ID A0A0L0BX30_LUCCU Unreviewed; 1159 AA.
AC A0A0L0BX30;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
DE Flags: Fragment;
GN ORFNames=FF38_09627 {ECO:0000313|EMBL:KNC24608.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24608.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC24608.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC24608.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC24608.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC24608.1}.
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DR EMBL; JRES01001205; KNC24608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BX30; -.
DR STRING; 7375.A0A0L0BX30; -.
DR EnsemblMetazoa; KNC24608; KNC24608; FF38_09627.
DR OMA; PSEQEYQ; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR CDD; cd21241; CH_SYNE1_rpt1; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR047290; CH_SYNE1_rpt1.
DR PANTHER; PTHR47535:SF1; MUSCLE-SPECIFIC PROTEIN 300 KDA; 1.
DR PANTHER; PTHR47535; MUSCLE-SPECIFIC PROTEIN 300 KDA, ISOFORM G; 1.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1130..1149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1036..1143
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KNC24608.1"
SQ SEQUENCE 1159 AA; 128462 MW; 2F14C0BC7140C6F2 CRC64;
AKMSGQQPPP NGPRGWNPRV ASPSTFMYRP PSPWTPVAPS PPPIISGPRR PSMPSPAPMS
PTPFAHAMSP GPSNLRGTRG TNNMPHPRPQ WPQQAPLAGN MSPAPYQPPT FQPSFYPNQQ
PTLTQLPPKV CPSPTAYVGA NGPRPFRPLT HQNSYGGDPT SSFQLSPTPS PIVCQTPNSE
FMYGSNRQTP MSHAYETQQQ QYPRQQQQQH YAPPPPLIPS MQQRPQSQNQ YDFVGVPLEP
PQPKSYVIYD DEEEYGPSTA EIIANQSQDY VDEKLAEYQM TILQLQGNTN SRIKLFEQQK
QKTTMDKTTD ERHEEDPPPS TMGVGEAQRP IPAVRKRRLG QTAVETSSTA DDTQTYVSQG
QMQQDFDNIE EASNAGLVYE DSMQETSSTI SRTITKTIKT TTSSSHEYLM EGFDTLGRPK
TPNTPLRLKQ KVAIYEKAWH SGEAGGIKRS AEHMSQESIR SSTDATDIDI NIDSDNPFDI
DVYEIEKRLR EERKRGLAEA EAAKLAFQQI QLRATPLSPA RKVEIHEEHT ASPFNVTLKT
TSKISPGAVT GRIELEEHSP KSPFNVTLRT TQRYRRNPNT PEELTQASPF NVTLRTTKRH
SSSPNAAAVD GKLASARFLE GEKTVREVIS ADGVKTIVTS SMTSDGRKHE EKIFRHGEGY
FSPRVSPQRE MRATTPSRSV DMTAGGRRIL IKLENEQEQM DMYSTDESYD ITDYKVTSER
HFKTTTSAGG ETVTLETPPN IDIIVGTTSN HPKRRTVSLE TKHEQMPWQT QQHYTSNSTA
SSSSSTAAFT TKTTTKITTT SARQQRESLE SDETSVKNIS ISKTIQSQGS TSPEESHRFV
TKQTITGLPS SPTSASVSTR IGKTVTKTTA THKLTKQETE TSPLPEHDAL KKRLEIVGYG
RDGLGHGTGE LGYKTDNKLR EPQSDDSDTE GATVSSIVIV PTGSSVTPAS ASVASSTISP
TKAGGIVSAS SHTNTGTLHK SLTPTQTQQH QSTTTTSQTS ANEYQEIQST MAAIQFARSN
SQYDTHIKEK REEQERVQKK TFTNWINSYL LKRVPPLRVD DLINDLRDGT KLIALLEVLS
GEKLPVERGR VLRRPHFLSN ANTALQFLAS KRIKLVNINP ADLVDGRPPV VLGLIWTIIL
YFQVIIIIIT THTYNYIIY
//
