ID CD2B2_DROME Reviewed; 319 AA.
AC Q9VKV5; C4XVH8; Q8T0Q7;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=CD2 antigen cytoplasmic tail-binding protein 2 homolog;
DE AltName: Full=Protein hole-in-one;
GN Name=holn1; ORFNames=CG5198;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-30; TYR-37 AND
RP SER-41, 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19884309; DOI=10.1534/genetics.109.110288;
RA Campos I., Geiger J.A., Santos A.C., Carlos V., Jacinto A.;
RT "Genetic screen in Drosophila melanogaster uncovers a novel set of genes
RT required for embryonic epithelial repair.";
RL Genetics 184:129-140(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22140578; DOI=10.1371/journal.pone.0028349;
RA Geiger J.A., Carvalho L., Campos I., Santos A.C., Jacinto A.;
RT "Hole-in-one mutant phenotypes link EGFR/ERK signaling to epithelial tissue
RT repair in Drosophila.";
RL PLoS ONE 6:E28349-E28349(2011).
CC -!- FUNCTION: Required for embryonic epithelial tissue repair, but not for
CC the assembly of the actomyosin cable at the wound edge. Probably acts
CC downstream of rl in the regulation of Ddc and msn transcription to
CC promote wound healing. {ECO:0000269|PubMed:19884309,
CC ECO:0000269|PubMed:22140578}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22140578}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Expression
CC is ubiquitous throughout embryonic development.
CC {ECO:0000269|PubMed:22140578}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Embryonic wound healing
CC defects. The few adult escapers show subtle rough eye phenotype and
CC extra and/or misplaced or missing macrochaetae on the scutellum.
CC {ECO:0000269|PubMed:19884309, ECO:0000269|PubMed:22140578}.
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DR EMBL; AE014134; AAF52953.1; -; Genomic_DNA.
DR EMBL; AY069127; AAL39272.1; -; mRNA.
DR EMBL; BT088782; ACS12715.1; -; mRNA.
DR RefSeq; NP_609404.2; NM_135560.3.
DR AlphaFoldDB; Q9VKV5; -.
DR SMR; Q9VKV5; -.
DR BioGRID; 60513; 6.
DR STRING; 7227.FBpp0079616; -.
DR iPTMnet; Q9VKV5; -.
DR PaxDb; 7227-FBpp0079616; -.
DR DNASU; 34432; -.
DR EnsemblMetazoa; FBtr0080026; FBpp0079616; FBgn0032250.
DR GeneID; 34432; -.
DR KEGG; dme:Dmel_CG5198; -.
DR UCSC; CG5198-RA; d. melanogaster.
DR AGR; FB:FBgn0032250; -.
DR CTD; 34432; -.
DR FlyBase; FBgn0032250; holn1.
DR VEuPathDB; VectorBase:FBgn0032250; -.
DR eggNOG; KOG2950; Eukaryota.
DR GeneTree; ENSGT00390000012483; -.
DR HOGENOM; CLU_062973_0_0_1; -.
DR InParanoid; Q9VKV5; -.
DR OMA; VRKCGEN; -.
DR OrthoDB; 2877705at2759; -.
DR PhylomeDB; Q9VKV5; -.
DR BioGRID-ORCS; 34432; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34432; -.
DR PRO; PR:Q9VKV5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032250; Expressed in egg cell and 24 other cell types or tissues.
DR Genevisible; Q9VKV5; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005682; C:U5 snRNP; ISS:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR039905; CD2BP2/Lin1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR PANTHER; PTHR13138:SF3; CD2 ANTIGEN CYTOPLASMIC TAIL-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR13138; PROTEIN LIN1; 1.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; GYF domain; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..319
FT /note="CD2 antigen cytoplasmic tail-binding protein 2
FT homolog"
FT /id="PRO_0000195039"
FT DOMAIN 260..316
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 64
FT /note="M -> I (in Ref. 3; AAL39272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36838 MW; D8009EB241F9C378 CRC64;
MASKRKHQAS QKVKEESFKK HTLDSDEEDS DDYEREYLND SDIEGGEEGV AKVEDDVKVT
PFNMKEELEE GHFDKDGHYH WNKETEAKDN WLDNIDWVKI GTQKNAFDPA KDEENSSDEE
KNEPVGKAFN LSMNLMKMVE FMKPGETVKM TLQRLGKQRP VLTTLQRIKQ KKAGIVDPKT
QEISQLTELA NEILSKTGNM DIYQDTYESI KAKIADLPGT SKPKVADDID MYADDFETKE
LERSKTSSSD SSKPTTTTSE VTWEFKWSQD ETDIQGPFST EKMLKWSQEN YFKNGVYVRK
CGENTNFYTS NRIDFDLYL
//
