ASAP_DROME
ID ASAP_DROME Reviewed; 1155 AA.
AC A1Z7A6; E1JH06; Q6AWJ6; Q95R80;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein {ECO:0000305};
GN Name=Asap {ECO:0000312|FlyBase:FBgn0050372};
GN Synonyms=Asap1 {ECO:0000312|FlyBase:FBgn0050372};
GN ORFNames=CG30372 {ECO:0000312|FlyBase:FBgn0050372};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|EMBL:AAT94481.1, ECO:0000312|EMBL:ABX00789.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 193-1127 (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAT94481.1, ECO:0000312|EMBL:ABX00789.1};
RC TISSUE=Larva {ECO:0000312|EMBL:AAT94481.1, ECO:0000312|EMBL:ABX00789.1},
RC and Pupae {ECO:0000312|EMBL:AAT94481.1, ECO:0000312|EMBL:ABX00789.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Wan K., Kapadia B., Park S., Yu C., Rubin G.M., Celniker S.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAL29125.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1155 (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL29125.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL29125.1};
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 [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CINDR, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21976699; DOI=10.1091/mbc.e11-04-0305;
RA Johnson R.I., Sedgwick A., D'Souza-Schorey C., Cagan R.L.;
RT "Role for a Cindr-Arf6 axis in patterning emerging epithelia.";
RL Mol. Biol. Cell 22:4513-4526(2011).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27535433; DOI=10.1091/mbc.e16-05-0272;
RA Rodrigues F.F., Shao W., Harris T.J.;
RT "The Arf GAP Asap promotes Arf1 function at the Golgi for cleavage furrow
RT biosynthesis in Drosophila.";
RL Mol. Biol. Cell 27:3143-3155(2016).
CC -!- FUNCTION: Probable GTPase-activating protein (GAP) for Arf family
CC proteins (Probable). Involved in Golgi apparatus organization by
CC targeting Arf1 to the Golgi, which may be important for membrane
CC trafficking during epithelial morphogenesis (PubMed:27535433).
CC Regulates the positioning of interommatidial precursor cells during
CC compound eye morphogenesis together with Arf6 and Cindr
CC (PubMed:21976699). Required for cleavage furrow ingression in early
CC embryonic cells (PubMed:27535433). {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:27535433, ECO:0000305}.
CC -!- SUBUNIT: Interacts with Cindr. {ECO:0000269|PubMed:21976699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:27535433}. Nucleus {ECO:0000269|PubMed:27535433}.
CC Cell membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. Cell
CC projection, microvillus {ECO:0000269|PubMed:27535433}. Note=Detected in
CC large puncta at the plasma membrane (PubMed:21976699, PubMed:27535433).
CC Excluded from the nucleus at interphase (PubMed:27535433). Enriched in
CC the nucleus at prometaphase (PubMed:27535433).
CC {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0050372};
CC IsoId=A1Z7A6-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0050372};
CC IsoId=A1Z7A6-2; Sequence=VSP_058985;
CC -!- DEVELOPMENTAL STAGE: Expressed in the ectoderm of embryos (at protein
CC level). {ECO:0000269|PubMed:27535433}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC compound eye morphogenesis (PubMed:21976699). Maternal RNAi-mediated
CC knockdown results in partial female infertility and, in early embryos,
CC abnormal aggregation of Golgi apparatus and disrupted cleavage furrow
CC ingression (PubMed:27535433). {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:27535433}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL29125.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF59133.4; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94364.1; -; Genomic_DNA.
DR EMBL; BT015252; AAT94481.1; -; mRNA.
DR EMBL; BT031167; ABX00789.1; -; mRNA.
DR EMBL; AY061577; AAL29125.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014504.1; NM_001014504.3. [A1Z7A6-1]
DR RefSeq; NP_001163085.1; NM_001169614.2. [A1Z7A6-2]
DR AlphaFoldDB; A1Z7A6; -.
DR SMR; A1Z7A6; -.
DR IntAct; A1Z7A6; 4.
DR STRING; 7227.FBpp0099488; -.
DR PaxDb; A1Z7A6; -.
DR PRIDE; A1Z7A6; -.
DR EnsemblMetazoa; FBtr0100140; FBpp0099488; FBgn0050372. [A1Z7A6-1]
DR EnsemblMetazoa; FBtr0300954; FBpp0290176; FBgn0050372. [A1Z7A6-2]
DR GeneID; 35783; -.
