Descriptions

ASAP1 is an Arf GTPase-activating protein (GAP) that functions on membrane surfaces to catalyze the hydrolysis of GTP bound to Arf. ASAP1 has a BAR domain which functions as membrane curvature sensors or as inducers of membrane curvature. The BAR domain influences GAP activity by binding to the PH domain and/or Arf GAP domain. The deletion of the entire BAR domain or the N-terminal extension increased GAP activity.

Autoinhibitory domains (AIDs)

Target domain

312-401 (PH domain);427-549 (Arf GAP domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A1Z7A6

Entry ID Method Resolution Chain Position Source
AF-A1Z7A6-F1 Predicted AlphaFoldDB

No variants for A1Z7A6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1Z7A6

No associated diseases with A1Z7A6

7 regional properties for A1Z7A6

Type Name Position InterPro Accession
domain Arf GTPase activating protein 427 - 547 IPR001164
domain SH3 domain 1091 - 1155 IPR001452
domain Pleckstrin homology domain 310 - 406 IPR001849
repeat Ankyrin repeat 556 - 663 IPR002110
domain BAR domain 32 - 267 IPR004148
domain ASAP1-like, SH3 domain 1095 - 1149 IPR035836
domain ASAP, PH domain 302 - 410 IPR037844

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Cell membrane; Peripheral membrane protein
  • Cell projection, microvillus
  • Detected in large puncta at the plasma membrane (PubMed:21976699, PubMed:27535433)
  • Excluded from the nucleus at interphase (PubMed:27535433)
  • Enriched in the nucleus at prometaphase (PubMed:27535433)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
apical part of cell The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
microvillus Thin cylindrical membrane-covered projections on the surface of an animal cell containing a core bundle of actin filaments. Present in especially large numbers on the absorptive surface of intestinal cells.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
metal ion binding Binding to a metal ion.
phosphatidylinositol phosphate binding Binding to phosphatidylinositol phosphate.

5 GO annotations of biological process

Name Definition
compound eye morphogenesis The morphogenetic process in which the anatomical structures of the compound eye are generated and organized. The adult compound eye is a precise assembly of 700-800 ommatidia. Each ommatidium is composed of 20 cells, identified by cell type and position. An example of compound eye morphogenesis is found in Drosophila melanogaster.
mitotic cleavage furrow ingression Advancement of the mitotic cleavage furrow from the outside of the cell inward towards the center of the cell. The cleavage furrow acts as a 'purse string' which draws tight to separate daughter cells during mitotic cytokinesis and partition the cytoplasm between the two daughter cells. The furrow ingresses until a cytoplasmic bridge is formed.
positive regulation of protein localization Any process that activates or increases the frequency, rate or extent of a protein localization.
regulation of Golgi organization Any process that modulates the frequency, rate or extent of Golgi organization.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.

15 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A5PK26 ACAP1 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 Bos taurus (Bovine) SS
O97902 ASAP1 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Bos taurus (Bovine) SS
Q15027 ACAP1 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 Homo sapiens (Human) EV
Q15057 ACAP2 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 Homo sapiens (Human) PR
Q9ULH1 ASAP1 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Homo sapiens (Human) EV
Q8TDY4 ASAP3 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 Homo sapiens (Human) SS
O43150 ASAP2 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 Homo sapiens (Human) SS
Q8K2H4 Acap1 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 Mus musculus (Mouse) SS
Q6ZQK5 Acap2 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 Mus musculus (Mouse) PR
Q9QWY8 Asap1 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Mus musculus (Mouse) SS
Q7SIG6 Asap2 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 Mus musculus (Mouse) SS
Q5U464 Asap3 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 Mus musculus (Mouse) SS
Q1AAU6 Asap1 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Rattus norvegicus (Rat) SS
Q9C6C3 AGD2 ADP-ribosylation factor GTPase-activating protein AGD2 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SMX5 AGD4 ADP-ribosylation factor GTPase-activating protein AGD4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MPPSLIAVSE FVEETRSDYS SPTTSTFASR MPDCRHTIGV LEERLEFDRE GLTKLKKAVK
70 80 90 100 110 120
AIHNSGNTHV DNEMFMVRAL ERLGGKVIEQ DEPDIGAAFL KFSVVTKELS ALMKTLMQNI
130 140 150 160 170 180
NNIVMFPVDS MLKSELRGVK GDMKRPFDKA AKDYEAKFIK IEKEKKAQAK EAGMVRTEID
190 200 210 220 230 240
AAVVAEEMEK ERRLYQLQTC EYLLKYKDIK TKTGIELLQH LIEYYHALSN YFKDGLQTIE
250 260 270 280 290 300
HFGTYIGDLS EKLHEIKQKQ DEDRRSLLDL RTVLRSTPDF ERVDNVPSSE SRSGGAGYSL
310 320 330 340 350 360
HQLQGDKHHG VTRQGHLLKK SEGKVRRVWQ KRRCRVTSDG FLDIFHADES KPPTRVNLLT
370 380 390 400 410 420
CQIKPVPDDK RGFDLISYNR PYHFQAEDEG DQKAWMAVLV NCKEKALTKA FQHANPQMSP
430 440 450 460 470 480
SLVELQKTVI RYVQLLPGND RCCDCGSRND VTWISLNFGI LVCIQCSGVH RDLGVHHSRI
490 500 510 520 530 540
QSLTLDNLTT ANLLIARAMG NSTLNDIMEA KLGRGKLQHE SSMEERYDFI RAKYVAKRYV
550 560 570 580 590 600
MRTCSDDNDL RCDLEQAVVN ADMSQLLQVW AEGADLTCCL PSSDAGETAL HLAVLREMGS
610 620 630 640 650 660
TLHIVDFLIQ NMPPKGLNKA TNPAGLLDVT GKNTALHLCA LHDRRECMKL LLRSGADYEL
670 680 690 700 710 720
KNSQNKTALD IAKEMGHNSC RELIECAIKR EKSAFDHINT DWNLPNEDGS TDFSDDETVI
730 740 750 760 770 780
DERKSRSRPP SFAGGDSPVL RSRSSTCDSI QSSSSPIANC PSRQFTLPSG LPSYTHSAGT
790 800 810 820 830 840
SPKQHISVGQ YLGSATNVGG NGPGNGGSSP SSASSQSVRA ARNSLNMQSD LGGHVTGARK
850 860 870 880 890 900
STSTANMNSL KKRTAPAPPP GTLGSASSSS FYGTLPHPPR HSQNFDASDI RAINHKNQSL
910 920 930 940 950 960
DVAYGTLPHL RSVESSPRGG GGYGYGVSQD PGGSGNGSNN SLMPAMTTFG HKRSPSGESL
970 980 990 1000 1010 1020
NRNIHLAGAK LVLPPTGELP TLKHVDKSAL TRPKIPPPGP PSEREISNGQ SNESISSMDE
1030 1040 1050 1060 1070 1080
GPVAPPRKLV NQSANFPDYE SWHTDMDSSG GGLDHSAESN VSSSDNDRLN SSPDNPSKTG
1090 1100 1110 1120 1130 1140
GAGLGGKFHY NGQRRCRALY DCVADNDDEL EFKEGEILIV LNERTDDENW MEGIIEGQPT
1150
RKGMFPVSFV HMLPD