQTT IPSQMGSNQY ASQKGMTGFG QPRWEVLDPS ISWQNRKSQG MVRLQSGTNR
FASQAGMIGF GTCRNTTFEA EGGELPYEAM KVSETIIPSQ AGWNKGDSQK KMTSFGAPRD
VKGKHLKRIW ELEYPEEAEI SLDRL
