ID A0A1S3J1L7_LINUN Unreviewed; 892 AA.
AC A0A1S3J1L7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Disks large 1 tumor suppressor protein isoform X3 {ECO:0000313|RefSeq:XP_013404156.1};
GN Name=LOC106169289 {ECO:0000313|RefSeq:XP_013404156.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013404156.1};
RN [1] {ECO:0000313|RefSeq:XP_013404156.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013404156.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR RefSeq; XP_013404156.1; XM_013548702.1.
DR AlphaFoldDB; A0A1S3J1L7; -.
DR EnsemblMetazoa; XM_013548702.1; XP_013404156.1; LOC106169289.
DR GeneID; 106169289; -.
DR OrthoDB; 2879721at2759; -.
DR Proteomes; UP000085678; Unplaced.
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; 1.
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:UP000085678};
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 188..275
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 284..371
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 443..524
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 554..624
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 702..877
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 78..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 98783 MW; B9FA8359DCB3AE64 CRC64;
MPVRRQDAHR ALELLEEYHK KLSKPSDGPL RTAIERVIRI FKSRLFQALL DIQEFYESTL
LDDGKSVHQK TLETLQVASK WESSPPLSNN TYLDKRDEEL PPPPPELMQN KSSPTKEQKP
PAAVITTTTT TTTTVTPATV KQPSPPLQRQ PVPESPPPPS PPEPQAAELE ASETQHMNGD
GIEWEYEEIA LERGGAGLGF SIAGGTDNPH IDDDPGIFIT KIIPGGAAAA DGRLRINDIV
VKVNQTSVLE VPHADAVDAL KKAGNSVTLL VRRQNNPPLE NIVELELVKG NKGLGFSIAG
GRGNQHIPGD NGIFVTKIIE GGASQQDGRL QVGDRLIAVN DVNLENVTHE DAVAALKATQ
ERVVLTVGKP TYLQNADFTD MGHSPQSSPT PDTVQIVQKP PPSPKHQPPP AVTVTSNSMQ
QMTSTPKPTP QVVDEDIPRE PRKVTLKKGS SGLGFNIVGG EDGEGIYVSF ILAGGPADLS
GELKRGDQLI SVNGVDLRDA THEQAAAALK HAGDTVEIVA QYKPEDYNRF EAKIHEIREQ
MLNTSQSSLK TTQKRTLYVR ALFDYDPSKD SGLPREGLEF RYGDILHVTN ASDDEWWQAK
RILPDGKEEG LGIIPSRRRV ERKERAKVKR VDFKGKGVDS KAVGGTAADK QKKKNFSFTK
KFPFMKSKDK SGTSMEDVTV DERGDEPVLT YEPVIQQELK VTRPIILLGP LKDRINDDLI
SEYPDKFGSC VPHTTRPRRD YEVDGRDYHF VDSREQMEKD IQDHLFIEAG QYNEHLYGTS
VASVREVAEK GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP RSAESIMEWN KRMTEEQAKK
SFEKALRLEQ EFGEYFTAVV SGDTPDDIYA KVKEVIRDQS GPMIWVPSKE KL
//