DR KEGG; dme:Dmel_CG30372; -.
DR UCSC; CG30372-RB; d. melanogaster. [A1Z7A6-1]
DR CTD; 35783; -.
DR FlyBase; FBgn0050372; Asap.
DR VEuPathDB; VectorBase:FBgn0050372; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000171062; -.
DR InParanoid; A1Z7A6; -.
DR OMA; MKMECHI; -.
DR PhylomeDB; A1Z7A6; -.
DR Reactome; R-DME-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; A1Z7A6; -.
DR BioGRID-ORCS; 35783; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Trim9; fly.
DR GenomeRNAi; 35783; -.
DR PRO; PR:A1Z7A6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0050372; Expressed in wing disc and 23 other tissues.
DR ExpressionAtlas; A1Z7A6; baseline and differential.
DR Genevisible; E1JH06; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISM:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:UniProtKB.
DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:1903829; P:positive regulation of protein localization; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISM:FlyBase.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11821; SH3_ASAP; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR043593; ASAP.
DR InterPro; IPR035836; ASAP1-like_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037844; PH_ASAP.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45854; PTHR45854; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Cell projection;
KW Cytoplasm; Developmental protein; GTPase activation; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Repeat; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..1155
FT /note="ArfGAP with SH3 domain, ANK repeat and PH domain-
FT containing protein"
FT /id="PRO_0000440690"
FT DOMAIN 310..404
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 427..547
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 585..617
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 631..660
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1091..1155
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 442..466
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 700..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 724..751
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_058985"
SQ SEQUENCE 1155 AA; 127271 MW; FC4C4832E2C0AFE8 CRC64;
MPPSLIAVSE FVEETRSDYS SPTTSTFASR MPDCRHTIGV LEERLEFDRE GLTKLKKAVK
AIHNSGNTHV DNEMFMVRAL ERLGGKVIEQ DEPDIGAAFL KFSVVTKELS ALMKTLMQNI
NNIVMFPVDS MLKSELRGVK GDMKRPFDKA AKDYEAKFIK IEKEKKAQAK EAGMVRTEID
AAVVAEEMEK ERRLYQLQTC EYLLKYKDIK TKTGIELLQH LIEYYHALSN YFKDGLQTIE
HFGTYIGDLS EKLHEIKQKQ DEDRRSLLDL RTVLRSTPDF ERVDNVPSSE SRSGGAGYSL
HQLQGDKHHG VTRQGHLLKK SEGKVRRVWQ KRRCRVTSDG FLDIFHADES KPPTRVNLLT
CQIKPVPDDK RGFDLISYNR PYHFQAEDEG DQKAWMAVLV NCKEKALTKA FQHANPQMSP
SLVELQKTVI RYVQLLPGND RCCDCGSRND VTWISLNFGI LVCIQCSGVH RDLGVHHSRI
QSLTLDNLTT ANLLIARAMG NSTLNDIMEA KLGRGKLQHE SSMEERYDFI RAKYVAKRYV
MRTCSDDNDL RCDLEQAVVN ADMSQLLQVW AEGADLTCCL PSSDAGETAL HLAVLREMGS
TLHIVDFLIQ NMPPKGLNKA TNPAGLLDVT GKNTALHLCA LHDRRECMKL LLRSGADYEL
KNSQNKTALD IAKEMGHNSC RELIECAIKR EKSAFDHINT DWNLPNEDGS TDFSDDETVI
DERKSRSRPP SFAGGDSPVL RSRSSTCDSI QSSSSPIANC PSRQFTLPSG LPSYTHSAGT
SPKQHISVGQ YLGSATNVGG NGPGNGGSSP SSASSQSVRA ARNSLNMQSD LGGHVTGARK
STSTANMNSL KKRTAPAPPP GTLGSASSSS FYGTLPHPPR HSQNFDASDI RAINHKNQSL
DVAYGTLPHL RSVESSPRGG GGYGYGVSQD PGGSGNGSNN SLMPAMTTFG HKRSPSGESL
NRNIHLAGAK LVLPPTGELP TLKHVDKSAL TRPKIPPPGP PSEREISNGQ SNESISSMDE
GPVAPPRKLV NQSANFPDYE SWHTDMDSSG GGLDHSAESN VSSSDNDRLN SSPDNPSKTG
GAGLGGKFHY NGQRRCRALY DCVADNDDEL EFKEGEILIV LNERTDDENW MEGIIEGQPT
RKGMFPVSFV HMLPD
