ID G3TA51_LOXAF Unreviewed; 907 AA.
AC G3TA51;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain 3 {ECO:0000313|Ensembl:ENSLAFP00000010717.3};
GN Name=ASAP3 {ECO:0000313|Ensembl:ENSLAFP00000010717.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010717.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010717.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010717.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010717.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010717.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3TA51; -.
DR STRING; 9785.ENSLAFP00000010717; -.
DR Ensembl; ENSLAFT00000012816.3; ENSLAFP00000010717.3; ENSLAFG00000012812.3.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000161085; -.
DR HOGENOM; CLU_006942_1_0_1; -.
DR InParanoid; G3TA51; -.
DR OMA; IMEAQLP; -.
DR TreeFam; TF325156; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
DR CDD; cd17900; ArfGap_ASAP3; 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 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; IPR047006; ASAP3_ArfGap.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037844; PH_ASAP.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45854:SF1; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 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 PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 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 PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW 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 429..551
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 588..623
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 624..656
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 276..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 99319 MW; 941FE48DAC60583D CRC64;
MPEQLSVAEF LAITAEDLSS PAGAVAFAAK MPRCRGAALA REESLEGDQA ILQRIKKSVR
AIHSSGLGHV ENEEQYREAV ESLGNSHLSQ NSHELSTGFL NLAVFTREVA ALFKNLVQNL
NNIVSFPLDS LLKGQLRDGR QDSKKQLDKA WKDYEAKTAF YQMERVSTRF PEGGLSIHSM
GTCKDHCVFS LCGCPYYLLK AGESQVKQGP DFLQSLVKFF HAQHNFFQDG WKAAQSLSPF
IEKLAASVHT LRQAQEEELQ KLTQLRDSLR GTLQLQNREE QETVGRKNSG GGYSIHQHQG
NKQFGTEKVG FLYKKSPRIR RVWQKRKCGV KYGCLTISHS TINRPPVKLT LLTCQVRPNP
EEKKCFDLVT HNRTYHFQTE DEHECEAWVS VLQNSKDEAL SSAFLGEPSS GPGPCGGAGL
DGEPRDLTKL LIAEVKSRPG NGQCCDCGAP DPTWLSTNLG VLTCIQCSGV HRELGVRFSR
MQSLTLDLLG PSELLLALNI GNTHFNEIME AQLPSHGGSK PSAESDMSPR RDYIVAKYVE
HRFARRSTLE PQRLWTAIYN RDLLSVLEAF ANGQDFGQTL PGPDGQAPGE LALHLAVRVA
NQASLPLVDF IIQNGGHLDA KAPDGNTALH YAALHNQPDC LKLLLKGRAS VSAVNEAGET
ALDVARKKQH KECQELLEQA QAGTLTFPLH VDYSWGISVE PGSDSEEDEE EKRYPLKLPA
QARWSSGRQD ISNKTYEAIA SLGSATPRSQ NEDFPPPLPV KNPSRTMVQG RVGHASGDCS
EAPSLSSEPP GTPESLRSPA SSSSSLTSPV EPGGPSQALP GSEESLQEPL GTTRPSLLPG
NTPAEMYPPV RFSSESTRSY RRGGRNLEDS PSARRPLPRR NMPVGFTEGD GSRTGVLPAS
SVQLLQD
//
