ID A0A3Q1M2M8_BOVIN Unreviewed; 1542 AA.
AC A0A3Q1M2M8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=LIM and calponin homology domains 1 {ECO:0000313|Ensembl:ENSBTAP00000064061.1};
GN Name=LIMCH1 {ECO:0000313|Ensembl:ENSBTAP00000064061.1,
GN ECO:0000313|VGNC:VGNC:30887};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000064061.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000064061.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000064061.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000064061.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000064061.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR SMR; A0A3Q1M2M8; -.
DR STRING; 9913.ENSBTAP00000064061; -.
DR Ensembl; ENSBTAT00000081117.1; ENSBTAP00000064061.1; ENSBTAG00000010677.6.
DR VEuPathDB; HostDB:ENSBTAG00000010677; -.
DR VGNC; VGNC:30887; LIMCH1.
DR GeneTree; ENSGT00950000183159; -.
DR InParanoid; A0A3Q1M2M8; -.
DR OMA; YKRNQGQ; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000010677; Expressed in longissimus muscle and 100 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M2M8; baseline.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032034; F:myosin II head/neck binding; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IBA:GO_Central.
DR CDD; cd21278; CH_LIMCH1; 1.
DR CDD; cd08368; LIM; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15551:SF3; LIM AND CALPONIN HOMOLOGY DOMAINS-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR15551; LIM DOMAIN ONLY 7; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 2.
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; Calponin-homology domain, CH-domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 21..138
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1470..1536
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 185..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 827..898
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1267..1308
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 173047 MW; 503E2EAAB9BD4FFD CRC64;
MACPVLGLEA LQPLQPEPPP EPAFSEAQKW IEQVTGRSFG DKDFRTGLEN GILLCELLNA
IKPGLVKKIN RLPTPIAGLD NIILFLRGCK ELGLKESQLF DPSDLQDTSN RVAVKSLDYS
RKLKNVLVTI YWLGKAANSC ASYSGTTLNL KEFEGLLAQM RKETDDIESP KRSIRDSGYI
DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSRQTPSPDV VLRGSSDGRG SDSESDLPHR
KLPDVKKDDM SARRTSHGEP KSAVPFNQYL PNKSNQTAYV PAPLRKKKAE REEYRKSWST
ATSPLGGERP FSYPETIEEE EGEVGSHCEE DPVSQMDTSG KPPDGGSELP TSCGKEQPPP
EGAVVAPAPK SEEKAAAEMQ KRRRLEQAGI KVMPAAQRFA SQKQLNDEKE AVRNIILRKE
NPFLVHQHGR DSESEDEVAC RLPDLEKDDF AARRARMNQT KPVVPLNQLL YGPYRKKEAE
KSDGSKQHSK GISEKKTLEH KRNQGQTEEV KSRVTCIVRA QESEPAEAGL RKVPDLYKDD
LAQRRIQSRL GPHREAPSFI TVASITEADL ETWERLKVSE KTRDGDVEHT CAPEPSPEIK
AETAIRDDFA SRKARAYKKA SSSPRQKFVH FGPVTEIDQQ TWKRLSIGRA GPRADAEEGI
SHDSKTHTCA VSAASAATSS LKEDRMLNPQ NDCRTVTSDV DDCCKRVSQL APVPESQEER
SFSAGEGPRR TEEVTRKQQP QDRKEEPEGV AQRDSEMAPK AERSEEGGQP LYGPRTPVSD
DAESTSMFDM RCEEEAAVQP HSRARQEQLQ LINSQLREED DKWQDDLARW KSRRRSASQD
LIRKEEERKK MEKLLAGEDG TRERRKSIKT YREIVQEKER RERELHEAYK NARTQEEAEG
ILQQYIERFT ISEAVLERLE MPKILERSHS TEPNLSPFLS DPNPMKYLRQ QSLPPPKFTA
TVETTIARPS VLDASMSAGS GSPSKTVSPK AVPMLTPKPY SQPKNSQEVL KTFKVDGKVT
MNGETTHGDE EEKERECPTV ALAPSLTKSQ MFEGEARVHG SPVELKQDSN SIEINIKKPS
SLPQELTATT EETEANSRED ENDGEEAEKG NTEVAPSEPQ LFTTTVTRSS PTVAFVELSP
SPQLKNEVPE EKEQKKPENE MSGKVELVLS QKVVKPKSPE PEATLTFPFL DKMPETNQSP
LPNLNSQESP GTASIPLRVQ NSWRRSQFFS QSVDSPSSEK SPVTTPQFKF WAWDPEEERR
RQEKWQQEQE RLLQERYQKE QDKLKEEWEK AQKEVEEEER RYYEEERKII EDTVVPFTVS
SSSADQLSTS SSVTEGSGTV NKMDLENCCE EEQETRQKRP LQEDNSDSLL KTREGDPLEE
KGSSLTQEVL THSENPASEG IYHQLDTEAG APQCGVNPQL AQDPSQNQQV SNPPMHILED
VKPKTLPLDK SINHQIESPS ERRKSISGKK LCSSCGLPLG KGAAMIIETL NLYFHIQCFK
CGICKGQLGD AVSGTDVRIR NGLLNCNDCY MRSRSAGQPT TL
//
