ID A0A2K6C0F1_MACNE Unreviewed; 1038 AA.
AC A0A2K6C0F1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSMNEP00000017136.1};
GN Name=ASAP1 {ECO:0000313|Ensembl:ENSMNEP00000017136.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000017136.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000017136.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6C0F1; -.
DR Ensembl; ENSMNET00000041361.1; ENSMNEP00000017136.1; ENSMNEG00000032554.1.
DR GeneTree; ENSGT00940000158547; -.
DR OMA; CAVKNGM; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032554; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
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 268..360
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 371..461
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 509..544
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 976..1038
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 115554 MW; 2D8E2B268F706F00 CRC64;
NYNYPDALDQ DRTALQKVKK SVKAIYNSGQ DHVQNEENYA QVLDKFGSNF LSRDNPDLGT
AFVKFSTLTK ELSTLLKNLL QGLSHNVIFT LDSLLKGDLK GVKGDLKKPF DKAWKDYETK
FTKIEKEKRE HAKQHGMIRT EITGAEIAEE MEKERRLFQL QMCEYLIKVN EIKTKKGVDL
LQNLIKYYHA QCNFFQDGLK TADKLKQYIE KLAADLYNIK QTQDEEKKQL TALRDLIKSS
LQLDQKEDSQ SRQGGYSMHQ LQGNKEYGSE KKGYLLKKSD GIRKVWQRRK CSVKNGILTI
SHATSNRQPA KLNLLTCQVK PNAEDKKSFD LISHNRTYHF QAEDEQDYIA KEEAANHVRG
EQWGLNDLTK PTWLSTNLGI LTCIECSGIH REMGVHISRI QSLELDKLGT SELLLAKNVG
NNSFNDIMEA NLPSPSPKPT PSSDMTVRKE YITAKYVDHR FSRKTCSTSS AKLNELLEAI
KSRDLLALIQ VYAEGVELME PLLEPGQELG ETALHLAVRT ADQTSLHLVD FLVQNCGNLD
KQTALGNTVL HYCSMYSKPE CLKLLLRSKP TVDIVNQAGE TALDIAKRLK ATQCEDLLSQ
AKSGKFNPHV HVEYEWNLRQ EEMDESDDDL DDKPSPIKKE RSPRPQSFCH SSSISPQDKP
ALPGFSTPRD KQRLSYGAFT NQIFVSTSTD SPTSPTTEAP PLPPRNAGKG PTGPPSTLPL
STQTSSGSST LSKKRPPPPP PGHKRTLSDP PSPLPHGPPN KGAVPWGNDG GPSSSSKTTN
KFEGLSQQSS TSSAKTALGP RVLPKLPQKV ALRKTDHLSI DKSNIPPEIF QKSSQLAELP
QKPPPGDLPP KPTELAPRPQ VGDLPPKPGE LPPKPQLGDL PPKPQLSDLP PKPQMKDLPP
KPQLGDLLAK SQTGDVSPKA QQPSEVTPKS HPLDLSPNVQ SRDAIQKQAS EDSNDLTPTL
PETPVPLPRK INTGKNKVRR VKTIYDCQAD NDDELTFIEG EVIIVTGEED QEWWIGHIEG
QPERKGVFPV SFVHILSD
//