ASAP1_RAT
ID ASAP1_RAT Reviewed; 1144 AA.
AC Q1AAU6; Q1AAU4; Q1AAU5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein;
DE AltName: Full=ADP-ribosylation factor-directed GTPase-activating protein 1;
DE Short=ARF GTPase-activating protein 1;
DE AltName: Full=Development and differentiation-enhancing factor 1;
DE Short=DEF-1;
DE Short=Differentiation-enhancing factor 1;
DE AltName: Full=PIP2-dependent ARF1 GAP;
GN Name=Asap1; Synonyms=Ddef1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=Sprague-Dawley;
RA Mueller T., Rothley M., Bauer M., Pankraz M., Sleeman J.;
RT "Enhanced ASAP1 expression is associated with tumor development and
RT progression, and promotes metastasis in experimental tumors.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729; SER-738; SER-851;
RP SER-1042; SER-1056 AND SER-1143, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Possesses phosphatidylinositol 4,5-bisphosphate-dependent
CC GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1)
CC and ARF5 and a lesser activity towards ARF6. May coordinate membrane
CC trafficking with cell growth or actin cytoskeleton remodeling by
CC binding to both SRC and PIP2. May function as a signal transduction
CC protein involved in the differentiation of fibroblasts into adipocytes
CC and possibly other cell types. Plays a role in ciliogenesis (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Activity stimulated by phosphatidylinositol 4,5-
CC bisphosphate (PIP2). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC RAB11FIP3. Interacts with PTK2B/PYK2. Interacts with CTTN. Interacts
CC (via SH3 domain) with APC (By similarity). Interacts with REPS2; the
CC interaction is direct (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ULH1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Predominantly
CC cytoplasmic. Partially membrane-associated (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Variant a;
CC IsoId=Q1AAU6-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant b;
CC IsoId=Q1AAU6-2; Sequence=VSP_021851;
CC Name=3; Synonyms=Variant c;
CC IsoId=Q1AAU6-3; Sequence=VSP_021850, VSP_021851;
CC -!- DOMAIN: The PH domain most probably contributes to the
CC phosphoinositide-dependent regulation of ADP ribosylation factors.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000250}.
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DR EMBL; DQ238622; ABB71896.1; -; mRNA.
DR EMBL; DQ238623; ABB71897.1; -; mRNA.
DR EMBL; DQ238624; ABB71898.1; -; mRNA.
DR RefSeq; NP_001037710.1; NM_001044245.1.
DR AlphaFoldDB; Q1AAU6; -.
DR BMRB; Q1AAU6; -.
DR SMR; Q1AAU6; -.
DR IntAct; Q1AAU6; 1.
DR STRING; 10116.ENSRNOP00000059763; -.
DR iPTMnet; Q1AAU6; -.
DR PhosphoSitePlus; Q1AAU6; -.
DR PaxDb; Q1AAU6; -.
DR PRIDE; Q1AAU6; -.
DR GeneID; 314961; -.
DR KEGG; rno:314961; -.
DR UCSC; RGD:1307379; rat. [Q1AAU6-1]
DR CTD; 50807; -.
DR RGD; 1307379; Asap1.
DR eggNOG; KOG0521; Eukaryota.
DR InParanoid; Q1AAU6; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q1AAU6; -.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q1AAU6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031253; C:cell projection membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISO:RGD.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
DR CDD; cd07641; BAR_ASAP1; 1.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11965; SH3_ASAP1; 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; IPR037928; ASAP1_BAR.
DR InterPro; IPR038016; ASAP1_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 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; 2.
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; Cilium biogenesis/degradation; Cytoplasm;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..1144
FT /note="Arf-GAP with SH3 domain, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000263054"
FT DOMAIN 336..428
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 451..574
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 612..644
FT /note="ANK 1"
FT REPEAT 648..677
FT /note="ANK 2"
FT DOMAIN 1082..1144
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 466..489
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..1004
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1063
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 304..315
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021850"
FT VAR_SEQ 813..869
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021851"
FT CONFLICT 175
FT /note="M -> T (in Ref. 1; ABB71897/ABB71898)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="A -> T (in Ref. 1; ABB71896)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="K -> Q (in Ref. 1; ABB71897/ABB71898)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="D -> N (in Ref. 1; ABB71897/ABB71898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1144 AA; 127088 MW; 798B02B3194BBA38 CRC64;
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL
EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK
FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYEMKFTKI
EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL
IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
PKEVGGLYVP SRANSDSQSR QGGYSMHQLQ GNKEYGSEKK GFLLKKSDGI RKVWQRRKCA
VKNGILTISH ATSNRQPAKL NLLTCQVKPN AEDKKSFDLI SHNRTYHFQA EDEQDYVAWI
SVLTNSKEEA LTMAFRGEQS TGENSLEDLT KAIIEDVQRL PGNDICCDCG SSEPTWLSTN
LGILTCIECS GIHREMGVHI SRIQSLELDK LGTSELLLAK NVGNNSFNDI MEANLPSPSP
KPTPSSDMTV RKEYITAKYV DHRFSRKTCA SSSAKLNELL EAIKSRDLLA LIQVYAEGVE
LMEPLLEPGQ ELGETALHLA VRTADQTSLH LVDFLVQNCG NLDKQTSVGN TVLHYCSMYG
KPECLKLLLR SKPTVDIVNQ NGETALDIAK RLKATQCEDL LSQAKSGKFN PHVHVEYEWN
LRQDEMDESD DDLDDKPSPI KKERSPRPQS FCHSSSISPQ DKLALPGFST PRDKQRLSYG
AFTNQIFVST STDLPTSPTS EAPPLPPRNA GKGPTGPPST LPLGTQTSSG SSTLSKKRSP
PPPPGHKRTL SDPPSPLPHG PPNKGAIPWG NDVGPSSSSK TANKFEGLSQ QASTSSAKTA
LGPRVLPKLP QKVALRKTET SHHLSLDRAN IPPETFQKSS QLSELPQKPP LGDLPPKPME
LAPKPQIGEL PPKPGELPPK PQLGDLPPKP QLSDLPPKPQ MKDLPPKPQL GDLLAKSQAS
DLSAKVQPPS EVTQRSHTGD LSPNVQSRDA IQKQASEDSN DLTPTLPETP VPLPRKINTG
KNKVRRVKTI YDCQADNDDE LTFIEGEVII VTGEEDQEWW IGHIEGQPER KGVFPVSFVH
ILSD
