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 29-MAY-2024, entry version 165. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7227-FBpp0289359; -. 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 AGR; FB:FBgn0259745; -. 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; DDKNMPI; -. DR OrthoDB; 2901369at2759; -. DR PhylomeDB; Q9V4M2; -. DR Reactome; R-DME-6798695; Neutrophil degranulation. 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 cell types or tissues. DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:FlyBase. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter. 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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter. DR GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter. DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IPI:FlyBase. DR CDD; cd19757; Bbox1; 1. DR CDD; cd19794; Bbox2_TRIM66-like; 1. DR CDD; cd14954; NHL_TRIM71_like; 1. DR Gene3D; 4.10.830.40; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR001258; NHL_repeat. DR InterPro; IPR000315; Znf_B-box. DR PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1. DR PANTHER; PTHR24104:SF40; NHL DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01436; NHL; 5. DR Pfam; PF00643; zf-B_box; 2. DR SMART; SM00336; BBOX; 2. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF101898; NHL repeat; 1. 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 //