ID A0A3B3QYV4_9TELE Unreviewed; 902 AA.
AC A0A3B3QYV4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Disks large homolog 1 {ECO:0000256|ARBA:ARBA00044189};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000010631.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000010631.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A3B3QYV4; -.
DR Ensembl; ENSPKIT00000034765.1; ENSPKIP00000010631.1; ENSPKIG00000025230.1.
DR GeneTree; ENSGT00940000164867; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0031594; C:neuromuscular junction; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd12031; SH3_DLG1; 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; 1.
DR InterPro; IPR019583; DLG1-4_PDZ_assoc.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
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:SF5; DISKS LARGE HOMOLOG 1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM01277; MAGUK_N_PEST; 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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 227..314
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 322..409
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 478..559
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 593..663
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 712..887
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 90..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 100107 MW; A1BABAB47FBC4A68 CRC64;
MPVRKRDAER ALVLLEEYRR KLSQTEDRQL RHSVDRVIDI FQSNLFQALI DIQEFYEVTL
LDSEKCVESP KPAEPTASVN LWDFSSLQST TVTSETQPSS ISTSIEKYRH QDEDTPPPEQ
SSPTPPGEPQ GPELVQVSEK NISQIENVHG FVSHSHISPM KVESLECIFD GPSALGVEEI
PTSAYSTLYS QSDVLLQANP PPVLVNTDSL DSPSYVNGTE ADYEYEEITL ERGNSGLGFS
IAGGTDNPHI GEDPSIFITK VIPGGAAAQD GRLRVNDCIL RVNDVDVRDV THSKAVEALK
EAGSIVRLYV RRRKPHSEKV MEIKLVKGPK GLGFSIAGGV GNQHIPGDNS IYVTKIIEGG
AAHKDGKLQI GDKLLAVNST PLEEVSHEDA VTALKNTPDV VYLKVAKPTS VFMNDGFAPP
DITASYSQHV ENHVSPPAYL GQPVVTNTTS TTSTMGRCSP TPPKALAGEE DLTREPRKVV
LHRGTTGLGF NIVGGEDGEG IFISFILAGG PADLCGELRK GDRIVSVNGV DLRSATHEQA
AAALKNAGQT VTIVAQYRPE EYSRFEAKIH DLREQMMNSS ISSGSGSLRT NQKRSLYVRA
LFDYDKTKDS GLPSQGLDFK FGDILHVVNA SDDEWWQARQ VTPDGEVEEI GVIPSKRRVE
KKERARLKTV KFNSKSRDKA EIPDDLGSKG LSGQEEYILS YEPVTQQEVN YTRPVIILGP
MKDRINDDLI SEFPDKFGSC VPHTTRPKRE YEVDGRDYHF VALREQMEKD IQDHKFIEAG
QYNNHLYGTS VQSVREVAEK GKHCILDVSG NAIKRLQNAQ LYPIAVFIKP KSVENIMEMN
KRLTEEQGKK TFDRAMKLEQ EFMEYFTAII QGDTLEEIYE QVKQVMEEHS GPYIWVPAKE
KL
//
