ID A0A194PH93_PAPXU Unreviewed; 879 AA.
AC A0A194PH93;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Disks large 1 tumor suppressor protein {ECO:0000313|EMBL:KPI92776.1};
GN ORFNames=RR46_13997 {ECO:0000313|EMBL:KPI92776.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI92776.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI92776.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI92776.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI92776.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR EMBL; KQ459603; KPI92776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PH93; -.
DR STRING; 66420.A0A194PH93; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0031594; C:neuromuscular junction; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd11861; SH3_DLG-like; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF51; DISKS LARGE 1 TUMOR SUPPRESSOR PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 3.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 173..260
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 278..370
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 406..487
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 512..581
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 689..864
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 92..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 98217 MW; 3E26031E42C3B170 CRC64;
MPVRKQEAHR ALELLEDYHS KLVKPQDRQL RLAIERVIRI FKSRLFQALL DIQEFYELTL
LDDNKSVQQK TAETIRIANK WEADGTRREI HTDEGDYRSV SNAFLQDSNR KEEHRNDDTP
DSGKMGTTPM LSPCGDNEEK KAHVPTPEMK QINGIEGGGT DRTVGEDGFL YLTVALSRAG
GAGLGFSIAG GSDNPHVAED SLIYVTKLIP GGAAAASQLQ INDAILQVND TNVENVTHAE
AVDALKKAGN TVRLKIRRRT AENTLTVPSI TNKEEAVEIE LVKGGSGLGF SIAGGVGNQH
IPGDNGIYVT KIMAGGAAHR DGRLRVGDKL LMVKNTSKGD VNLDNVTHEE AVSALKASGE
RVLLVLVPGP RHGQPSPRTS RANTPSSTAN SLRREDVTDG TEEPRVVELE KGPQGLGFNI
VGGEDGHGIY VSFLLAGGPA EKSGELRRGD RLLAVNDIDI THATHEQAAK ALKGTGQNVK
LTVVYRPQEY NKFEARINEL KQHHTLLRTS QKRSLYVRAL FDYDPVRDDG LPSRGLPFRY
GDILHVTNAS DDEWWQARRI DTTEADAIGI IPSKRRWERK QRARDRQVKF QGQGTPSQST
LERKKKTLSF SRKFPFMKSR EDGKSEDGSD QEPFMLCYTQ EDTNADGEIL YRVELPMMEE
ITLIYLEDES QDENVLSYET VQQLTIAYTR PVIILGPLKD RINDDLISEF PDKFGSCVPH
TTRPRRDYEV DGRDYHFVSS REQMERDIQN HLFIEAGQYN DNLYGTSVAS VREVAEKGKH
CILDVSGNAI KRLQVAQLYP IAIFIKPKSV ESIMEMNKRM TEDQAKKTYE RALKMEQEFA
EYFTAVVTGD TPEEIYAKVK AVITAESGPT VWVPRREPL
//
