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Database: UniProt
Entry: A0A2K6C0F1_MACNE
LinkDB: A0A2K6C0F1_MACNE
Original site: A0A2K6C0F1_MACNE 
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
//
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