ID A0A3Q1F1M9_9TELE Unreviewed; 982 AA.
AC A0A3Q1F1M9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSAPOP00000009957.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000009957.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000009957.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSAPOT00000000676.1; ENSAPOP00000009957.1; ENSAPOG00000012445.1.
DR GeneTree; ENSGT00940000155623; -.
DR Proteomes; UP000257200; 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; cd07642; BAR_ASAP2; 1.
DR CDD; cd13251; PH_ASAP; 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; 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; PS50297; ANK_REP_REGION; 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:UP000257200};
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 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 584..619
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 620..652
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 920..982
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 287..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 109703 MW; 118E8742D5DE0658 CRC64;
MPDQITVSEF VAETNEDYKS PTASNFTTRM SHCRNTVAAL EEALDVDRSV LYKMKKSVKA
IYTSGLAHVE NEEQYTQALE KFGENCVYRD DPDLGSAFLK FSVFTKELTA LFKNLFQNMN
NIITFPLDSL LKGDLKGVKG DLKKPFDKAW KDYETKVTKI EKEKKEHARQ HGMIRTEISG
AEIAEEMEKE RRFFQLQMCE YLLKVNEIKI KKGVDLLQNL IKYFHAQCNF FQDGLKAVDN
LKPSIEKLAT DLHTIKQVQD EERKQLTQLR DVLKSALQVE QKEDSQVRQS TTYSLHQPQG
NKEHGTERSG YLYKKSDGLR KVWQKRKCTA KNGYLTISHG TANRPPAKLN LLTCQVKHNP
EEKRSFDLIS HDRTYHFQAE DDQDCQIWIS VLQNSKEEAL NQAFKGDHHV GENNIVQELT
KAILGEVKRM TGNDVCCDCG APNPTWLSTN LGILTCIECS GIHRELGVHY SRIQSLTLDV
LSTSELLLAK NVGNAGFNEI MEACLSAENV VKPNPASDMQ ARKDFITAKY TEKRFARKKC
PDPTSRLHTL CDAVKARDIF SLIQVYAEGV DLMEPIPLAN GHEQGETALH LAVRLVDRTS
LHIVDFLTQN SLNLDKQTAK GSTALHYCCL TDNSECLKLL LRGKASIEIA NEAGETPLDI
ARRLKHLQCE ELLNQALAGK FNAHVHVEYE WCLQHEDLDE SDEDLDEKPS PHRRDERPVS
CYTPGSNSHL QSGSAGRDAA GLSKDKQRPY MPNLVNNETY GTILNTNPPQ PATTSAPPLP
PRNLAQLAGL GGISQSSASS SWKPGSLDLV GRQRSSSDPP NMHXPPVPPM RLTSTGGLGL
APVAKMEAMS IQSKSSQGPL GSRSAPPKSP AGNDKSFNRG PLNRTESIER AAKEVPGCPQ
NSIGQSLPPA PMPRKAYPKQ RPKRVKAIYN CVADNPDELT FSEGEVIVVD GEEDQEWWLG
HIEGDPMRRG AFPVTFVHFI AD
//
