ID A0A452IDA5_9SAUR Unreviewed; 887 AA.
AC A0A452IDA5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000025824.1};
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:ENSGAGP00000025824.1, 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:ENSGAGP00000025824.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452IDA5; -.
DR Ensembl; ENSGAGT00000029375.1; ENSGAGP00000025824.1; ENSGAGG00000018846.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IEA:InterPro.
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; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..98
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 133..192
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 202..261
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 349..408
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 826..887
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 267..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 99469 MW; 30602DEF193BA7EB CRC64;
MWSSGSTEVI YRRYSKFFDL QMQMLDKFPM EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA
VKRLIPIDEY CKALIQLPPY ISQCEEVLQF FETRPEDLNP PKEEPIGKKK SGFIQRTASF
LQRGGDLASV DPMVLEQYVV VADYQKQESS EISLCVGQVV DIIEKNESGW WFVSTSDEQG
WVPATCLEAQ DGVQDEFSMQ PEEEEKYTVI YPYTARDEDE MNLDKGDVVE VIQKNLEGWW
KIRYQGQEGW APASYLKKGT GEMFTQKLGS GSSTHSCALD LDGVPRQQNS TGREKDGPNN
QREGRFDGRP LPQADIRRKS PKMRQRPPPR RDLTIPRGLN LPKPPVPPQV EEEYYTIADF
QTIIPDGISF HAGMKVEVIE KNLSGWWYIQ IEEKEGWAPA TFIDKYKKTS NASRPNFLAP
LPNEMAQLQL GEATAERNTN EEATGPSRPL PEAPPNGIDC GMKWAKDWKG KEALKSAPSE
SGDVAAGYEE ISDPDTEEKP SLPPRKESII KSEGELTERQ RPPPKPPGMI LPMIPPKQTA
APRDSKKPEL KTEKGKLFQL KNEMGLECGH KVSAKEVKKP NLRPTVKPAK PKAEPPEDKS
EPMTQNPFLK SKPQIRPKPT AASRTDPPQA DDKLDIGNLR SKLRPAKSQE KPSEQDPMPT
ENVFNNNVLP AEVSGRPQER LSVENRPPTK QDSQIPKEAP TRAPFSLPKM ADSEPKNSSP
TPREPPLQRP VVPPRRPPPP KKVVSSSSGP TAELKAPQRE VPEIRAASVP GRPMLVPPKA
KPFLPAMCQD EAKGKSSLGP KVTSKQVERG EARERTAAPF TSPDISKEAL YVAVADFEGD
EETSSFKEGT LFEVREKNSS GWWFCKVLTG GPCWEGWIPS NYLRKKP
//
