ID A0A2Y9LM25_DELLE Unreviewed; 1119 AA.
AC A0A2Y9LM25;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 isoform X1 {ECO:0000313|RefSeq:XP_022409791.1};
GN Name=ASAP1 {ECO:0000313|RefSeq:XP_022409791.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022409791.1};
RN [1] {ECO:0000313|RefSeq:XP_022409791.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022409791.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022409791.1; XM_022554083.2.
DR AlphaFoldDB; A0A2Y9LM25; -.
DR STRING; 9749.A0A2Y9LM25; -.
DR KEGG; dle:111164426; -.
DR InParanoid; A0A2Y9LM25; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000248483; 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; 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 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:UP000248483};
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 324..416
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 439..562
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 600..635
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 636..668
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1057..1119
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 711..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 123959 MW; 69F6681D97A42D03 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
QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK NGILTISHAT
SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED EQDYVAWISV LTNSKEEALT
MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG NDVCCDCGSS EPTWLSTNLG ILTCIECSGI
HREMGVHISR IQSLELDKLG TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK
EYITAKYVDH RFSRKTCSSS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL
GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTA LHYCSMYGKP ECLKLLLRSK
PTVDVANQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH VHVEYEWNLR QEEMDESDDD
LDDKVSPSPI KKERSPRPQS FCHSSSTSPQ DKLSLPGFST PRDKQRLSYG AFTNQIFVST
STDSPTAPTA EAPPLPPRNA GKGPTGPPSA LPLSTQTSSG SSTLSKKRPP PPPPGHKRTL
SDPPSPLPHG PPNKGAVPWG NDVGPSSSSK TANKFEGLSQ QSSTGSAKTA LGPRVLPKLP
QKVALRKTET SHHLSLDKAN VPPELFQKSS QLAELPQKPP PGDLPPKPTE LAPKPPIGDL
PPKPGDLPPK PQLADLPPKP QVKDLPPKPQ LGDLLAKPQA ADASPKAQPP PELALKSHPA
DLSPNIPKQA SEDSNDLTPT LPETPVPLPR KINTGKSKVR RVKTIYDCQA DNDDELTFME
GEVIVVTGEE DQEWWIGHIE GQPERKGVFP VSFVHILSD
//
