ID A0A2Y9LMD3_DELLE Unreviewed; 1008 AA.
AC A0A2Y9LMD3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 isoform X2 {ECO:0000313|RefSeq:XP_022409886.1};
GN Name=ASAP2 {ECO:0000313|RefSeq:XP_022409886.1};
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_022409886.1};
RN [1] {ECO:0000313|RefSeq:XP_022409886.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022409886.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_022409886.1; XM_022554178.1.
DR AlphaFoldDB; A0A2Y9LMD3; -.
DR Ensembl; ENSDLET00000006724; ENSDLEP00000006069; ENSDLEG00000004523.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08849; ArfGap_ASAP2; 1.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11966; SH3_ASAP2; 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; IPR035677; ASAP2_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:SF4; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 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; 3.
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:UP000248483};
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 305..397
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 421..543
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 620..652
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 946..1008
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 284..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..896
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 111696 MW; 21D176089094AF79 CRC64;
MPDQISVSEF VAETHEDYKA PTASSFTTRT AQCRNTVAAI EEALDVDRMV LYKMKKSVKA
INISGLAHVE NEEQYTQALE KFGGNCVCRD DPDLGSAFLR FSVFTKELTA LFKNLIQNMN
NIISFPLDSL LKGDLKGVKG DLKKPFDKAW KDYETKITKI EKEKKEHAKL HGMIRTEISG
AEIAEEMEKE RRFFQLQMCE YLLKVNEIKI KKGVDLLQNL IKYFHAQCNF FQDGLKAVES
LKPSIETLST DLHTIKQAQD EERRQLIQLR DILKSALQVE QKEDSQLRQS TAYSLHQPQG
NKEHGTERNG NLYKKSDGIR KVWQKRKCSV KNGFLTISHG TANRPPAKLN LLTCQVKTNP
EEKKCFDLIS HDRTYHFQAE DEQECQIWMS VLQNSKEEAL NNAFKGDDNT GENNIVQELT
KEIISEVQRM TGNDVCCDCG APDPTWLSTN LGILTCIECS GIHRELGVHY SRMQSLTLDV
LGTSELLLAK NIGNAGFNEI MECCLPAEDS IKPNPSSDMN ARKDYITAKY IERKYARKRH
ADNAAKLHSL CEAVKARDIF GLLQAYADGV DLTEKIPLAN GHEPDETALH LAVRSVDRTS
LHIVDFLVQN SGNLDKQTGK GSTALHYCCL TDSAECLKLL LRGKASIGIA NESGETPLDI
AKRLRHERCE ELLTQALSGR FNSHVHVEYE WRLLHEDLDE SDDDVDEKLQ PSPSRREDRP
VSFYQLGSSQ LQSNAASLAR DAASLAKDKQ RSFVPSILQN ETYGAILSSS PPPAQPAAPS
AASAPPLPPR NVAKVQPASS ANALWKTNSV SVDSVSRQRS SSDPPAVHPP LPPLRVTSTN
PLAPTPPPPV AKTPSVLEAL SQQSKPAQPG LPPSKAPPPL PPQLPSRLPQ KRPAPGPDKS
SPLINKGQPR GPAVDLSGTE TLGPLSNAVV TQPPAPMPRK SQVTKLKPKR VKALYNCVAD
NPDELTFSEG DVIVVDGEED QEWWIGHIDG DPSRKGAFPV SFVHFIAD
//