ASAP3_MOUSE
ID ASAP3_MOUSE Reviewed; 904 AA.
AC Q5U464;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3;
DE AltName: Full=Development and differentiation-enhancing factor-like 1;
GN Name=Asap3; Synonyms=Ddefl1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Promotes cell proliferation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; BC085250; AAH85250.1; -; mRNA.
DR CCDS; CCDS18802.1; -.
DR RefSeq; NP_001008233.1; NM_001008232.2.
DR AlphaFoldDB; Q5U464; -.
DR SMR; Q5U464; -.
DR STRING; 10090.ENSMUSP00000041899; -.
DR iPTMnet; Q5U464; -.
DR PhosphoSitePlus; Q5U464; -.
DR jPOST; Q5U464; -.
DR MaxQB; Q5U464; -.
DR PaxDb; Q5U464; -.
DR PRIDE; Q5U464; -.
DR ProteomicsDB; 277244; -.
DR Antibodypedia; 30164; 169 antibodies from 25 providers.
DR DNASU; 230837; -.
DR Ensembl; ENSMUST00000047526; ENSMUSP00000041899; ENSMUSG00000036995.
DR GeneID; 230837; -.
DR KEGG; mmu:230837; -.
DR UCSC; uc008vhu.2; mouse.
DR CTD; 55616; -.
DR MGI; MGI:2684986; Asap3.
DR VEuPathDB; HostDB:ENSMUSG00000036995; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000161085; -.
DR HOGENOM; CLU_006942_1_0_1; -.
DR InParanoid; Q5U464; -.
DR OMA; LQHTQCI; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q5U464; -.
DR TreeFam; TF325156; -.
DR BioGRID-ORCS; 230837; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Asap3; mouse.
DR PRO; PR:Q5U464; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q5U464; protein.
DR Bgee; ENSMUSG00000036995; Expressed in ectoplacental cone and 82 other tissues.
DR Genevisible; Q5U464; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISS:UniProtKB.
DR CDD; cd13251; PH_ASAP; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 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; IPR028775; ASAP3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037844; PH_ASAP.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45854; PTHR45854; 1.
DR PANTHER; PTHR45854:SF1; PTHR45854:SF1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 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.
PE 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Cytoplasm; Metal-binding; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..904
FT /note="Arf-GAP with SH3 domain, ANK repeat and PH domain-
FT containing protein 3"
FT /id="PRO_0000232888"
FT DOMAIN 302..394
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 425..550
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 584..616
FT /note="ANK 1"
FT REPEAT 620..649
FT /note="ANK 2"
FT ZN_FING 440..463
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 275..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..169
FT /evidence="ECO:0000255"
FT COILED 249..273
FT /evidence="ECO:0000255"
FT COMPBIAS 735..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 99276 MW; A8B0A6BFCDA3D95D CRC64;
MPEQLSVAEF LAVTAEDLSS PAGAAAFAAK MPRCRGAALA REEALEGDQA ILQRIKKAVR
AIHSSGLGHV ETEEHYREAV EALGNSHLSQ NSHELSTGFL NLAVFTREVA ALFKNLVQNL
NNIVSFPLDS LMKGHLRDGR HDSKKHLEKA WKDYESKVAK LEKERDRARF PGGSHGVMSQ
DTQRERRVFQ LHMCEYLVKA GESQVKQGPD FLQSLIKFFH AQHNFFQDGW KAAQSLSPFI
DKLAASVHGL RQAQEEELHK LTQLRDSLRG MLHLESREDH PNRKNSGGGY SIHQHQGNKQ
FGTEKVGFLY KKSDGIRRVW QKRKCGVKYG CLTISHSMIN RPPVKLPLLT CQVRPNPEEK
RCFDLVTHNR TYHFHAEDEQ ECEAWVSVLQ NSKDEALSNA FHGEPSGGQW SWGTRLDTEP
HDLTNMLVAE VKSRPGNDRC CDCGAADPTW LSTNLGVLTC IQCSGVHREL GVRFSRIQSL
TLDLLGPSEL LLALNIGNSH FNEVMEAHLP SHGSPKPSAE SDMSSRRNYI VAKYVEHKFA
RHSTPDPQKL RTAICSRDLL SVLEAFANGQ DFGQLLPGPD GQAPGELALH LAIRVASHAS
LPIVDFLIQN GGHLDAKAAD GNTALHCAAL HGQLDCLKLL LRGRAPVGAV NDAGETALDI
ARNRQHKECE ELLEQAQAGT LAFPLHMDYH WGHSMEHGFD SEEEEEEEKH CPSKPPAQAC
WGSVRLDISN KTYETVATPG PATTQSQSED SPPPLPIKNS SRTIVLGRAG HCSGDRSDLP
SLRSESPEAL ENRSSPASSS SSLTSSVEPG GLSQAPSSPE EGLQESASIS RPGLASGTTS
AEVYLPVKFS SESTRSYRRG GRSLEDSPSA RQPLCSRRHI PVGLVEGDGS KIGVLPDSLQ
LLHD