ASAP1_BOVIN
ID ASAP1_BOVIN Reviewed; 1129 AA.
AC O97902;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 151.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND PROTEIN SEQUENCE OF
RP 80-101; 303-324; 550-558; 804-826; 839-854 AND 1039-1049.
RC TISSUE=Brain;
RX PubMed=10022919; DOI=10.1128/mcb.19.3.2330;
RA King F.J., Hu E., Harris D.F., Sarraf P., Spiegelman B.M., Roberts T.M.;
RT "DEF-1, a novel src SH3 binding protein that promotes adipogenesis in
RT fibroblastic cell lines.";
RL Mol. Cell. Biol. 19:2330-2337(1999).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 61-65; 130-133;
RP 424-427 AND 502-525.
RC TISSUE=Brain;
RX PubMed=9819391; DOI=10.1128/mcb.18.12.7038;
RA Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA Randazzo P.A.;
RT "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT associates with and is phosphorylated by Src.";
RL Mol. Cell. Biol. 18:7038-7051(1998).
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. Plays a role in ciliogenesis (By
CC similarity). May function as a signal transduction protein involved in
CC the differentiation of fibroblasts into adipocytes and possibly other
CC cell types. {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 {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Partially membrane-associated.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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; AF112886; AAD19965.1; -; mRNA.
DR RefSeq; NP_787015.1; NM_175821.2.
DR AlphaFoldDB; O97902; -.
DR SMR; O97902; -.
DR IntAct; O97902; 2.
DR STRING; 9913.ENSBTAP00000045295; -.
DR PaxDb; O97902; -.
DR PRIDE; O97902; -.
DR GeneID; 327705; -.
DR KEGG; bta:327705; -.
DR CTD; 50807; -.
DR eggNOG; KOG0521; Eukaryota.
DR InParanoid; O97902; -.
DR OrthoDB; 751525at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031253; C:cell projection membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; IBA:GO_Central.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IBA:GO_Central.
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; PF00018; SH3_1; 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 ANK repeat; Cilium biogenesis/degradation; Cytoplasm;
KW Direct protein sequencing; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..1129
FT /note="Arf-GAP with SH3 domain, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000074195"
FT DOMAIN 327..419
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 442..565
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 603..635
FT /note="ANK 1"
FT REPEAT 639..668
FT /note="ANK 2"
FT DOMAIN 1067..1129
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 457..480
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..812
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1AAU6"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1048
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT CONFLICT 65
FT /note="D -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 125382 MW; C1576C2EAC0ACDA8 CRC64;
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL
EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK
FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI
EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL
IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
QKESRRDSQS RQGGYSMHQL QGNKEYGSEK KGYLLKKSDG IRKVWQRRKC SVKNGILTIS
HATSNRQPAK LNLLTCQVKP NAEDKKSFDL ISHNRTYHFQ AEDEQDYVAW ISVLTNSKEE
ALTMAFRGEQ SAGESSLEEL TKAIIEDVQR LPGNDVCCDC GSAEPTWLST NLGILTCIEC
SGIHREMGVH ISRIQSLELD KLGTSELLLA KNVGNNSFND IMEANLPSPS PKPTPSSDMT
VRKEYITAKY VDHRFSRKTC SSSSAKLNEL LEAIKSRDLL ALIQVYAEGV ELMEPLLEPG
QELGETALHL AVRTADQTSL HLVDFLVQNC GNLDKQTALG NTALHYCSMY SKPECLKLLL
RSKPTVDVVN QAGETALDIA KRLKATQCED LLSQAKSGKF NPHVHVEYEW NLRQEEMDES
DDDLDDKPSP IKKERSPRPQ SFCHSSSISP QDKLSLPGFS TPRDKQRLSY GAFTNQIFVS
TSTDSPTSPI AEAPPLPPRN ATKGPPGPPS TLPLSTQTSS GSSTLSKKRS PPPPPGHKRT
LSDPPSPLPH GPPNKGAVPW GNDVGPSSSS KTTNKFEGLS QQSSTGSAKT ALGPRVLPKL
PQKVALRKTE TSHHLSLDKA NVPPEIFQKS SQLTELPQKP PPGDLPPKPT ELAPKPPIGD
LPPKPGELPP KPQLGDLPPK PQLADLPPKP QVKDLPPKPQ LGELLAKPQT GDASPKAQPP
LELTPKSHPA DLSPNVPKQA SEDTNDLTPT LPETPVPLPR KINTGKSKVR RVKTIYDCQA
DNDDELTFME GEVIVVTGEE DQEWWIGHIE GQPERKGVFP VSFVHILSD
