ID E9QMI7_MOUSE Unreviewed; 1090 AA.
AC E9QMI7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain1 {ECO:0000313|Ensembl:ENSMUSP00000105741.4};
GN Name=Asap1 {ECO:0000313|Ensembl:ENSMUSP00000105741.4,
GN ECO:0000313|MGI:MGI:1342335};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000105741.4, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000105741.4, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000105741.4,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000105741.4}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000105741.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; E9QMI7; -.
DR SMR; E9QMI7; -.
DR jPOST; E9QMI7; -.
DR MaxQB; E9QMI7; -.
DR PeptideAtlas; E9QMI7; -.
DR ProteomicsDB; 310183; -.
DR Antibodypedia; 27290; 275 antibodies from 30 providers.
DR Ensembl; ENSMUST00000110114.10; ENSMUSP00000105741.4; ENSMUSG00000022377.17.
DR AGR; MGI:1342335; -.
DR MGI; MGI:1342335; Asap1.
DR VEuPathDB; HostDB:ENSMUSG00000022377; -.
DR GeneTree; ENSGT00940000158547; -.
DR ChiTaRS; Asap1; mouse.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000022377; Expressed in saccule of membranous labyrinth and 258 other cell types or tissues.
DR ExpressionAtlas; E9QMI7; baseline and differential.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:E9QMI7,
KW ECO:0007829|MaxQB:E9QMI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 339..431
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 454..577
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 615..650
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 651..683
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1028..1090
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 725..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 121644 MW; B28FAAB4D8C71A84 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
PKEVGGLYVA SRANSVIRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS DGIRKVWQRR
KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF DLISHNRTYH FQAEDEQDYI
AWISVLTNSK EEALTMAFRG EQSTGENSLE DLTKAIIEDV QRLPGNDICC DCGSSEPTWL
STNLGILTCI ECSGIHREMG VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS
PSPKPTPSSD MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE
GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS VGNTVLHYCS
MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC EDLLSQAKSG KFNPHVHVEY
EWNLRQDEMD ESDDDLDDKP SPIKKERSPR PQSFCHSSSI SPQDKLALPG FSTPRDKQRL
SYGAFTNQIF ASTSTDLPTS PTSEAPPLPP RNAGKGNDVG PLSSSKTANK FEGLSQQAST
SSAKTALGPR VLPKLPQKVA LRKTETSHHL SLDRTNIPPE TFQKSSQLTE LPQKPPLGEL
PPKPVELAPK PQVGELPPKP GELPPKPQLG DLPPKPQLSD LPPKPQMKDL PPKPQLGDLL
AKSQAGDVSA KVQPPSEVTQ RSHTGDLSPN VQSRDAIQKQ ASEDSNDLTP TLPETPVPLP
RKINTGKNKV RRVKTIYDCQ ADNDDELTFI EGEVIIVTGE EDQEWWIGHI EGQPERKGVF
PVSFVHILSD
//
