ID A0A452IEA0_9SAUR Unreviewed; 945 AA.
AC A0A452IEA0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000025810.1};
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:ENSGAGP00000025810.1, 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:ENSGAGP00000025810.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SH3PXD2 family.
CC {ECO:0000256|ARBA:ARBA00009628}.
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DR AlphaFoldDB; A0A452IEA0; -.
DR STRING; 38772.ENSGAGP00000025810; -.
DR Ensembl; ENSGAGT00000029361.1; ENSGAGP00000025810.1; ENSGAGG00000018846.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IEA:InterPro.
DR CDD; cd06888; PX_FISH; 1.
DR CDD; cd12075; SH3_Tks4_1; 1.
DR CDD; cd12018; SH3_Tks4_4; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037961; SH3PXD2_PX.
DR InterPro; IPR035477; SH3PXD2B_SH3_1.
DR InterPro; IPR035480; SH3PXD2B_SH3_4.
DR PANTHER; PTHR15706:SF2; BUD EMERGENCE PROTEIN 1; 1.
DR PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00498; P47PHOX.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..128
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 163..222
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 260..319
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 407..466
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 884..945
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 325..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 106514 MW; 183FB1ACB3904C69 CRC64;
MPRRSILEVK VLDVQKRRTP NKHYVYIIKV MWSSGSTEVI YRRYSKFFDL QMQMLDKFPM
EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLIPIDEY CKALIQLPPY ISQCEEVLQF
FETRPEDLNP PKEEPIGKKK SGFIQRTASF LQRGGDLASV DPMVLEQYVV VADYQKQESS
EISLCVGQVV DIIEKNESGW WFVSTSDEQG WVPATCLEAQ DGVQDEFSMQ PEEVPWRYWS
LPRHVGRRRT LGDLYTSGWG QEEKYTVIYP YTARDEDEMN LDKGDVVEVI QKNLEGWWKI
RYQGQEGWAP ASYLKKGTGE MFTQKLGSGS STHSCALDLD GVPRQQNSTG REKDGPNNQR
EGRFDGRPLP QADIRRKSPK MRQRPPPRRD LTIPRGLNLP KPPVPPQVEE EYYTIADFQT
IIPDGISFHA GMKVEVIEKN LSGWWYIQIE EKEGWAPATF IDKYKKTSNA SRPNFLAPLP
NEMAQLQLGE ATAERNTNEE ATGPSRPLPE APPNGIDCGM KWAKDWKGKE ALKSAPSESG
DVAAGYEEIS DPDTEEKPSL PPRKESIIKS EGELTERQRP PPKPPGMILP MIPPKQTAAP
RDSKKPELKT EKGKLFQLKN EMGLECGHKV SAKEVKKPNL RPTVKPAKPK AEPPEDKSEP
MTQNPFLKSK PQIRPKPTAA SRTDPPQADD KLDIGNLRSK LRPAKSQEKP SEQDPMPTEN
VFNNNVLPAE VSGRPQERLS VENRPPTKQD SQIPKEAPTR APFSLPKMAD SEPKNSSPTP
REPPLQRPVV PPRRPPPPKK VVSSSSGPTA ELKAPQREVP EIRAASVPGR PMLVPPKAKP
FLPAMCQDEA KGKSSLGPKV TSKQVERGEA RERTAAPFTS PDISKEALYV AVADFEGDEE
TSSFKEGTLF EVREKNSSGW WFCKVLTGGP CWEGWIPSNY LRKKP
//
