ID A0A2K5DSC9_AOTNA Unreviewed; 1089 AA.
AC A0A2K5DSC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSANAP00000023868.1};
GN Name=ASAP1 {ECO:0000313|Ensembl:ENSANAP00000023868.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000023868.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000023868.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5DSC9; -.
DR Ensembl; ENSANAT00000041783.1; ENSANAP00000023868.1; ENSANAG00000029467.1.
DR GeneTree; ENSGT00940000158547; -.
DR Proteomes; UP000233020; Unplaced.
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; 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; 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; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
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:UP000233020};
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 284..376
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 399..512
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 560..595
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1027..1089
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 121213 MW; 2BABC623929BB532 CRC64;
LLRHYSHHWI ALDQDRTALQ KVKKSVKAIY NSGQDHVQNE ENYAQVLDKF GSNFLSRDNP
DLGTAFVKFS TLTKELSTLL KNLLQGLSHN MIFTLDSLLK GDLKGVKGDL KKPFDKAWKD
YETKFTKIEK EKREHAKQHG MIRTEITGAE IAEEMEKERR LFQLQMCEYL IKVNEIKTKK
GVDLLQNLIK YYHAQCNFFQ DGLKTADKLK QYIEKLAADL YNIKQTQDEE KKQLTALRDL
IKSSLQLDQK EVSGLHVYKR ANNDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK
VWQRRKCSVK NGILTISHAT SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED
EQDYVAWISV LTNSKEEALT MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG NDICCDCGSS
EPTWLSTNLG ILTCIECSGI HREMGVHISR IQSLELDKLG TSELLLAKNV GNNSFNDIME
ANLPSPSPKP MPSSDMTVRK EYITAKYVDH RFSRKTCSTS SAKLNELLEA IKSRDLLALI
QVYAEGVELM EPLLEPGQEL GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV
LHYCSMYSKP ECLKLLLRSK PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH
VHVEYEWNLR QEEMDESDDD LDDKPSPIKK ERSPRPQSFC HSSSISPQDK LALPGFSTPR
DKQRLSYGAF TNQIFISTST DSPTSPTAEA PPLPPRNAGK GPTGPPSTLP LSTQTSSGSS
TLSKKRPPPP PPGHKRTLSD PPSPLPHGPP NKGAVLWGND VGPSSSSKTT NKFEGLSQQS
STSSAKTALG PRVLPKLPQK VALRKTDHLS LDKANIPPEI FQKSSQLAEL PQKPPPGDLP
PKPTELAPKP QVGDLPPKPG ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA
KSQTGDVSPK AQQPSEVTPK SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT LPETPVPLPR
KINTGKNKVR RVKTIYDCQA DNDDELTFIE GEVIIVTGEE DQEWWIGHIE GQPERKGVFP
VSFVHILSD
//
