ID A1L1D7_XENTR Unreviewed; 1056 AA.
AC A1L1D7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 {ECO:0000313|RefSeq:NP_001090735.1};
DE SubName: Full=LOC100036721 protein {ECO:0000313|EMBL:AAI29010.1};
GN Name=asap1 {ECO:0000313|RefSeq:NP_001090735.1,
GN ECO:0000313|Xenbase:XB-GENE-1013472};
GN Synonyms=ddef1 {ECO:0000313|RefSeq:NP_001090735.1}, LOC100036721
GN {ECO:0000313|EMBL:AAI29010.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI29010.1};
RN [1] {ECO:0000313|RefSeq:NP_001090735.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI29010.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000313|EMBL:AAI29010.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001090735.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; BC129009; AAI29010.1; -; mRNA.
DR RefSeq; NP_001090735.1; NM_001097266.1.
DR GeneID; 100036721; -.
DR KEGG; xtr:100036721; -.
DR AGR; Xenbase:XB-GENE-1013472; -.
DR CTD; 50807; -.
DR Xenbase; XB-GENE-1013472; asap1.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000008143; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08848; ArfGap_ASAP1; 1.
DR CDD; cd07641; BAR_ASAP1; 1.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11965; SH3_ASAP1; 1.
DR Gene3D; 1.25.40.950; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR004148; BAR_dom.
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:SF2; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45854; ASAP FAMILY MEMBER; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 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; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 304..396
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 419..543
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 580..615
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 616..648
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 994..1056
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 692..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..915
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 118112 MW; EB658E350A52C35B CRC64;
MPDQISVSEF ISETTEDYNS PTTSSFTTRL QSCRNSINVL EEALDQDRTA LQKVKKSVKA
IYNSGQDHVQ NEENYAQALD KFGSNFLSRD NADLGTAFVK FSTLTKELST LLKNLLQGLS
HNVIFTLDSL LKGDLKGVKG DLKKPFDRAW KDYETKFTKI EKEKREHAKQ HGMIRTEITG
AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL IKYYHAQCNF FQDGLKTADK
LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD QKEDSQSKQA GYSMHQLQGN
KEYGSEKKGY LLKKSDGIRK VWQRRKCTVK NGILTISHAT SNRPPTKLNL LTCQVKPNAD
EKKCFDLISH NRTYHFQAED EQEYIAWISV LTNSKEDALN MAFRGDQSTG ESSLEDLTKA
IIDDVQKTPG NEVCCDCGSP DPTWLSTNLG ILTCIECSGI HREMGVHISR IQSLELDKLG
TSELLLAKNV GNNSFNDIME GNLLSPSAKP SPSSDMIARK EYITAKYVER RFSRKICSTG
AEKLNELLEA VKSRDLLALI QVYAEGVEIM EPLLESGQEP GETALHYAVR TADHTSLPLV
DFLVQNCGNL DKQTGKGNTA LHYCCLYNKP ECLKLLLRGK PTIDAVNHIG ETAFDVAKRQ
KAAQCEELVS QALAGKLNPH VHVEYDWNLR QEEMDESDDD LEDKPSPIKK ERSPRPQSFC
HSSSISPQDK LSLPGFNTPR DKQRLSYGAF TNQIFMSTST DSPTSPTADA PPLPPRNAGK
GNDLGPSAAD RTLNKFERLS QSSGTGTTKT ALGPRVLPKL PQKVALRKID TTHHLSMDKY
NQQPEIFQKS PQPGDLPQKP QIADLPPKPQ PLDIAQKPHV GDLPPKPGEL PPKPQLGDLP
PKPQDLPPKP QLKDLPPKPN LAEVMCKTPV ADIVPKPHTN EANQNSQPVD ATHNAQPTDQ
TPVQKQVPET SNNGPPPLPE TPVPLPRKIN TGKNKLKRVK TIYDCQADND DELTFAEGEV
IIVTGEEDQE WWIGHIEGFP DRKGVFPVSF VHLLTE
//
