ID A0A452IWL2_9SAUR Unreviewed; 1269 AA.
AC A0A452IWL2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000032299.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000032299.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000032299.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSGAGT00000036617.1; ENSGAGP00000032299.1; ENSGAGG00000023098.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd17901; ArfGap_ARAP1; 1.
DR CDD; cd13254; PH2_ARAP; 1.
DR CDD; cd13256; PH3_ARAP; 1.
DR CDD; cd17226; RA_ARAP1; 1.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR45899:SF3; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 5.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 3.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 10..69
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 257..331
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 353..442
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 448..573
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 656..763
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 865..1046
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1079..1168
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 96..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 144109 MW; B3E5AEECE16CEA7E CRC64;
TAEQGASLPV AEWLRALHLD QYLESFEKND LWKVSDCRNL TDGALTQIGI LLPGHRKRIL
FGLQKAFMET LPATEGPVVA ARRPVPMKRN IFRVSDSATP ASRKSPLLTE LENPAGLSQV
PPPIPPRLGC PPSCTVNPSS LAPTLQPQPL PCSKSLISSP TPEPIPPSRS LTHHTQPAAP
ALSSLLHCEP PIPGTTPQPS PPHXHTPNPS PPAPSQSLHP QPEPSSPNTP TCCPIPEPPP
LAKANQPLPS RYSSYIYQRR WVKLDADYLR YFDSEKDTYS KRFIPVTSIV RVASIGDQKF
EVITNSRTFA FRAESDADRN EWMRTLQQMV DERKFKGLNR ISLFQPPTGA LDSVDKCGLL
ELRGFKNKLY VVVAGEKVFL YKNAEDYRQG IGITYIEMNV GNVKDVDRRG FDLTTPYRIF
SFSADSDQEK DEWVEAMQQS IAEALSNSEV AEKIWSVEAN RFCADCGSPK PDWASVNLCV
VICKRCAGEH RGLGPSITKV RSLKMDRKVW TEELIELFCQ VGNSVANQFW AANVPPSEAI
HVASGSQERR RFLIAKYKEG KYRRYHPLFG NQEELNKALC ATVTTSDLAE TQSLVFCGAE
VSCFSGDPDF PNPIALAEQA GQKLQMEFLL HNKNSEIPRV EAGSSEEKHY SVILPSVTHN
GFLYKTPSMA KLVHERKSRE EFSRRWCTLN DSIFSYYEND RNAVPNGEIK MEEIVCLVNN
PPDTHGFEST FEVYIESERL YLFGLDNPEA IWKWVKSIAK SFIHPRADEL LSHDFERIGR
LQYKGGLNLE RAKEGWFALS QSVLYAFFED SDKEETVHLK KLQELSKGLW GLVSLPRTLY
IQGERKLDFL GWVAAIQKAA GSSGDTLSEQ QLTESDIPVI VDRCIDYITQ CGLTSEGIYR
KSGQNSKTTG LLEMLRKDAR RVRLKEGEHH VDDVSNTLKR FFRDLGDGLF TKEFCQDWLK
AAAVENEEEK IGQYRQLLSS LPVVNRATVK ALINHLYRVQ YFSEMNQMNT HNLAIVFGPT
LFQTDGKDYK AGRVVEDLIS RYVVIFSVDE QEMRKQQDEI QAIIKMRIAG SSSGTQQAGD
FICTVYLEEK KTEAEQHIKI PATMTAEELT FEILDRRKIE TKEKEYWSCF EVNEREEAER
PLHYSEKVLP ILHGLGTDSY LVVKKQLSME NMLIYLASRV SDSKHGMMKF REERNLLGLG
LSTGFHDRYF ILNNSCLRLY KEVRSHRPEK EWPVKNLKVY LGIKKKLRPP SCWGFTVFYE
NEKHEKQQW
//