LIMC1_XENLA
ID LIMC1_XENLA Reviewed; 1083 AA.
AC Q3KQW7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=LIM and calponin homology domains-containing protein 1 {ECO:0000305};
GN Name=limch1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Actin stress fibers-associated protein that activates non-
CC muscle myosin IIa. Through the activation of non-muscle myosin IIa,
CC positively regulates actin stress fibers assembly and stabilizes focal
CC adhesions. It therefore negatively regulates cell spreading and cell
CC migration. {ECO:0000250|UniProtKB:Q9UPQ0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q9UPQ0}.
CC -!- SIMILARITY: Belongs to the LIMCH1 family. {ECO:0000305}.
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DR EMBL; BC106026; AAI06027.1; -; mRNA.
DR RefSeq; NP_001089675.1; NM_001096206.1.
DR AlphaFoldDB; Q3KQW7; -.
DR SMR; Q3KQW7; -.
DR BioGRID; 592517; 1.
DR PRIDE; Q3KQW7; -.
DR GeneID; 734736; -.
DR KEGG; xla:734736; -.
DR CTD; 734736; -.
DR Xenbase; XB-GENE-5950315; limch1.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 734736; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00889; CALPONIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..1083
FT /note="LIM and calponin homology domains-containing protein
FT 1"
FT /id="PRO_0000293621"
FT DOMAIN 21..138
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1011..1077
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..424
FT /evidence="ECO:0000255"
FT COILED 784..835
FT /evidence="ECO:0000255"
FT COMPBIAS 185..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 122183 MW; AFEA1AB27ED89A1C CRC64;
MASNAALQGE DIPQPQESPP DTACMEAQKW IEQVTGKSFG DRDFRTGLEN GILLCELLNA
IKPGLVKKIN RLPTPIAGLD NITLFLRGCK ELGLKESQLF DPGDLQDTAN RTTGRTSDCN
RKLRNVLVTV YWLGKAANGC SSFSGTNLDL KEFEGLLAQI RKENEEIESP KRSIRDSGYI
DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSQQTPSPDV VLRGSSDGRG SDSESDLPHR
RIPDVRKDDM SARRVSFGEN KAFVPFNQYL PNKNNQTAYI PAPLRKKKAE REDYRKSWST
ATSPLGGERP FRSMSMCDMR YEEEGSMLPH SRAHHEHLQH VNSLLKEEDD TWQDDLARWK
TRRRSASQDL IKKEEERKKM ERLMSGDSEL SDRRKSIKTY REIVEEKERR EKELHVAYKN
AKTRGEAERI LKSYIEKFTI SEAVLEGLVM PKILERSQSV EPSLLSSSED PNPLKYLRQQ
SLPSPKYTST VEATVTPSSP CESKSPTGLI SPSKNIISKT VPMLTAKPYS QPKNTQEVLK
TFKVDGKVNL NGVEEQKGKE SGSQTFAAPS LTRSQMFEGV ARVDAPVVET KQDVASIKLN
LARPNTLNSL HESNSLCEDR NHISQKDEPD SFVQEESVHS VEQLSEGNTQ SNSTTQAVPA
VSSIEIPPLT VNGKDTEDKR KVEAAELIMH WSLDSNYKEA KKNSLPPLKS SENVEESSKI
KENESSHKVQ LNITLQTRNA WRRSQFFLQS VDTECTEKSP ALVPNLSSPN RSCTWDPEEE
RKRQEKWQQE QERLLQERYQ KEQEKLKEEW EKAQKEVEEE ERKYYEEERK IIEDTVVPLT
LSPNSNVHFN ISERNGNFIP VLPDHAKRDQ ENNNGQLMAE PNRVIKNEIH MHSNVTQQQI
LYAHERSMLA AEETQIKGKT EKWEAEPCNH VQSNECNTPT RLTLQAGCKQ VMLSESCDLG
SPKTPVDENA VHHNMSSIIS TRGIDSKEET LNSSQSTSQC QSPNRSVSGK KLCSTCGLPL
GKGAAMIIET LSLYFHIQCF KCGLCKGQLG DATTGTDVRI RNGLLNCNDC YVKSRTAGHP
TPL
