WECH_DROME
ID WECH_DROME Reviewed; 832 AA.
AC Q9V4M2; A4IJ45; B7YZS8; Q0E9G5; Q95SY8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein wech;
DE AltName: Full=Protein dappled;
GN Name=wech; Synonyms=dpld; ORFNames=CG42396;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8725239; DOI=10.1093/genetics/143.2.929;
RA Rodriguez A., Zhou Z., Tang M.L., Meller S., Chen J., Bellen H.,
RA Kimbrell D.A.;
RT "Identification of immune system and response genes, and novel mutations
RT causing melanotic tumor formation in Drosophila melanogaster.";
RL Genetics 143:929-940(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-470; SER-475 AND
RP SER-506, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18327251; DOI=10.1038/ncb1704;
RA Loeer B., Bauer R., Bornheim R., Grell J., Kremmer E., Kolanus W., Hoch M.;
RT "The NHL-domain protein Wech is crucial for the integrin-cytoskeleton
RT link.";
RL Nat. Cell Biol. 10:422-428(2008).
CC -!- FUNCTION: Vital for larval development. Plays a role in tumor
CC formation. A crucial component for the physical link between integrins
CC and the cytoskeleton in the epidermal muscle attachment sites.
CC {ECO:0000269|PubMed:18327251, ECO:0000269|PubMed:8725239}.
CC -!- SUBUNIT: Interacts with the head domain of rhea and the kinase domain
CC of Ilk.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in all epithelial cells
CC during early stages of embryogenesis. Specifically expressed at
CC epidermal muscle attachment site. {ECO:0000269|PubMed:18327251,
CC ECO:0000269|PubMed:8725239}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:18327251}.
CC -!- DISRUPTION PHENOTYPE: Muscle detachment in late-stage-16/early-stage-17
CC embryos. {ECO:0000269|PubMed:18327251}.
CC -!- MISCELLANEOUS: 'Wech' means 'detached' or 'gone' in German.
CC -!- CAUTION: Was originally termed dappled. {ECO:0000305|PubMed:8725239}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25460.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF59246.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68901.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83068.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83069.1; -; Genomic_DNA.
DR EMBL; AY060421; AAL25460.1; ALT_FRAME; mRNA.
DR EMBL; BT010087; AAQ22556.1; -; mRNA.
DR EMBL; BT030403; ABO52822.1; -; mRNA.
DR RefSeq; NP_001137614.1; NM_001144142.3.
DR RefSeq; NP_001137615.1; NM_001144143.2.
DR RefSeq; NP_524772.2; NM_080033.4.
DR RefSeq; NP_724567.1; NM_165533.3.
DR RefSeq; NP_724568.1; NM_165534.3.
DR AlphaFoldDB; Q9V4M2; -.
DR SMR; Q9V4M2; -.
DR BioGRID; 69183; 11.
DR DIP; DIP-21516N; -.
DR IntAct; Q9V4M2; 2.
DR STRING; 7227.FBpp0289359; -.
DR iPTMnet; Q9V4M2; -.
DR PaxDb; Q9V4M2; -.
DR PRIDE; Q9V4M2; -.
DR DNASU; 44653; -.
DR EnsemblMetazoa; FBtr0300080; FBpp0289357; FBgn0259745.
DR EnsemblMetazoa; FBtr0300081; FBpp0289358; FBgn0259745.
DR EnsemblMetazoa; FBtr0300082; FBpp0289359; FBgn0259745.
DR EnsemblMetazoa; FBtr0300083; FBpp0289360; FBgn0259745.
DR EnsemblMetazoa; FBtr0300084; FBpp0289361; FBgn0259745.
DR GeneID; 44653; -.
DR KEGG; dme:Dmel_CG42396; -.
DR CTD; 44653; -.
DR FlyBase; FBgn0259745; wech.
DR VEuPathDB; VectorBase:FBgn0259745; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000164246; -.
DR HOGENOM; CLU_008645_4_0_1; -.
DR InParanoid; Q9V4M2; -.
DR OMA; LECNEFM; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q9V4M2; -.
DR BioGRID-ORCS; 44653; 0 hits in 1 CRISPR screen.
DR ChiTaRS; wech; fly.
DR GenomeRNAi; 44653; -.
DR PRO; PR:Q9V4M2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0259745; Expressed in cleaving embryo and 60 other tissues.
DR Genevisible; Q9V4M2; DM.
DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:FlyBase.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0002168; P:instar larval development; IMP:UniProtKB.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IPI:FlyBase.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF01436; NHL; 5.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Metal-binding; Myogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..832
FT /note="Protein wech"
FT /id="PRO_0000220369"
FT REPEAT 537..580
FT /note="NHL 1"
FT REPEAT 584..627
FT /note="NHL 2"
FT REPEAT 631..674
FT /note="NHL 3"
FT REPEAT 680..722
FT /note="NHL 4"
FT REPEAT 727..770
FT /note="NHL 5"
FT ZN_FING 118..163
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 184..224
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 832 AA; 90573 MW; A5672AFC3FDE1FE1 CRC64;
MMELLSNNSV PQQMASSNAP SANNVAHSST ANGSGGGSVS SNASNSSERL LAGILESFPA
WDLNVGLLPN VGQSSPPRAD FFINNFLGGL DTHGDFSIGP IGSGARSNPK MSPESSNNSS
ISCGWCEVSA SIRCLECNEF MCNDCLREHR NSPLSSNHSI VSLPTPIGAS PTGGSSVNAQ
TPPSGNFICD IHNEMLRYVC DYCRKLVCQC CTLHEHKEHS YASIQSFMVG SKEKLEGAIE
SSQVGTRCIK SSIDKALAFI RLIERNCSEL SDNIRKAFRQ FIIAIEDRER FLLDFVEKLR
QRRLAILHDQ MAGLKSALAG LSETSDMLSK VADNACNMDQ IEIAMKLTNG QRQMEQFAGI
YKDLQPKQEV FAFAPPDYSL LQDIRNQGGV ILVDDKNLPI VSSSNGIVPS VSSVNAVAAA
SVGVVGGVAG VVGGVGVSNG LDLAFGMNMP NNPLSVASSS VRRPLLRDNS FRIPSPIMQP
RGGSACGMSS GMSSAALDWE LNGLRSSPGL HFSAPRTTQA IPGCMDLVKV RNSNALSLSF
ATEGHEDGQV SRPWGLCVDK MGHVLVSDRR NNRVQVFNPD GSLKFKFGRK GVGNGEFDLP
AGICVDVDNR IIVVDKDNHR VQIFTASGVF LLKFGSYGKE YGQFQYPWDV AVNSRRQIVV
TDSRNHRIQQ FDSEGRFIRQ IVFDNHGQTK GIASPRGVCY TPTGNIIVSD FDNHCLYLID
PDINDILSVK GHEGSGFHEF NRPSGLCCDD EGRIIVADSK NQRILVFNQN LDFMWDIEVR
PSINPLMPPT LDEKDRTCDV AIMPDGRIVF LIELSPDSKE GSNPYKRFVH VF
