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CD2 antigen cytoplasmic tail-binding protein 2 homolog (Protein hole-in-one)

 CD2B2_DROME             Reviewed;         319 AA.
Q9VKV5; C4XVH8; Q8T0Q7;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 98.
RecName: Full=CD2 antigen cytoplasmic tail-binding protein 2 homolog;
AltName: Full=Protein hole-in-one;
Name=holn1; ORFNames=CG5198;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-30; TYR-37 AND
SER-41, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19884309; DOI=10.1534/genetics.109.110288;
Campos I., Geiger J.A., Santos A.C., Carlos V., Jacinto A.;
"Genetic screen in Drosophila melanogaster uncovers a novel set of
genes required for embryonic epithelial repair.";
Genetics 184:129-140(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=22140578; DOI=10.1371/journal.pone.0028349;
Geiger J.A., Carvalho L., Campos I., Santos A.C., Jacinto A.;
"Hole-in-one mutant phenotypes link EGFR/ERK signaling to epithelial
tissue repair in Drosophila.";
PLoS ONE 6:E28349-E28349(2011).
-!- FUNCTION: Required for embryonic epithelial tissue repair, but not
for the assembly of the actomyosin cable at the wound edge.
Probably acts downstream of rl in the regulation of Ddc and msn
transcription to promote wound healing.
{ECO:0000269|PubMed:19884309, ECO:0000269|PubMed:22140578}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22140578}.
-!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically.
Expression is ubiquitous throughout embryonic development.
{ECO:0000269|PubMed:22140578}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal. Embryonic wound healing
defects. The few adult escapers show subtle rough eye phenotype
and extra and/or misplaced or missing macrochaetae on the
scutellum. {ECO:0000269|PubMed:19884309,
ECO:0000269|PubMed:22140578}.
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EMBL; AE014134; AAF52953.1; -; Genomic_DNA.
EMBL; AY069127; AAL39272.1; -; mRNA.
EMBL; BT088782; ACS12715.1; -; mRNA.
RefSeq; NP_609404.2; NM_135560.3.
UniGene; Dm.391; -.
ProteinModelPortal; Q9VKV5; -.
SMR; Q9VKV5; -.
BioGrid; 60513; 3.
STRING; 7227.FBpp0079616; -.
iPTMnet; Q9VKV5; -.
PaxDb; Q9VKV5; -.
PRIDE; Q9VKV5; -.
EnsemblMetazoa; FBtr0080026; FBpp0079616; FBgn0032250.
GeneID; 34432; -.
KEGG; dme:Dmel_CG5198; -.
UCSC; CG5198-RA; d. melanogaster.
CTD; 34432; -.
FlyBase; FBgn0032250; holn1.
eggNOG; KOG2950; Eukaryota.
eggNOG; ENOG4111KF5; LUCA.
GeneTree; ENSGT00390000012483; -.
InParanoid; Q9VKV5; -.
KO; K13099; -.
OMA; TGNMDIY; -.
OrthoDB; EOG091G0MVR; -.
PhylomeDB; Q9VKV5; -.
Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
GenomeRNAi; 34432; -.
PRO; PR:Q9VKV5; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0032250; -.
Genevisible; Q9VKV5; DM.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005682; C:U5 snRNP; ISS:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
GO; GO:0035220; P:wing disc development; IMP:FlyBase.
GO; GO:0042060; P:wound healing; IMP:FlyBase.
CDD; cd00072; GYF; 1.
Gene3D; 3.30.1490.40; -; 1.
InterPro; IPR003169; GYF.
InterPro; IPR035445; GYF-like_domain.
Pfam; PF02213; GYF; 1.
SMART; SM00444; GYF; 1.
SUPFAM; SSF55277; SSF55277; 1.
PROSITE; PS50829; GYF; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 319 CD2 antigen cytoplasmic tail-binding
protein 2 homolog.
/FTId=PRO_0000195039.
DOMAIN 260 316 GYF. {ECO:0000255|PROSITE-
ProRule:PRU00101}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 37 37 Phosphotyrosine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 64 64 M -> I (in Ref. 3; AAL39272).
{ECO:0000305}.
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


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