GenomeNet

Database: UniProt
Entry: A0A182VJG0_ANOME
LinkDB: A0A182VJG0_ANOME
Original site: A0A182VJG0_ANOME 
ID   A0A182VJG0_ANOME        Unreviewed;       837 AA.
AC   A0A182VJG0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   RecName: Full=Actin-binding lim zn-finger protein limatin involved in axon guidance {ECO:0008006|Google:ProtNLM};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM016003-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM016003-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM016003-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   AlphaFoldDB; A0A182VJG0; -.
DR   STRING; 30066.A0A182VJG0; -.
DR   EnsemblMetazoa; AMEM016003-RA; AMEM016003-PA; AMEM016003.
DR   VEuPathDB; VectorBase:AMEM016003; -.
DR   VEuPathDB; VectorBase:AMEM21_012423; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   CDD; cd09327; LIM1_abLIM; 1.
DR   CDD; cd09328; LIM2_abLIM; 1.
DR   CDD; cd09329; LIM3_abLIM; 1.
DR   CDD; cd09330; LIM4_abLIM; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24213; ACTIN-BINDING LIM PROTEIN; 1.
DR   PANTHER; PTHR24213:SF9; UNCOORDINATED 115A, ISOFORM B-RELATED; 1.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          4..63
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          64..123
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          207..266
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          772..837
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          159..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..569
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  93191 MW;  131653EC1E1C3CA9 CRC64;
     KSKIQCSKCQ KKCSGEVLRV SDRYFHKTCF QCTKCNKSLA TGGFFSKDGA YYCTLDYQKL
     YGTKCAACSQ YVEGEVVSTM GNTYHQKCFT CSKCKQPFKS GSKVTNTGKE VLCESCVKCP
     PGSGVGGGGG ATATGSPTVG AAAGVVQGTG SATVSPKSRA IEQKQEQRTI KEITSSPTKA
     ATLQHHQETV KKQQQLLQNG GKQPDPNDCA GCQQQLKEGQ ALIALDRQWH IWCFKCNACG
     TTLNGEYMGK DGVPYCEKDF QKSFGVKCAH CNRYISGKVL QAGDNHHFHP TCARCTKCGD
     PFGDGEEMYL QGGAIWHPRC GPGPSSEAGI LNGVDTNGFN TETEFDRTST SGMSEIQVSE
     EEGEEGTRGD EMCFLCYHRT TSPGLILREY KNQGYEDIAR IYTYSYLTEE PGYLRRPIEP
     YDRAPVSPHF HRPVQHYSSM GGGTASSIGT RSASGSRSHS RSRSAMKVLV DSIRSETPRP
     KSPGMNNEEP IELSHYPAAK KPPPGEKPKI ERDDFPAPPY PYTDPERRRR YSDSYKGVPE
     SDDEVDHANN KENVTEKRHT KEEEELRKLK SSGMGTVILK DLQEKKRYEH WKQENLDPRN
     ASRTPSASKE PMYRMRYESP VGASPSRNLD HQKPFYEDEF DRSTSYRGSV GRAIGNATSY
     NGKQNGRGTA IHSYRSPPKP GYGFKTSTLP PSLRNGYSSD FSFSGLGDKT HSTEFSCGKS
     DISGDSITEG DRRALGAELP ASSTYSGALS YHYPQQPTRR SLPNMAHSML VHEPAKIYPY
     HLLLITNYRL PSDVDRCNLE RHLSDVEFEA ILQCTRPEFY RMPQWKRNDM KRRARLF
//
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